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Human Metabolome Database Version 2.5

 

Showing metabocard for Hydrogen (HMDB01362)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-16 14:52:05
Update Date 2008-12-14 02:58:38
Accession Number HMDB01362
Secondary Accession Numbers Not Available
Common Name Hydrogen
Description Hydrogen is a colorless, odorless, nonmetallic, tasteless, highly flammable diatomic gas with the molecular formula H2. With an atomic weight of 1.00794, hydrogen is the lightest element. Besides the common H1 isotope, hydrogen exists as the stable isotope Deuterium and the unstable, radioactive isotope Tritium. Hydrogen is the most abundant of the chemical elements, constituting roughly 75% of the universe's elemental mass. Hydrogen can form compounds with most elements and is present in water and most organic compounds. It plays a particularly important role in acid-base chemistry, in which many reactions involve the exchange of protons between soluble molecules. Oxidation of hydrogen, in the sense of removing its electron, formally gives H+, containing no electrons and a nucleus which is usually composed of one proton. That is why H+ is often called a proton. This species is central to discussion of acids. Under the Bronsted-Lowry theory, acids are proton donors, while bases are proton acceptors. A bare proton H+ cannot exist in solution because of its strong tendency to attach itself to atoms or molecules with electrons. However, the term 'proton' is used loosely to refer to positively charged or cationic hydrogen, denoted H+. H2 is a product of some types of anaerobic metabolism and is produced by several microorganisms, usually via reactions catalyzed by iron- or nickel-containing enzymes called hydrogenases. These enzymes catalyze the reversible redox reaction between H2 and its component two protons and two electrons. Creation of hydrogen gas occurs in the transfer of reducing equivalents produced during pyruvate fermentation to water.
Synonyms
  1. Hydrogen cation
  2. Proton
  3. Hydrogen
  4. Dihydrogen
  5. Hydrogen gas
  6. Hydronium
  7. Hydrogen ion
Chemical IUPAC Name hydrogen
Chemical Formula H2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Inorganic
Super Class
  • Inorganic compounds
Class
  • Inorganic Ions and Gases
Sub Class
  • Gases
Family
  • Microbial Metabolite
Species
—
Biofunction
  • Osmolyte, enzyme cofactor, signalling
Application
—
Source
  • Endogenous
Average Molecular Weight 2.016
Monoisotopic Molecular Weight 2.015650
Isomeric SMILES [H][H]
Canonical SMILES [H][H]
KEGG Compound ID C00282 Link Image
BioCyc ID ALPHA-GLUCOSE-16-BISPHOSPHATE Link Image
BiGG ID 33778 Link Image
Wikipedia Link Hydrogen Link Image
NuGOwiki Link HMDB01362 Link Image
Metagene Link HMDB01362 Link Image
METLIN ID Not Available
PubChem Compound 5362549 Link Image
PubChem Substance 8146671 Link Image
ChEBI ID 29235 Link Image
CAS Registry Number 1333-74-0
InChI Identifier InChI=1/H2/h1H
Synthesis Reference Ait-Ichou, I.; Formenti, M.; Pommier, B.; Teichner, S. J. Photocatalytic dehydrogenation of isopropanol on platinum/titania catalysts. Journal of Catalysis (1985), 91(2), 293-307.
Melting Point (Experimental) -259.2 oC
Experimental Water Solubility 0.00162 mg/mL at 21 oC [VENABLE,CS & FUWA,T (1922)] Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Physiological Charge 0
State Liquid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0 [Predicted by PubChem via XLOGP]; 0.45 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
  • golgi apparatus
  • lysosome
  • mitochondria
  • nucleus
  • peroxisome
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Carnitine Synthesis SMP00465 Link Image
Catecholamine Biosynthesis SMP00012 Link Image map00350 Link Image
Degradation of Superoxides SMP00468 Link Image
Ethanol Degradation SMP00449 Link Image
Homocysteine Degradation SMP00455 Link Image
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids SMP00482 Link Image
Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids SMP00481 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
Mitochondrial Electron Transport Chain SMP00355 Link Image map00190 Link Image
Plasmalogen Synthesis SMP00479 Link Image
Pyruvaldehyde Degradation SMP00459 Link Image
Threonine and 2-Oxobutanoate Degradation SMP00452 Link Image
Transfer of Acetyl Groups into Mitochondria SMP00466 Link Image
Trehalose Degradation SMP00467 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Hydrogenase
  2. [Fe] hydrogenase
  3. [Fe] hydrogenase
  4. Iron hydrogenase
  5. Hydrogenase-1 small chain
  6. Hydrogenase-1 large chain
  7. Hydrogenase-2 large chain
  8. Hydrogenase-2 small chain
  9. Hydrogenase 1, small subunit
  10. Hydrogenase 1, large subunit
  11. Hydrogenase 2, large subunit
  12. Hydrogenase 2, small subunit
  13. Voltage-gated hydrogen channel 1
Enzyme 1 [top]
Enzyme 1 ID 15964
Enzyme 1 Name Hydrogenase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name hydA
Enzyme 1 Protein Sequence >Hydrogenase 
MTFMIINIDKDLCTGCRECSKVCPVNAIEGEEGKPQEINLDRCVMCGQCVQTCKSYASVI
DEGFEFLQEKKQEREIPESINEPIFAAYNVCDIDKVKKALSDPNVFTMVQCAPAVRVALG
EDFGYYLGYLGAGKMAAALRALNFDRVYDTNFAADLTIMEEGSELIKRVTEGGTLPMFTS
CCPAWVKFMEKNYPKLTNHLSSCKSPQQMGGAIFKTYGAEINNVDASKIFSVSIMPCTCK
KYECDREEMDSSGYRDVDVVLTTRELAYLIKDMGIDFKNLREEKFDSPLGSYSGAGTIFG
VTGGVMEAAIRTGYELITGESIPDVEVKQVRGENGFRKSTIKIGDLDLRVGVVSGLKNVI
PVLEDLEKGKLDVDFIEVMTCPVGCVSGGGQPKILLEEYKELAYENRTKATYVHDEHLAI
RKSHENPDIKKLYDEYLVEPLGEKSHHLLHTTYCIGKEVAK
Enzyme 1 Number of Residues 461
Enzyme 1 Molecular Weight 51231.4
Enzyme 1 Theoretical pI 4.81
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ferredoxin hydrogenase activity
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in electron carrier activity
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+ [RN:R00019]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 115249314 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q180F8 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name Q180F8_CLOD6 Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1386 bp 
ATGGATAATTTAAATAAAAAGTTTTTGATGGAATATATAGATGAGATACAGGGAGAATTA
AGAGATATATCAGATAAGATATGGAAAAATCCAGAACTTCAGTATAAAGAATACTATGCT
TCAAATTTACAAAAAGAATGTTTAAAAAAACATGGTTTTAGTATAGAGGGATTAGAAGAT
ATGGATACAGCATTTGTGGCTAGTTATGGAGAAGGTAGACCAGTTATAGCAGTTTTGGGA
GAATATGATGCTTTAGATGGTTTGTCTCAAAAAGTATCTACTACTAAAGAACCTATTGTA
GATGGTGGTGCAGGTCATGGATGTGGACATAACTTACTTGGTACAGGTTCAATAGGAGCT
GTAATTGCAGTAAAGGAATTAATCAAACTAAAAAAGCTGAAAGGGACTATAAAATACTAT
GGATGTCCAGCAGAAGAAGATTTATCTGGAAAAGTATTGATGATAAAAAAAGGTTTTTTT
GATGGAATTGATTGTGCTTTTAGTTGGCATCCATTTGATATAAATACTCCTATAAGAATC
CCAACACTTGCTAATTACTCTGTGAAATTTAGATATAATGGGATTAGTGCTCATGCAGCA
CAAGCTCCTTATAACGGAAGAAGTGCACTTGATGCAGTAGAACTTATGAATATAGGTTGT
AATTATTTGAGAGAACATATATTTGATAGTTGTAGAGTACACTATGTAACTACTAATGGT
GGAAAAATGCCAAATATAGTTCCAGATTTTGCAGAAGTGTGGTATTACATAAGAGGAGTT
AAAATGGAGCATGTAAGAGATGTATTTGGTAGGATTGTTGATATAGCAAAAGGAGCAGCA
TTAATGACTGGTACTAGTATGGAATATGATATTATAAGTGGAGTATATGACTATATTCCA
AATACAATATTAACAGATATTCTATCACAAAATATGAAATTAGTAGGTGTGCAAAACTAT
AATGAAAATGACTACTACTTTGCAGATAAATTAGCTGAGACAGTGTCTATAGATAAAAGA
AGTAGTGTTTCTAGTGTCTTAAGTGGAAATAAGGATATTACTAAGATGAATTTACATGAT
GAGGTTACAGATGATACATTTACTCATAATAACTGTATATCATTATCATTGGATATTGGA
GATGTTAGTTACATAATTCCTACAGCACAGTGTTCTTGTTCAGTTTGGCCTATTGGTATT
TCTGCCCATACATGGCAATCTTGTGCCAGTGCAGGTTCTGATATGGGATTTAAGGCAATG
TTATTGGCATCTAAATCTATATCATGTTCAATAAATGATGTAATGCTTGATGAATTGGTT
ATAAATAAAGCAAAAAAAGAATTGAAGGATACTGTAGGTAGTTTTAAATATATACCAATT
ATTTAA
Enzyme 1 GenBank Gene ID AM180355 Link Image
Enzyme 1 GeneCard ID hydA Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus CD3314
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Sebaihia M, Wren BW, Mullany P, Fairweather NF, Minton N, Stabler R, Thomson NR, Roberts AP, Cerdeno-Tarraga AM, Wang H, Holden MT, Wright A, Churcher C, Quail MA, Baker S, Bason N, Brooks K, Chillingworth T, Cronin A, Davis P, Dowd L, Fraser A, Feltwell T, Hance Z, Holroyd S, Jagels K, Moule S, Mungall K, Price C, Rabbinowitsch E, Sharp S, Simmonds M, Stevens K, Unwin L, Whithead S, Dupuy B, Dougan G, Barrell B, Parkhill J: The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat Genet. 2006 Jul;38(7):779-86. Epub 2006 Jun 25. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 15965
Enzyme 2 Name [Fe] hydrogenase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name Not Available
Enzyme 2 Protein Sequence >[Fe] hydrogenase 
MNKKYDSLFKELISSYYSEDNFDEKLNDIVKNNFNSKEDAIDVLSSLCGVDIDKNSDNIA
YDIRKAITTQKIKKNIVDKVSVCTKNCSKESKGKCQSLCPFDAILTDPIDNSKYIDPNLC
QNCGICVQVCESGHFLDRIELLPIIDLIKNNETVIAAVAPAIAGQFGENVSLDMLREAFI
KIGFSDMIEVAFAADILSIKEAVEFNHHVEKTGDILITSCCCPMWVAMLRKCYKDLVKDV
SPSVSPMIAAGRVIKKLNKDAKVVFIGPCIAKKAEAREKDLVGDIDYVLTFEELKGIFEA
LKIDLSSMKGVPSIEYTSRGGRLYARTGGVSEAINDVVKELYPDKAKIFKAVQANGVKEC
KELLNKVQSGELKANFIEGMGCVGGCVGGPKRIVDPSIGKKHVDEVAYNSPIKVATHSHT
MDEVLLRLGINSLKSFEDKEKISIFEREF
Enzyme 2 Number of Residues 449
Enzyme 2 Molecular Weight 49626.9
Enzyme 2 Theoretical pI 6.04
Enzyme 2 GO Classification
Function
  • binding
  • electron carrier activity
  • iron-sulfur cluster binding
  • metal cluster binding
Process
—
Component
—
Enzyme 2 General Function Involved in electron carrier activity
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+ [RN:R00019]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 110683143 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q0SWA8 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q0SWA8_CLOPS Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1350 bp 
ATGAATAAAAAGTATGACTCTTTATTTAAAGAACTTATATCTTCATATTATTCAGAAGAT
AACTTTGATGAAAAATTAAATGATATAGTAAAAAATAATTTTAATAGTAAAGAAGATGCT
ATTGATGTTCTTTCATCCCTATGTGGAGTTGATATAGATAAAAACTCAGATAATATTGCT
TATGACATAAGAAAAGCTATAACAACACAAAAAATCAAAAAAAATATAGTTGATAAAGTT
TCTGTATGTACAAAAAACTGTTCAAAAGAAAGTAAAGGTAAATGTCAAAGCCTTTGTCCC
TTTGATGCAATACTGACTGATCCTATAGATAATAGTAAATATATAGATCCAAATCTATGT
CAAAATTGTGGTATATGTGTTCAGGTATGCGAAAGTGGTCACTTCTTAGATAGAATTGAA
CTTCTTCCTATTATTGATTTAATAAAAAATAATGAGACTGTAATTGCCGCGGTAGCTCCT
GCTATAGCTGGACAATTTGGTGAAAATGTCTCCTTAGATATGCTAAGAGAAGCATTTATA
AAAATAGGCTTCTCAGATATGATTGAAGTTGCATTTGCCGCTGATATACTTTCAATTAAA
GAAGCTGTTGAATTTAATCATCATGTAGAAAAAACTGGAGATATATTAATAACATCTTGC
TGTTGCCCTATGTGGGTGGCCATGTTAAGAAAGTGTTATAAGGATTTAGTAAAGGATGTC
TCCCCTTCTGTTTCACCTATGATAGCTGCTGGGAGAGTAATAAAAAAATTAAATAAAGAT
GCTAAGGTAGTTTTTATAGGTCCCTGTATAGCTAAGAAAGCTGAAGCAAGAGAAAAAGAC
TTAGTTGGTGACATAGATTATGTCTTAACTTTTGAAGAATTAAAGGGCATATTTGAAGCA
TTAAAAATAGATCTATCATCTATGAAAGGTGTTCCCTCTATAGAATACACCTCTAGAGGT
GGAAGGCTTTACGCTCGAACTGGAGGGGTATCAGAGGCCATAAATGATGTGGTTAAAGAA
CTCTATCCTGATAAAGCTAAGATATTTAAGGCAGTTCAAGCTAATGGAGTTAAAGAATGT
AAAGAACTCTTAAATAAAGTTCAATCTGGTGAATTAAAAGCAAACTTTATTGAAGGTATG
GGATGTGTTGGAGGATGCGTTGGTGGTCCCAAAAGAATAGTAGATCCTAGCATAGGTAAA
AAACACGTTGATGAAGTTGCTTATAATTCTCCAATAAAAGTTGCTACTCATAGCCATACT
ATGGATGAAGTCCTATTAAGATTAGGAATAAATTCATTAAAGTCTTTTGAGGATAAAGAA
AAAATATCTATTTTTGAAAGAGAATTCTAA
Enzyme 2 GenBank Gene ID CP000312 Link Image
Enzyme 2 GeneCard ID Not Available
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus CPR_0261
Enzyme 2 SNPs Not Available
Enzyme 2 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15966
Enzyme 3 Name [Fe] hydrogenase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >[Fe] hydrogenase 
MSKHLATTIRVAIEKDNPSICRDEEKCIKCGSCKNICTDYIGVNGHYSLEKTNDIAVCIN
CGQCANVCPTSSITEVFDYKKVEDAINDKDKIVIVSTSPAVRVSLGEEFNMDDGSFVQGK
MIALLRKLGFKYVLDTNFAADMTIVEEASELVERITKNNKPLPQFTSCCPAWIKYAETFH
PEILDHISTSKSPIGMQGPTIKTYFAKNMGIDPSKIINVALTPCTAKKFEIKREEMNASG
RYYGIEDMRDMDYVITTREVAIWAKEKGIDFNSLEDSNFDKLMGEASGAGVIFANTGGVM
EAALRTAYKYITKKEPPKDFYDLEAVRGMEDIREASFKINDLDINVAVIYGTENASKFIS
KMKDSDKKYHFVEVMTCPGGCIGGGGQPKDKNLQGDKLREKRIDGLYRRDSSMKLKVSCE
NEEIKNLYKEFYGKPLSDLAEKMLHTTYSDRSSDLGGENMSESVKYRCTVCGYIQEGELP
EGFICPVCKSPASVFVKVEEKTEVDDKEDNKSKSTNESSNKYKGTKTEKNLMDALAGESI
ARNKYTFFADVAKNEGYEQIYKLFLKTAGNEREHAKLWFKELGYLGDTQENLLHGSEGEH
YEWSDMYARFAKEAEEEGFFDLAEKFVEVAKIEKSHEDRYRKLLNNIKMKKVFEKSEETM
WECLNCGYLVMGKKAPEVCPVCNYAEGFFEVRAENY
Enzyme 3 Number of Residues 696
Enzyme 3 Molecular Weight 78665.8
Enzyme 3 Theoretical pI 5.19
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ferredoxin hydrogenase activity
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 3 General Function Involved in electron carrier activity
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+ [RN:R00019]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 110682790 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q0SUE5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q0SUE5_CLOPS Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2091 bp 
ATGAAGGAGTATAAAATTGAGAATTTAAGAAATATAGGTATTATAGGACATAGTGATTCA
GGTAAAACTGCATTATCAGAAGCTTTACTTTATTATACAAAAACTACTGATAGATTAGGA
ACTTGTGAAGATGGAAATACAATAAGTGATTATGATCAAGAAGAGAAAAAAAGAAAGATA
TCACTAGCCTTATCTATTATTCCTTTTGAATATGATGGAACTAAGATTAATATATTGGAT
ACTCCAGGTTATTTTGATTTTGTTGGAGAGCAAATAGAAGGTGTTAAGGCTGCTGACTCT
GCAATTATAACTGTATGCGGAGTGACTGGAGTTCAAGTTGGAACTGAAAAAGCCTGGGAA
TGCTGTGAAAAAGAAAAATTACCAAGAGCCTTTTTTATAAATAAATTAGATAGAGAAAAC
TCAAATTTTGATAAGGTATTAGAAAATATAAGAAATATTTTTGGAAACAAAGTAATTCCT
ACTCAATATCCATTAGGAAAAGAAAAGGAGTTTAAGGGAATTGTAAATCTTATAACTGAA
AAAGCTTTTGAGTATGATAAAAAATCAGGAAAAATAAATAAGATAGAAATACCTAATGAA
GTAAAAGATAAGGTCAATGAGTATAGAACTTATTTAATGGAATCTGTAGCTGAAACTGAT
GAGGAATTACTTGATAAATATTTATCTGAAGGAGAGCTTACAGTAGATGAAATCTATAAA
GGACTTTCTATTGGATTTGAAGAAGGAGATATAGCTCCAGTTATGTGTGGAAGTTCAGTA
TCAATAGTTGGTATGAAAAGCCTATTAGATTCAATTAAAGGATATTTCCCATCACCATAT
ATAAGCAAAGCTAAAGTTGCTATTGATAGCAATAATAAAGAAATATTAGTTAAGTCAAAT
AAAGATATGCCATTTTCTGCATTTGTATTTAAAACAATTGCTGATCCTTTTGTAGGAAAG
CTTTCAATATTTAAGGTGCAAACAGGAGAGCTAACAACTGATAAGATAATTATAAATTCA
AAAAATAATAAGATAGAAAAAGTTAGTTCCTTATGCTTTTTAAGAGGTAAAAATCAAATA
CAAACAAATAAAATAGGTGCTGGAGATATAGGAGCTATTACAAAACTTCAATATACTTCA
ACTGGTGATACTCTTTGTGAAAGTAACTTTAAGATTGCTTATGAAGAATTTGAGTTTCCA
GAGGCAGTTATGACTATGGCAGTATTACCAAAAAGTAAATGTGATGAAGAAAAAATTTCT
CAAGGACTTTCTAAACTTCTAGATGAAGATCCAACATTTAAGGTTTCTAGAGATCAAGAA
AATGCAGAAACCTTAGTTTCTGGTATTGGAGAGACACATGTAGAGGTTTTAGCTAGTAAA
TTAAAGAGTAAATTTGGAATTGATGTAATTCTTCAAGATCCTAAGATTCCCTATAGAGAA
ACTATAAAAGGTAGTTCTGATGTACAAGGAAAGCATAAAAAACAATCTGGAGGCCATGGT
CAATATGGAGATGTAAAAATTAAATTTGAGCCTAGAAGAGACGGTGAGCTTGATTTAGAA
TTTGTGGATAAGGTTGTTGGAGGAGTTGTGCCTAGAAACTATATACCAGCAGTAGAAAAA
GGATTAAGAGATTGTTTAAAGAAAGGGGTTTTAGCAGGTTATCCTGTAATAGGAATTAAG
GCTACATTACATGATGGATCATATCACCCTGTAGATTCATCAGAAATGGCATTTAAGGTA
GCTGCTTCATTAGCATATAAGAAAGGTATGGAGAATGCAAAACCTGTTATATTAGAGCCT
ATTATGAAGGTAAAAATAATAATTCCAGATGAATACATGGGAGATATAATTAGTGATATA
AATAAGAAAAGAGGAAGAGTAATTGGAATGGAACCAGAAGGTAATAATGAAAAAGTTATA
GCTGATATTCCTTTATCAGAAATGTTTAAGTATGCTACTGATTTACGTTCAATGACTCAA
GGAAGAGGAAGCTTTAGCATGGAATTTGAAAAATATGAGGAAGTTCCAAGTACAGAGGTA
GATAAAATAATAGAAGATGCAAAGAAAATAAAAGAAGCTAAGGAAGCTTAA
Enzyme 3 GenBank Gene ID CP000312 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus CPR_0938
Enzyme 3 SNPs Not Available
Enzyme 3 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15967
Enzyme 4 Name Iron hydrogenase
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name hydA
Enzyme 4 Protein Sequence >Iron hydrogenase 
MNKIIINDKTIEFDGDKTILDLARENGFDIPVLCELKNCGNKGQCGVCLVEQEGNDRLLR
SCAIKAKDGMVIKTDSEKVLEARKERVAELLDEHEFKCGPCKRRENCEFLKLVIKTKARA
HKPFVVADKSEYVDDRSKSIVLDRSKCVKCGRCVAACRTRTATNSIKFHRIDGVRLVGPE
ELKCFDDTNCLLCGQCVAACPVDALSEKSHIERVQDALNDPEKHVIVAIAPAVRTSMGEL
FKMGYGQDVTGKLYTALRKLGFDKVFDINFGADMTIMEEATELIERIKNNGPFPMLTSCC
PSWVREVENYFPELVENLSTAKSPQQIFGSASKTYYPQVADIDPKKVFTVTVMPCTSKKF
EADRPEMENEGIRNIDAVITTRELARMIKAAKIDFAKLEDSEVDPAMGEYTGAGVIFGAT
GGVMEAALRTAKDFMENDNLDNVDYEAVRGLAGIKEAEVEIAGNEYKLAVVNGAANVFEL
VKSGKINDYHFIEVMACPGGCVNGGGQPHISAEDSDKIDIREVRASVLYNQDKNLEKRKS
HQNSALLKMYENYMGKPGHGRAHELLHMKYKK
Enzyme 4 Number of Residues 572
Enzyme 4 Molecular Weight 63587.4
Enzyme 4 Theoretical pI 6.31
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ferredoxin hydrogenase activity
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 4 General Function Involved in electron carrier activity
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+ [RN:R00019]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 110683869 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q0SQK1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q0SQK1_CLOPS Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1719 bp 
ATGAATAAAATAATAATCAATGATAAGACTATCGAATTTGATGGTGACAAGACGATACTT
GACTTAGCAAGAGAGAATGGGTTTGACATTCCAGTGCTTTGTGAGTTAAAAAATTGCGGA
AACAAAGGACAATGTGGAGTTTGTCTTGTTGAGCAAGAAGGAAATGATAGACTATTAAGA
TCTTGTGCAATAAAAGCTAAAGATGGAATGGTTATTAAAACTGATAGTGAAAAAGTACTA
GAAGCTAGAAAAGAAAGAGTTGCAGAACTTTTAGATGAGCATGAGTTCAAATGTGGACCA
TGTAAAAGAAGAGAGAATTGTGAATTCTTAAAACTTGTAATTAAAACAAAGGCAAGAGCT
CACAAACCATTTGTAGTTGCAGATAAATCAGAATATGTAGATGACAGAAGTAAATCAATA
GTTTTAGATAGAAGTAAATGTGTTAAATGTGGTAGATGTGTTGCTGCATGTAGAACAAGA
ACTGCTACTAACTCAATAAAATTCCACAGAATTGATGGAGTAAGATTAGTAGGACCAGAG
GAATTAAAATGTTTCGACGATACAAATTGTTTATTATGTGGACAATGTGTAGCTGCTTGT
CCAGTTGATGCATTATCAGAAAAATCACATATTGAAAGAGTTCAAGATGCATTAAATGAT
CCAGAAAAGCATGTAATAGTTGCTATAGCACCAGCTGTAAGAACATCAATGGGTGAATTA
TTCAAAATGGGTTACGGCCAAGATGTTACTGGAAAATTATATACTGCTTTAAGAAAACTA
GGTTTTGATAAAGTATTTGATATAAACTTCGGTGCTGATATGACAATAATGGAAGAAGCT
ACTGAGCTTATAGAAAGAATAAAAAATAATGGGCCTTTCCCAATGTTAACTTCATGTTGC
CCATCATGGGTTAGAGAAGTTGAAAACTACTTCCCAGAATTAGTAGAAAATCTTTCAACA
GCTAAGTCACCACAACAAATATTTGGTTCAGCATCAAAAACTTATTATCCTCAAGTTGCT
GATATAGATCCTAAAAAAGTATTTACAGTAACTGTAATGCCTTGTACTTCTAAAAAATTC
GAAGCTGATAGACCTGAAATGGAAAACGAAGGAATAAGAAATATAGATGCAGTTATAACA
ACTAGAGAGTTAGCTAGAATGATAAAGGCTGCTAAAATAGATTTTGCTAAATTAGAAGAC
AGTGAAGTAGATCCAGCTATGGGTGAGTATACTGGAGCAGGTGTTATATTTGGAGCTACT
GGTGGAGTTATGGAAGCTGCTTTAAGAACAGCTAAAGATTTCATGGAAAATGATAACTTA
GACAATGTAGATTATGAAGCTGTTAGAGGATTAGCTGGAATAAAAGAAGCTGAAGTAGAA
ATAGCAGGAAATGAATATAAATTAGCTGTTGTAAATGGAGCTGCTAATGTATTTGAATTA
GTTAAGTCTGGTAAAATAAATGATTACCACTTCATCGAAGTAATGGCATGTCCAGGTGGA
TGTGTTAACGGTGGGGGACAACCACATATCTCAGCTGAAGATAGTGATAAAATTGATATT
AGAGAAGTAAGAGCTTCTGTTCTTTACAATCAAGATAAGAATTTAGAGAAGAGAAAATCA
CATCAAAACTCAGCTTTATTAAAAATGTATGAAAACTACATGGGTAAACCAGGTCATGGA
AGAGCTCATGAGTTATTACACATGAAATATAAAAAATAA
Enzyme 4 GenBank Gene ID CP000312 Link Image
Enzyme 4 GeneCard ID hydA Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus CPR_2341
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15968
Enzyme 5 Name Hydrogenase-1 small chain
Enzyme 5 Synonyms
  1. HYD1
  2. Membrane-bound hydrogenase 1 small subunit
  3. NiFe hydrogenase
Enzyme 5 Gene Name hyaA
Enzyme 5 Protein Sequence >Hydrogenase-1 small chain 
MNNEETFYQAMRRQGVTRRSFLKYCSLAATSLGLGAGMAPKIAWALENKPRIPVVWIHGL
ECTCCTESFIRSAHPLAKDVILSLISLDYDDTLMAAAGTQAEEVFEDIITQYNGKYILAV
EGNPPLGEQGMFCISSGRPFIEKLKRAAAGASAIIAWGTCASWGCVQAARPNPTQATPID
KVITDKPIIKVPGCPPIPDVMSAIITYMVTFDRLPDVDRMGRPLMFYGQRIHDKCYRRAH
FDAGEFVQSWDDDAARKGYCLYKMGCKGPTTYNACSSTRWNDGVSFPIQSGHGCLGCAEN
GFWDRGSFYSRVVDIPQMGTHSTADTVGLTALGVVAAAVGVHAVASAVDQRRRHNQQPTE
TEHQPGNEDKQA
Enzyme 5 Number of Residues 372
Enzyme 5 Molecular Weight 40681.0
Enzyme 5 Theoretical pI 7.15
Enzyme 5 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • NADH dehydrogenase (quinone) activity
  • NADH dehydrogenase (ubiquinone) activity
  • NADH dehydrogenase activity
  • binding
  • catalytic activity
  • cofactor binding
  • ferredoxin hydrogenase activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • quinone binding
Process
  • metabolic process
  • oxidation reduction
Component
  • ferredoxin hydrogenase complex
  • macromolecular complex
  • protein complex
Enzyme 5 General Function Involved in NADH dehydrogenase (ubiquinone) activity
Enzyme 5 Specific Function This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • H2 + A = AH2 [RN:R07182]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-45
Enzyme 5 Transmembrane Regions
  • 326-348
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4062385 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P69739 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name MBHS_ECOLI Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1119 bp 
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG
Enzyme 5 GenBank Gene ID AP009048 Link Image
Enzyme 5 GeneCard ID hyaA Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus b0972
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Menon NK, Robbins J, Peck HD Jr, Chatelus CY, Choi ES, Przybyla AE: Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames. J Bacteriol. 1990 Apr;172(4):1969-77. [PubMed Link Image]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  4. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [PubMed Link Image]
  5. Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [PubMed Link Image]
  6. Tullman-Ercek D, DeLisa MP, Kawarasaki Y, Iranpour P, Ribnicky B, Palmer T, Georgiou G: Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides. J Biol Chem. 2007 Mar 16;282(11):8309-16. Epub 2007 Jan 11. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15969
Enzyme 6 Name Hydrogenase-1 large chain
Enzyme 6 Synonyms
  1. HYD1
  2. Membrane-bound hydrogenase 1 large subunit
  3. NiFe hydrogenase
Enzyme 6 Gene Name hyaB
Enzyme 6 Protein Sequence >Hydrogenase-1 large chain 
MSTQYETQGYTINNAGRRLVVDPITRIEGHMRCEVNINDQNVITNAVSCGTMFRGLEIIL
QGRDPRDAWAFVERICGVCTGVHALASVYAIEDAIGIKVPDNANIIRNIMLATLWCHDHL
VHFYQLAGMDWIDVLDALKADPRKTSELAQSLSSWPKSSPGYFFDVQNRLKKFVEGGQLG
IFRNGYWGHPQYKLPPEANLMGFAHYLEALDFQREIVKIHAVFGGKNPHPNWIVGGMPCA
INIDESGAVGAVNMERLNLVQSIITRTADFINNVMIPDALAIGQFNKPWSEIGTGLSDKC
VLSYGAFPDIANDFGEKSLLMPGGAVINGDFNNVLPVDLVDPQQVQEFVDHAWYRYPNDQ
VGRHPFDGITDPWYNPGDVKGSDTNIQQLNEQERYSWIKAPRWRGNAMEVGPLARTLIAY
HKGDAATVESVDRMMSALNLPLSGIQSTLGRILCRAHEAQWAAGKLQYFFDKLMTNLKNG
NLATASTEKWEPATWPTECRGVGFTEAPRGALGHWAAIRDGKIDLYQCVVPTTWNASPRD
PKGQIGAYEAALMNTKMAIPEQPLEILRTLHSFDPCLACSTHVLGDDGSELISVQVR
Enzyme 6 Number of Residues 597
Enzyme 6 Molecular Weight 66252.9
Enzyme 6 Theoretical pI 5.85
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ferredoxin hydrogenase activity
  • ion binding
  • metal ion binding
  • nickel ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 6 General Function Involved in ferredoxin hydrogenase activity
Enzyme 6 Specific Function This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • H2 + A = AH2 [RN:R07182]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 85674807 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P0ACD8 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name MBHL_ECOLI Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1794 bp 
ATGAGCACTCAGTACGAAACTCAGGGATACACCATCAATAATGCCGGACGCCGCCTGGTG
GTCGACCCGATTACGCGCATCGAAGGCCACATGCGCTGCGAAGTGAATATTAACGATCAG
AATGTGATCACCAATGCCGTCTCCTGCGGCACCATGTTTCGCGGGCTGGAGATCATCCTA
CAAGGGCGCGACCCGCGCGATGCGTGGGCGTTCGTTGAACGTATCTGCGGCGTCTGTACT
GGCGTACACGCCCTGGCTTCGGTTTACGCCATCGAAGATGCTATCGGTATTAAAGTGCCG
GACAACGCCAATATCATCCGCAACATTATGCTGGCAACGCTCTGGTGCCACGATCATCTG
GTGCACTTCTATCAGCTTGCCGGGATGGACTGGATCGATGTGTTAGATGCGCTGAAAGCC
GACCCGCGGAAAACCTCCGAACTGGCGCAAAGTCTCTCCTCTTGGCCGAAATCATCCCCT
GGCTATTTCTTCGACGTACAAAACCGCCTGAAAAAATTTGTTGAAGGCGGGCAGTTGGGG
ATCTTCCGCAATGGCTACTGGGGGCACCCGCAGTACAAACTGCCGCCAGAAGCTAACCTG
ATGGGCTTTGCCCACTATCTCGAAGCTCTCGATTTCCAGCGTGAAATTGTCAAAATCCAC
GCGGTCTTTGGCGGTAAAAACCCGCATCCAAACTGGATTGTCGGCGGGATGCCTTGCGCC
ATCAACATTGACGAAAGCGGCGCGGTCGGGGCAGTCAATATGGAACGCCTGAACCTGGTG
CAGTCAATTATCACCCGCACGGCGGACTTCATTAACAACGTGATGATCCCCGACGCCTTA
GCCATCGGTCAGTTCAACAAACCGTGGAGCGAAATCGGCACTGGTCTTTCTGATAAATGC
GTTCTCAGCTACGGCGCATTCCCGGATATTGCCAACGACTTTGGCGAGAAAAGTCTGCTG
ATGCCTGGCGGCGCGGTGATTAACGGCGACTTCAACAATGTGCTGCCAGTGGATTTGGTT
GATCCGCAGCAGGTGCAGGAGTTTGTCGACCACGCCTGGTATCGATATCCCAACGATCAG
GTCGGGCGTCATCCGTTCGATGGCATCACCGACCCGTGGTACAACCCCGGCGATGTCAAA
GGCAGCGATACCAACATTCAGCAGCTGAATGAACAGGAACGCTACTCGTGGATCAAAGCG
CCACGCTGGCGCGGTAACGCGATGGAAGTGGGGCCGCTGGCGCGCACGTTAATCGCTTAT
CACAAAGGCGATGCTGCGACCGTTGAGTCGGTCGATCGCATGATGTCGGCGTTGAACCTG
CCGCTTTCCGGTATCCAGTCAACGTTAGGCCGCATTTTGTGCCGCGCGCACGAAGCGCAG
TGGGCCGCAGGTAAGTTGCAGTATTTCTTCGACAAGCTGATGACCAACCTGAAAAACGGC
AATCTCGCCACTGCTTCCACGGAAAAATGGGAACCTGCAACCTGGCCGACAGAGTGCCGT
GGTGTCGGTTTTACCGAAGCGCCGCGCGGGGCGTTAGGCCACTGGGCCGCCATTCGCGAT
GGCAAGATTGATCTCTACCAGTGCGTGGTGCCGACCACCTGGAACGCCAGCCCGCGCGAT
CCCAAAGGGCAGATTGGCGCTTATGAAGCGGCGCTGATGAACACCAAAATGGCGATCCCC
GAGCAACCGCTGGAGATCCTGCGTACTCTGCACAGCTTTGACCCGTGCCTCGCCTGTTCA
ACACACGTGCTGGGCGACGACGGTAGCGAGCTGATCTCCGTGCAGGTGCGTTAA
Enzyme 6 GenBank Gene ID AP009048 Link Image
Enzyme 6 GeneCard ID hyaB Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus b0973
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Menon NK, Robbins J, Peck HD Jr, Chatelus CY, Choi ES, Przybyla AE: Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames. J Bacteriol. 1990 Apr;172(4):1969-77. [PubMed Link Image]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  4. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15970
Enzyme 7 Name Hydrogenase-2 large chain
Enzyme 7 Synonyms
  1. HYD2
  2. Membrane-bound hydrogenase 2 large subunit
  3. NiFe hydrogenase
Enzyme 7 Gene Name hybC
Enzyme 7 Protein Sequence >Hydrogenase-2 large chain 
MSQRITIDPVTRIEGHLRIDCEIENGVVSKAWASGTMWRGMEEIVKNRDPRDAWMIVQRI
CGVCTTTHALSSVRAAESALNIDVPVNAQYIRNIILAAHTTHDHIVHFYQLSALDWVDIT
SALQADPTKASEMLKGVSTWHLNSPEEFTKVQNKIKDLVASGQLGIFANGYWGHPAMKLP
PEVNLIAVAHYLQALECQRDANRVVALLGGKTPHIQNLAVGGVANPINLDGLGVLNLERL
MYIKSFIDKLSDFVEQVYKVDTAVIAAFYPEWLTRGKGAVNYLSVPEFPTDSKNGSFLFP
GGYIENADLSSYRPITSHSDEYLIKGIQESAKHSWYKDEAPQAPWEGTTIPAYDGWSDDG
KYSWVKSPTFYGKTVEVGPLANMLVKLAAGRESTQNKLNEIVAIYQKLTGNTLEVAQLHS
TLGRIIGRTVHCCELQDILQNQYSALITNIGKGDHTTFVKPNIPATGEFKGVGFLEAPRG
MLSHWMVIKDGIISNYQAVVPSTWNSGPRNFNDDVGPYEQSLVGTPVADPNKPLEVVRTI
HSFDPCMACAVHVVDADGNEVVSVKVL
Enzyme 7 Number of Residues 567
Enzyme 7 Molecular Weight 62490.7
Enzyme 7 Theoretical pI 6.23
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ferredoxin hydrogenase activity
  • ion binding
  • metal ion binding
  • nickel ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 7 General Function Involved in ferredoxin hydrogenase activity
Enzyme 7 Specific Function This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • H2 + A = AH2 [RN:R07182]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1800032 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P0ACE0 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name MBHM_ECOLI Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1704 bp 
ATGGCTTTTGTATCAGAAAGAGAAATTGTAAGAAAGATATTTAGCAAAAAAATTGACTTT
ACGATCTTGGCATTTTTCTATATTTCCTCTATTTTTTTTCTTCTTTGTAGTGGCGTTCTC
TTTCAATATTTTACCGCTGCCTTCACAAAAGGTAATTGTTATGAATGCTCAATGAAACTT
GATTACATAAAACAATTTTATTTTTCACTGGAAACCGCATGGTACCTCATATCTGCTGTT
GCAGTATTTATTGCATCTGTTTTTATACAGCATAGAATTAAAGCTTATTTAACATTATTA
GCTATTACATGGATTGTACTAACAATAACAGATGTGGCGTTAATACACGCCTTAGACAAT
ATAGCCATGAATAATATTTTGTTAAATATACTATATAATCTTTTTGGGGCGATTTTATTG
TCACTGTTTATGTGTTTATCAAATTCCCTCCTTTTCCACCTTAATAAGATAAAACATATT
CCAATGATTTTATCGGCAATGATTCCATTAGTTTCCGCAATAATAATAGCCATACTCATA
ACCGCTGTTATATATTTATTGTTTGCCCGGCAGGCGGTAGAGATTGAGATGGATATATCT
GAAGGTTCAGACATCGCATATGTAGGTGTAAAAGATAATGAGGAATCATTTGGGTTTTTA
AATGATAAAAAAACAGACACACCAACGTATCTGGATGTAATCAAAAATGGTAGTTTGATA
TATAATGATACACAGGGTTTAAGTGGTGCTGATATTTATATTGTCTCCGGTTGTTATGCC
CTTCCAGATTTACTTCGCAATGTACCGCTTGATGCTAAAAAATCTTTTCTGAATGTAAAA
AAGCTAGAAATCACACAGAAACTTCCAATGATGGGGTTCATACAAGGTGAATCCGCTGAT
GTGATGCCTAAAGCAGCATCCAGGTTAAGTTTGAGCAAGCAAGATGATAAATTTATGCTA
GCCTCAAGTGTTACTGACTCTCAAATAAAATTTAAATCAAACAATGCACAATTGATGGTT
GCTTTCGCATTTATGCCAATAACAACGAATGGTATTTTACATGATTATACATACGATATA
ATAATAAATGATAAAAAATATAAAATTGAAAATCATGTTGCACCTCTATCTAGGCTTGAT
AAAAATAAGAAGATGAAGTGTGAATACCAGCAAATATCGGATTTAACAAATACGTATAAC
ATTAATGCAAATTACTTAACGGGTTTTTTACTTGTCCTAAAACCAGATGATATTATTAAT
TACAACAATAGCCCTTCCGTACTACTCAAGACTGATTTTGCGTTCTATAAAAAAACATAC
CAGAAGCTTGATAAAATATATGATGACATAAGCAATGGAAAATTATCTTCACTGAGAGCA
ACAGGTATCTCCCAGTTTAGTATCAACGGGAAACATTTGTCGTTAAGGCCAGAATCGGAG
ATTATTATTTCTGAAGGGAGTTTGTATGGACTAGTTAATAAAAGCAAAAAAATCAAAATA
TATGGCACAGCAGATCTTGTTTTTGTTGATAACAAGATAATGAACCTTCGTAAAATAACT
TATTTGCAATCTAAGCTAGAAATTTTTGGTTCTTCTATTATGGATATATTAAAGTATATA
TTTGGTTTAGGTCTGCTAGCAATTTCTATAAAATTCATTCATTCTTACTTTAAGAATGAT
GTGAATGAAAATTTATTCTTGTAA
Enzyme 7 GenBank Gene ID AP009048 Link Image
Enzyme 7 GeneCard ID hybC Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus b2994
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Menon NK, Chatelus CY, Dervartanian M, Wendt JC, Shanmugam KT, Peck HD Jr, Przybyla AE: Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2. J Bacteriol. 1994 Jul;176(14):4416-23. [PubMed Link Image]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  4. Sargent F, Ballantine SP, Rugman PA, Palmer T, Boxer DH: Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit--identification of a soluble precursor of the small subunit in a hypB mutant. Eur J Biochem. 1998 Aug 1;255(3):746-54. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 15971
Enzyme 8 Name Hydrogenase-2 small chain
Enzyme 8 Synonyms
  1. HYD2
  2. Membrane-bound hydrogenase 2 small subunit
  3. NiFe hydrogenase
Enzyme 8 Gene Name hybO
Enzyme 8 Protein Sequence >Hydrogenase-2 small chain 
MTGDNTLIHSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECT
GCTESLLRATHPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGS
IPLKDNGIYCMVAGEPIVDHIRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVL
PGKTVINIPGCPPNPHNFLATVAHIITYGKPPKLDDKNRPTFAYGRLIHEHCERRPHFDA
GRFAKEFGDEGHREGWCLYHLGCKGPETYGNCSTLQFCDVGGVWPVAIGHPCYGCNEEGI
GFHKGIHQLANVENQTPRSQKPDVNAKEGGNVSAGAIGLLGGVVGLVAGVSVMAVRELGR
QQKKDNADSRGE
Enzyme 8 Number of Residues 372
Enzyme 8 Molecular Weight 39651.8
Enzyme 8 Theoretical pI 6.74
Enzyme 8 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • NADH dehydrogenase (quinone) activity
  • NADH dehydrogenase (ubiquinone) activity
  • NADH dehydrogenase activity
  • binding
  • catalytic activity
  • cofactor binding
  • ferredoxin hydrogenase activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • quinone binding
Process
  • metabolic process
  • oxidation reduction
Component
  • ferredoxin hydrogenase complex
  • macromolecular complex
  • protein complex
Enzyme 8 General Function Involved in NADH dehydrogenase (ubiquinone) activity
Enzyme 8 Specific Function This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • H2 + A = AH2 [RN:R07182]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-37
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4062385 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P69741 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name MBHT_ECOLI Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1119 bp 
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG
Enzyme 8 GenBank Gene ID AP009048 Link Image
Enzyme 8 GeneCard ID hybO Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus b2997
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  2. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  3. Sargent F, Ballantine SP, Rugman PA, Palmer T, Boxer DH: Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit--identification of a soluble precursor of the small subunit in a hypB mutant. Eur J Biochem. 1998 Aug 1;255(3):746-54. [PubMed Link Image]
  4. Tullman-Ercek D, DeLisa MP, Kawarasaki Y, Iranpour P, Ribnicky B, Palmer T, Georgiou G: Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides. J Biol Chem. 2007 Mar 16;282(11):8309-16. Epub 2007 Jan 11. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16746
Enzyme 9 Name Hydrogenase 1, small subunit
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name hyaA
Enzyme 9 Protein Sequence >Hydrogenase 1, small subunit 
MNNEETFYQAMRRQGVTRRSFLKYCSLAATSLGLGAGMAPKIAWALENKPRIPVVWIHGL
ECTCCTESFIRSAHPLAKDVILSLISLDYDDTLMAAAGTQAEEVFEDIITQYNGKYILAV
EGNPPLGEQGMFCISSGRPFIEKLKRAAAGASAIIAWGTCASWGCVQAARPNPTQATPID
KVITDKPIIKVPGCPPIPDVMSAIITYMVTFDRLPDVDRMGRPLMFYGQRIHDKCYRRAH
FDAGEFVQSWDDDAARKGYCLYKMGCKGPTTYNACSSTRWNDGVSFPIQSGHGCLGCAEN
GFWDRGSFYSRVVDIPQMGTHSTADTVGLTALGVVAAAVGVHAVASAVDQRRRHNQQPTE
TEHQPGNEDKQA
Enzyme 9 Number of Residues 372
Enzyme 9 Molecular Weight 40681.0
Enzyme 9 Theoretical pI 7.15
Enzyme 9 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • NADH dehydrogenase (quinone) activity
  • NADH dehydrogenase (ubiquinone) activity
  • NADH dehydrogenase activity
  • binding
  • catalytic activity
  • cofactor binding
  • ferredoxin hydrogenase activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • quinone binding
Process
  • metabolic process
  • oxidation reduction
Component
  • ferredoxin hydrogenase complex
  • macromolecular complex
  • protein complex
Enzyme 9 General Function Involved in NADH dehydrogenase (ubiquinone) activity
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 169888312 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID B1X8S5 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B1X8S5_ECODH Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1119 bp 
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG
Enzyme 9 GenBank Gene ID CP000948 Link Image
Enzyme 9 GeneCard ID hyaA Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus ECDH10B_1042
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16747
Enzyme 10 Name Hydrogenase 1, large subunit
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name hyaB
Enzyme 10 Protein Sequence >Hydrogenase 1, large subunit 
MSTQYETQGYTINNAGRRLVVDPITRIEGHMRCEVNINDQNVITNAVSCGTMFRGLEIIL
QGRDPRDAWAFVERICGVCTGVHALASVYAIEDAIGIKVPDNANIIRNIMLATLWCHDHL
VHFYQLAGMDWIDVLDALKADPRKTSELAQSLSSWPKSSPGYFFDVQNRLKKFVEGGQLG
IFRNGYWGHPQYKLPPEANLMGFAHYLEALDFQREIVKIHAVFGGKNPHPNWIVGGMPCA
INIDESGAVGAVNMERLNLVQSIITRTADFINNVMIPDALAIGQFNKPWSEIGTGLSDKC
VLSYGAFPDIANDFGEKSLLMPGGAVINGDFNNVLPVDLVDPQQVQEFVDHAWYRYPNDQ
VGRHPFDGITDPWYNPGDVKGSDTNIQQLNEQERYSWIKAPRWRGNAMEVGPLARTLIAY
HKGDAATVESVDRMMSALNLPLSGIQSTLGRILCRAHEAQWAAGKLQYFFDKLMTNLKNG
NLATASTEKWEPATWPTECRGVGFTEAPRGALGHWAAIRDGKIDLYQCVVPTTWNASPRD
PKGQIGAYEAALMNTKMAIPEQPLEILRTLHSFDPCLACSTHVLGDDGSELISVQVR
Enzyme 10 Number of Residues 597
Enzyme 10 Molecular Weight 66252.9
Enzyme 10 Theoretical pI 5.85
Enzyme 10 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ferredoxin hydrogenase activity
  • ion binding
  • metal ion binding
  • nickel ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 10 General Function Involved in ferredoxin hydrogenase activity
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 169888465 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID B1X8S6 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B1X8S6_ECODH Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1794 bp 
ATGAGCACTCAGTACGAAACTCAGGGATACACCATCAATAATGCCGGACGCCGCCTGGTG
GTCGACCCGATTACGCGCATCGAAGGCCACATGCGCTGCGAAGTGAATATTAACGATCAG
AATGTGATCACCAATGCCGTCTCCTGCGGCACCATGTTTCGCGGGCTGGAGATCATCCTA
CAAGGGCGCGACCCGCGCGATGCGTGGGCGTTCGTTGAACGTATCTGCGGCGTCTGTACT
GGCGTACACGCCCTGGCTTCGGTTTACGCCATCGAAGATGCTATCGGTATTAAAGTGCCG
GACAACGCCAATATCATCCGCAACATTATGCTGGCAACGCTCTGGTGCCACGATCATCTG
GTGCACTTCTATCAGCTTGCCGGGATGGACTGGATCGATGTGTTAGATGCGCTGAAAGCC
GACCCGCGGAAAACCTCCGAACTGGCGCAAAGTCTCTCCTCTTGGCCGAAATCATCCCCT
GGCTATTTCTTCGACGTACAAAACCGCCTGAAAAAATTTGTTGAAGGCGGGCAGTTGGGG
ATCTTCCGCAATGGCTACTGGGGGCACCCGCAGTACAAACTGCCGCCAGAAGCTAACCTG
ATGGGCTTTGCCCACTATCTCGAAGCTCTCGATTTCCAGCGTGAAATTGTCAAAATCCAC
GCGGTCTTTGGCGGTAAAAACCCGCATCCAAACTGGATTGTCGGCGGGATGCCTTGCGCC
ATCAACATTGACGAAAGCGGCGCGGTCGGGGCAGTCAATATGGAACGCCTGAACCTGGTG
CAGTCAATTATCACCCGCACGGCGGACTTCATTAACAACGTGATGATCCCCGACGCCTTA
GCCATCGGTCAGTTCAACAAACCGTGGAGCGAAATCGGCACTGGTCTTTCTGATAAATGC
GTTCTCAGCTACGGCGCATTCCCGGATATTGCCAACGACTTTGGCGAGAAAAGTCTGCTG
ATGCCTGGCGGCGCGGTGATTAACGGCGACTTCAACAATGTGCTGCCAGTGGATTTGGTT
GATCCGCAGCAGGTGCAGGAGTTTGTCGACCACGCCTGGTATCGATATCCCAACGATCAG
GTCGGGCGTCATCCGTTCGATGGCATCACCGACCCGTGGTACAACCCCGGCGATGTCAAA
GGCAGCGATACCAACATTCAGCAGCTGAATGAACAGGAACGCTACTCGTGGATCAAAGCG
CCACGCTGGCGCGGTAACGCGATGGAAGTGGGGCCGCTGGCGCGCACGTTAATCGCTTAT
CACAAAGGCGATGCTGCGACCGTTGAGTCGGTCGATCGCATGATGTCGGCGTTGAACCTG
CCGCTTTCCGGTATCCAGTCAACGTTAGGCCGCATTTTGTGCCGCGCGCACGAAGCGCAG
TGGGCCGCAGGTAAGTTGCAGTATTTCTTCGACAAGCTGATGACCAACCTGAAAAACGGC
AATCTCGCCACTGCTTCCACGGAAAAATGGGAACCTGCAACCTGGCCGACAGAGTGCCGT
GGTGTCGGTTTTACCGAAGCGCCGCGCGGGGCGTTAGGCCACTGGGCCGCCATTCGCGAT
GGCAAGATTGATCTCTACCAGTGCGTGGTGCCGACCACCTGGAACGCCAGCCCGCGCGAT
CCCAAAGGGCAGATTGGCGCTTATGAAGCGGCGCTGATGAACACCAAAATGGCGATCCCC
GAGCAACCGCTGGAGATCCTGCGTACTCTGCACAGCTTTGACCCGTGCCTCGCCTGTTCA
ACACACGTGCTGGGCGACGACGGTAGCGAGCTGATCTCCGTGCAGGTGCGTTAA
Enzyme 10 GenBank Gene ID CP000948 Link Image
Enzyme 10 GeneCard ID hyaB Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus ECDH10B_1043
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16748
Enzyme 11 Name Hydrogenase 2, large subunit
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name hybC
Enzyme 11 Protein Sequence >Hydrogenase 2, large subunit 
MSQRITIDPVTRIEGHLRIDCEIENGVVSKAWASGTMWRGMEEIVKNRDPRDAWMIVQRI
CGVCTTTHALSSVRAAESALNIDVPVNAQYIRNIILAAHTTHDHIVHFYQLSALDWVDIT
SALQADPTKASEMLKGVSTWHLNSPEEFTKVQNKIKDLVASGQLGIFANGYWGHPAMKLP
PEVNLIAVAHYLQALECQRDANRVVALLGGKTPHIQNLAVGGVANPINLDGLGVLNLERL
MYIKSFIDKLSDFVEQVYKVDTAVIAAFYPEWLTRGKGAVNYLSVPEFPTDSKNGSFLFP
GGYIENADLSSYRPITSHSDEYLIKGIQESAKHSWYKDEAPQAPWEGTTIPAYDGWSDDG
KYSWVKSPTFYGKTVEVGPLANMLVKLAAGRESTQNKLNEIVAIYQKLTGNTLEVAQLHS
TLGRIIGRTVHCCELQDILQNQYSALITNIGKGDHTTFVKPNIPATGEFKGVGFLEAPRG
MLSHWMVIKDGIISNYQAVVPSTWNSGPRNFNDDVGPYEQSLVGTPVADPNKPLEVVRTI
HSFDPCMACAVHVVDADGNEVVSVKVL
Enzyme 11 Number of Residues 567
Enzyme 11 Molecular Weight 62490.7
Enzyme 11 Theoretical pI 6.23
Enzyme 11 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ferredoxin hydrogenase activity
  • ion binding
  • metal ion binding
  • nickel ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 11 General Function Involved in ferredoxin hydrogenase activity
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 169890076 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID B1XFF0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B1XFF0_ECODH Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1704 bp 
ATGGCTTTTGTATCAGAAAGAGAAATTGTAAGAAAGATATTTAGCAAAAAAATTGACTTT
ACGATCTTGGCATTTTTCTATATTTCCTCTATTTTTTTTCTTCTTTGTAGTGGCGTTCTC
TTTCAATATTTTACCGCTGCCTTCACAAAAGGTAATTGTTATGAATGCTCAATGAAACTT
GATTACATAAAACAATTTTATTTTTCACTGGAAACCGCATGGTACCTCATATCTGCTGTT
GCAGTATTTATTGCATCTGTTTTTATACAGCATAGAATTAAAGCTTATTTAACATTATTA
GCTATTACATGGATTGTACTAACAATAACAGATGTGGCGTTAATACACGCCTTAGACAAT
ATAGCCATGAATAATATTTTGTTAAATATACTATATAATCTTTTTGGGGCGATTTTATTG
TCACTGTTTATGTGTTTATCAAATTCCCTCCTTTTCCACCTTAATAAGATAAAACATATT
CCAATGATTTTATCGGCAATGATTCCATTAGTTTCCGCAATAATAATAGCCATACTCATA
ACCGCTGTTATATATTTATTGTTTGCCCGGCAGGCGGTAGAGATTGAGATGGATATATCT
GAAGGTTCAGACATCGCATATGTAGGTGTAAAAGATAATGAGGAATCATTTGGGTTTTTA
AATGATAAAAAAACAGACACACCAACGTATCTGGATGTAATCAAAAATGGTAGTTTGATA
TATAATGATACACAGGGTTTAAGTGGTGCTGATATTTATATTGTCTCCGGTTGTTATGCC
CTTCCAGATTTACTTCGCAATGTACCGCTTGATGCTAAAAAATCTTTTCTGAATGTAAAA
AAGCTAGAAATCACACAGAAACTTCCAATGATGGGGTTCATACAAGGTGAATCCGCTGAT
GTGATGCCTAAAGCAGCATCCAGGTTAAGTTTGAGCAAGCAAGATGATAAATTTATGCTA
GCCTCAAGTGTTACTGACTCTCAAATAAAATTTAAATCAAACAATGCACAATTGATGGTT
GCTTTCGCATTTATGCCAATAACAACGAATGGTATTTTACATGATTATACATACGATATA
ATAATAAATGATAAAAAATATAAAATTGAAAATCATGTTGCACCTCTATCTAGGCTTGAT
AAAAATAAGAAGATGAAGTGTGAATACCAGCAAATATCGGATTTAACAAATACGTATAAC
ATTAATGCAAATTACTTAACGGGTTTTTTACTTGTCCTAAAACCAGATGATATTATTAAT
TACAACAATAGCCCTTCCGTACTACTCAAGACTGATTTTGCGTTCTATAAAAAAACATAC
CAGAAGCTTGATAAAATATATGATGACATAAGCAATGGAAAATTATCTTCACTGAGAGCA
ACAGGTATCTCCCAGTTTAGTATCAACGGGAAACATTTGTCGTTAAGGCCAGAATCGGAG
ATTATTATTTCTGAAGGGAGTTTGTATGGACTAGTTAATAAAAGCAAAAAAATCAAAATA
TATGGCACAGCAGATCTTGTTTTTGTTGATAACAAGATAATGAACCTTCGTAAAATAACT
TATTTGCAATCTAAGCTAGAAATTTTTGGTTCTTCTATTATGGATATATTAAAGTATATA
TTTGGTTTAGGTCTGCTAGCAATTTCTATAAAATTCATTCATTCTTACTTTAAGAATGAT
GTGAATGAAAATTTATTCTTGTAA
Enzyme 11 GenBank Gene ID CP000948 Link Image
Enzyme 11 GeneCard ID hybC Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus ECDH10B_3171
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16749
Enzyme 12 Name Hydrogenase 2, small subunit
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name hybO
Enzyme 12 Protein Sequence >Hydrogenase 2, small subunit 
MTGDNTLIHSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECT
GCTESLLRATHPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGS
IPLKDNGIYCMVAGEPIVDHIRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVL
PGKTVINIPGCPPNPHNFLATVAHIITYGKPPKLDDKNRPTFAYGRLIHEHCERRPHFDA
GRFAKEFGDEGHREGWCLYHLGCKGPETYGNCSTLQFCDVGGVWPVAIGHPCYGCNEEGI
GFHKGIHQLANVENQTPRSQKPDVNAKEGGNVSAGAIGLLGGVVGLVAGVSVMAVRELGR
QQKKDNADSRGE
Enzyme 12 Number of Residues 372
Enzyme 12 Molecular Weight 39651.8
Enzyme 12 Theoretical pI 6.74
Enzyme 12 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • NADH dehydrogenase (quinone) activity
  • NADH dehydrogenase (ubiquinone) activity
  • NADH dehydrogenase activity
  • binding
  • catalytic activity
  • cofactor binding
  • ferredoxin hydrogenase activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on hydrogen as donor
  • oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor
  • quinone binding
Process
  • metabolic process
  • oxidation reduction
Component
  • ferredoxin hydrogenase complex
  • macromolecular complex
  • protein complex
Enzyme 12 General Function Involved in NADH dehydrogenase (ubiquinone) activity
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 169888312 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID B1XFF3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B1XFF3_ECODH Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1119 bp 
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG
Enzyme 12 GenBank Gene ID CP000948 Link Image
Enzyme 12 GeneCard ID hybO Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus ECDH10B_3174
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 17228
Enzyme 13 Name Voltage-gated hydrogen channel 1
Enzyme 13 Synonyms
  1. Hydrogen voltage-gated channel 1
  2. HV1
  3. Voltage sensor domain-only protein
Enzyme 13 Gene Name HVCN1
Enzyme 13 Protein Sequence >Voltage-gated hydrogen channel 1 
MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPT
PVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAEL
ILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVV
SFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAA
KIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN
Enzyme 13 Number of Residues 273
Enzyme 13 Molecular Weight 31682.9
Enzyme 13 Theoretical pI 6.80
Enzyme 13 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 13 General Function Involved in ion channel activity
Enzyme 13 Specific Function Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 101-121 136-156 170-190 198-218
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 91992153 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q96D96 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name HVCN1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >822 bp 
ATGGCCACCTGGGACGAAAAGGCAGTCACCCGCAGGGCCAAGGTGGCTCCCGCTGAGAGG
ATGAGCAAGTTCTTAAGGCACTTCACGGTCGTGGGAGACGACTACCATGCCTGGAACATC
AACTACAAGAAATGGGAGAATGAAGAGGAGGAGGAGGAGGAGGAGCAGCCACCACCCACA
CCAGTCTCAGGCGAGGAAGGCAGAGCTGCAGCCCCTGACGTTGCCCCTGCCCCTGGCCCC
GCACCCAGGGCCCCCCTTGACTTCAGGGGCATGTTGAGGAAACTGTTCAGCTCCCACAGG
TTTCAGGTCATCATCATCTGCTTGGTGGTTCTGGATGCCCTCCTGGTGCTTGCTGAGCTC
ATCCTGGACCTGAAGATCATCCAGCCCGACAAGAATAACTATGCTGCCATGGTATTCCAC
TACATGAGCATCACCATCTTGGTCTTTTTTATGATGGAGATCATCTTTAAATTATTTGTC
TTCCGCCTGGAGTTCTTTCACCACAAGTTTGAGATCCTGGATGCCGTCGTGGTGGTGGTC
TCATTCATCCTCGACATTGTCCTCCTGTTCCAGGAGCACCAGTTTGAGGCTCTGGGCCTG
CTGATTCTGCTCCGGCTGTGGCGGGTGGCCCGGATCATCAATGGGATTATCATCTCAGTT
AAGACACGTTCAGAACGGCAACTCTTAAGGTTAAAACAGATGAATGTACAATTGGCCGCC
AAGATTCAACACCTTGAGTTCAGCTGCTCTGAGAAGGAACAAGAAATTGAAAGACTTAAC
AAACTATTGCGACAGCATGGACTTCTTGGTGAAGTGAACTAG
Enzyme 13 GenBank Gene ID NM_001040107.1 Link Image
Enzyme 13 GeneCard ID HVCN1 Link Image
Enzyme 13 GenAtlas ID HVCN1 Link Image
Enzyme 13 HGNC ID HGNC:28240 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 12q24.11
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ramsey IS, Moran MM, Chong JA, Clapham DE: A voltage-gated proton-selective channel lacking the pore domain. Nature. 2006 Apr 27;440(7088):1213-6. Epub 2006 Mar 22. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available