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Human Metabolome Database Version 2.5

 

Showing metabocard for Uroporphyrin III (HMDB00916)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-12 15:16:44
Accession Number HMDB00916
Secondary Accession Numbers Not Available
Common Name Uroporphyrin III
Description Uroporphyrin is the porphyrin produced by oxidation of the methylene bridges in uroporphyrinogen. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation. Excessive amounts of uroporphyrin I are excreted in congenital erythropoietic porphyria, and both types I and III are excreted in porphyria cutanea tarda. Uroporphyrin I and III are the most common isomers.
Synonyms
  1. 3,8,13,17-tetrakis(carboxymethyl)porphyrin-2,7,12,18-tetrapropanoate
  2. 3,8,13,17-tetrakis(carboxymethyl)porphyrin-2,7,12,18-tetrapropanoic acid
  3. 3,8,13,17-tetramethyl-2,7,12,18-Porphinetetrapropionate
  4. 3,8,13,17-tetramethyl-2,7,12,18-Porphinetetrapropionic acid
  5. Coproporphyrin III
  6. Uroporphyrin III
Chemical IUPAC Name 3,8,13,17-tetrakis(carboxymethyl)porphyrin-2,7,12,18-tetrapropanoic acid
Chemical Formula C40H38N4O16
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Porphyrins
Sub Class
  • Uroporphyrins
Family
  • Microbial Metabolite
Species
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 830.747
Monoisotopic Molecular Weight 830.228271
Isomeric SMILES OC(=O)CCC1=C2NC(/C=C3N=C(C=C4NC(=CC5=NC(=C/2)C(CCC(O)=O)=C5CC(O)=O)/C(CC(O)=O)=C4CCC(O)=O)C(CC(O)=O)=C3CCC(O)=O)=C1CC(O)=O
Canonical SMILES OC(=O)CCC1=C2NC(C=C3N=C(C=C4NC(=CC5=NC(=C2)C(CCC(O)=O)=C5CC(O)=O)C(CC(O)=O)=C4CCC(O)=O)C(CC(O)=O)=C3CCC(O)=O)=C1CC(O)=O
KEGG Compound ID C02469 Link Image
BioCyc ID UROPORPHYRIN_III Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00916 Link Image
Metagene Link HMDB00916 Link Image
METLIN ID 5870 Link Image
PubChem Compound Not Available
PubChem Substance 5484 Link Image
ChEBI ID 15436 Link Image
CAS Registry Number 18273-06-8
InChI Identifier InChI=1/C40H38N4O16/c45-33(46)5-1-17-21(9-37(53)54)29-14-27-19(3-7-35(49)50)22(10-38(55)56)30(43-27)15-28-20(4-8-36(51)52)24(12-40(59)60)32(44-28)16-31-23(11-39(57)58)18(2-6-34(47)48)26(42-31)13-25(17)41-29/h13-16,41,44H,1-12H2,(H,45,46)(H,47,48)(H,49,50)(H,51,52)(H,53,54)(H,55,56)(H,57,58)(H,59,60)/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-
Synthesis Reference Kajiwara, Masahiro; Mizutani, Minoru; Kojima, Ichiro. Manufacture of uroporphyrin III with Arthrobacter. Jpn. Kokai Tokkyo Koho (1993), 7 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0366 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -8
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.75 [Predicted by ALOGPS]; -3.8 [Predicted by PubChem via XLOGP] 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 1R3T Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location
  • Urine
Tissue Location
Tissue References
Liver —
Concentrations (Normal) Not Available
Concentrations (Abnormal)
Biofluid Urine
Value 0.00005 (0.00005-0.0007) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Comments Not Available
References
  • Ozalla D, Herrero C, Ribas-Fito N, To-Figueras J, Toll A, Sala M, Grimalt J, Basagana X, Lecha M, Sunyer J: Evaluation of urinary porphyrin excretion in neonates born to mothers exposed to airborne hexachlorobenzene. Environ Health Perspect. 2002 Feb;110(2):205-9. [PubMed Link Image]
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Tsai SF, Bishop DF, Desnick RJ: Purification and properties of uroporphyrinogen III synthase from human erythrocytes. J Biol Chem. 1987 Jan 25;262(3):1268-73. [PubMed Link Image]
  2. Bozek P, Hutta M, Hrivnakova B: Rapid analysis of porphyrins at low ng/l and microg/l levels in human urine by a gradient liquid chromatography method using octadecylsilica monolithic columns. J Chromatogr A. 2005 Aug 19;1084(1-2):24-32. [PubMed Link Image]
  3. Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. [PubMed Link Image]
  4. Luo J, Lim CK: Isolation and characterization of new porphyrin metabolites in human porphyria cutanea tarda and in rats treated with hexachlorobenzene by HPTLC, HPLC and liquid secondary ion mass spectrometry. Biomed Chromatogr. 1995 May-Jun;9(3):113-22. [PubMed Link Image]
  5. Schonning C, Leeming R, Stenstrom TA: Faecal contamination of source-separated human urine based on the content of faecal sterols. Water Res. 2002 Apr;36(8):1965-72. [PubMed Link Image]
  6. Hernandez-Zavala A, Del Razo LM, Garcia-Vargas GG, Aguilar C, Borja VH, Albores A, Cebrian ME: Altered activity of heme biosynthesis pathway enzymes in individuals chronically exposed to arsenic in Mexico. Arch Toxicol. 1999 Mar;73(2):90-5. [PubMed Link Image]
  7. Salen G, Berginer V, Shore V, Horak I, Horak E, Tint GS, Shefer S: Increased concentrations of cholestanol and apolipoprotein B in the cerebrospinal fluid of patients with cerebrotendinous xanthomatosis. Effect of chenodeoxycholic acid. N Engl J Med. 1987 May 14;316(20):1233-8. [PubMed Link Image]
  8. To-Figueras J, Ozalla D, Mateu CH: Long-standing changes in the urinary profile of porphyrin isomers after clinical remission of porphyria cutanea tarda. Ann Clin Lab Sci. 2003 Summer;33(3):251-6. [PubMed Link Image]
Metabolic Enzymes
  1. Porphyrin biosynthesis protein includes: uroporphyrinogen-III methyltransferase and uroporphyrinogen-III synthase]
  2. Uroporphyrinogen III methylase
  3. Uroporphyrinogen-III methyltransferase/synthase
  4. Uroporphyrinogen-III methyltransferase/synthase
  5. Siroheme synthase
  6. Putative uroporphyrinogen-III C-methyltransferase
  7. Siroheme synthase
Enzyme 1 [top]
Enzyme 1 ID 15856
Enzyme 1 Name Porphyrin biosynthesis protein includes: uroporphyrinogen-III methyltransferase and uroporphyrinogen-III synthase]
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name hemD
Enzyme 1 Protein Sequence >Porphyrin biosynthesis protein includes: uroporphyrinogen-III methyltransferase and uroporphyrinogen-III synthase] 
MRIMKGKVYLVGAGPGDYKLMTLKGLECIRKSDVIVYDRLANSSYLREAKPDCELIYVGK
ASSNHILPQEDINRIIAEKAKEGKIVTRLKGGDPYVFGRGGEEAETLVDEGIEFEVVPGI
TSAIGGLCYAGIPITHRDHASSFHVITGHLKGDDSGELNWNALANNKGTLVFLMGISNLE
KISENLMKEGKDKDTPVALISWATRYNQRVVTSTLENVYETAIKEEVKPPTLIVVGSVVG
LREKLNFFESKPLFGKSIAVTRSRNQNSVLVEKIMDLGGNPIEIPTIKVEKIQNNINLEN
EIKNINKYNYLILTSKNAVEIFFEKIYEMNFDLRILSNLKVCAIGSATSNELKKRGIIAD
IVPKKFVAESLYEELAPILNDDDNILIPRAENARDYLVDKLKAICEVTEVHIYRTVIDEE
KKGEILDILNSNDIDYITFTSSSTVNNLVEIIGKENIKILEKIKTLSIGPITTETINSLG
IKLYKESATSTIDSLVDLIIKN
Enzyme 1 Number of Residues 502
Enzyme 1 Molecular Weight 55824.8
Enzyme 1 Theoretical pI 5.47
Enzyme 1 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrinogen-III synthase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole biosynthetic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 1 General Function Involved in methyltransferase activity
Enzyme 1 Specific Function S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 115250886 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q180R8 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name Q180R8_CLOD6 Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1509 bp 
TTGCTAAAGAGAGTGAGGTGTAGCTATTTGAAAAAAAATAGATTAATAGCAAAGAATATA
TCAATAGCATTTATAGTACTATTCTTTTTTAGTGTATTTACATTCTTTTATGTAGGTAAT
ATTAATAGAGTGTTAGAATATGAAACAAATGACATAATAACAGTTACAATTGCTGGATGG
ATTATACTTTCATTTTTATTTTTAGGTATTATAATTTACATATTATATTCAAAAGCAAAT
AGTCAAAAAACTATAGAAAAAGTAGCATATACGGATTTTGTAACAGGTTATTCCAACTGG
AGAAAGTTTGAATTAGATGTTACAAATTTATTAAAGAAAACATCACAAAATAATAAATAT
GCAATGGTCATATTCGATATTGATAAATTTAAAGCAATTAATGATATATATGGCCATAAA
AAGGGAAATTTAATATTAAAAGATATTGCAGATACTTTAAATGAATTGACTGATATCAAT
GAAACTTTTGCTCGTGTAAGTGCTGATAATTTCAATATATTATTAACATATAACAAAAAA
GAGGATATAATAAATATTATCAAAAAGATTATGGCAAATAATGAACTTGTAAACTTATCT
TTTGGAATTTATGAAATCAAAGATAAGGATTTATCTGTAAGTGTATATAGTGATAGAGCT
TCACTTGCAAAATCATCAATAAAAAATAATAGTGATGTAAATTTTGCATTTTTTAATGAC
AAATTAAGAGAGAAATTATTATTTGAAGATAAGATAGAAAAAGAAATGGAATATGCTCTT
GAAAGTGGGCAATTCGTAATGTATTTACAACCAAAATACAATATTAAATTAGATAAATTT
TGTGGAAGTGAAGCCCTAGTCAGATGGCAATATACAGAAAAAGAGGTCATATATCCAGGT
GATTTTATTCCTATATTTGAAAAAAATGGATTTATTAGAAAGATTGATATGTACATATTA
GAACAAGCTTGTAAAGAAATCCGGTCTTTATTTGATAAAGGAATTTCACCTTTACCTATA
TCTGTAAACTTCTCAAGAGTTGATTTTTTTAAAAAAGATTTTATTGAAAACATAGTAAAT
ATATGTGATAGATATAAAATACCATATAGTTTAATAGAAATTGAAATTACTGAATCTAGT
ATGTTTGGAGATACTGATACTCTATTTAATGTTAGTAGAAACCTACAGGATATTGGCTTT
ATAGTTGCAATGGATGATTTTGGCTCTGGATATTCTTCTGTAAATATGCTTAAAAATATA
CCATTAAATGTAATAAAATTAGATAGAGGATTTTTTGTTGATGATAAAGATGTTGATAAG
AGTCAAATTGTTATAAAAAGCATAGTTTCTCTCATTAAGCAATTAGGAATAAGGGTTGTT
GCTGAAGGAATTGAAACAAGAAGTCAAATAGAAATGTTAAAAAAAGCAAATTGTGATATT
GTTCAAGGATATTATTTTTCAAAACCATTACCAATTAAAGAATTTGAAAAATTAGTCTAT
AAAATATAG
Enzyme 1 GenBank Gene ID AM180355 Link Image
Enzyme 1 GeneCard ID hemD Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus CD3420
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 15857
Enzyme 2 Name Uroporphyrinogen III methylase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name hemX
Enzyme 2 Protein Sequence >Uroporphyrinogen III methylase 
MSKKAYIIGAGPGDEELLTLKAINALQKCTAVLYDRLVGNNILNYLNDDCEIYYCGKEPG
CHYKTQEEINESIVELAKKGHVVGRVKGGDPYVFGRGGEEVLALVEENIPFEVIPGVTSP
ISVLNYAGIPITHRGLAQSFHIVTGMSARTLNVNWEALSKENGTLVFMMGLSNLETIVEK
LLENGKDIETPCGVVMRGTTSKQRKVIGTLENICKKVREAKLESPCIIVVGDVVSLNEKL
SWYEKLPLFGANICLTRSKEQSKEIKWKLKELGAEVTEINSIKIKKTAENLDEYINTLEK
YDHIVFTSVNAVNVFFDYLVKNRVDIRKIKADFAVLGKATKKALISRGIVPSIMAHSFTA
EGLFEVLKDNIKEGEEVLIPCSSLSREYLFDNLASLGAKCHRVNIYDTVCGDVKNPRAFK
EVDMVLYTSPSTVKNMIDMIGLEALKEKVSIAIGPITLKALNESGIEGKMCKTHCGDGFL
SEIEGIWQEVKK
Enzyme 2 Number of Residues 492
Enzyme 2 Molecular Weight 54448.8
Enzyme 2 Theoretical pI 6.70
Enzyme 2 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrinogen-III synthase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole biosynthetic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 2 General Function Involved in methyltransferase activity
Enzyme 2 Specific Function S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 18144562 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8XKG5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q8XKG5_CLOPE Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1479 bp 
ATGGAGTTTTTAGATAAAGACTTAGTTTCCATACAGGAAACTAGGGGGCTTATAAGAAAG
GCTAAAGAAGCTCAAAGCAAGTTAGCCCGTATGAGTCAACAAGACATAGACAGAATAGTT
AAAGCTATATCTGATGCTGCTTATGAAAATTCTGAAAAACTTGCTAAGATGGCAAATGAG
GAAACAGGATTTGGTAAATGGGAAGATAAAGTATTAAAAAATGTTTTTGCTGCAAGAACA
GTTTATGAATCAATAAAGGATACAAAAACTGTTGGAATAGTAGAGGAAAATGTTGAGAAA
AGAGCATTTAAAATTATGGTGCCAGTAGGAGTAGTTGCAGGACTTATACCATCAACAAAT
CCAACTTCAACAGCAATCTACAAAGCTATGATTTCAATAAAAGCTAGAAATGCAATTGTT
TTATCACCACATCCAAGTGCAAAAAAATGTATTATTGAAACAGCTAAGATAATAGCTAAG
GCTGCTGAGAGAGCAGGTTGTCCAGAAGGAGCTATAGGATGCATTACAGTACCTTCAATA
GAAGGAACTAATGAACTTATGAAGAATAAAGATACTTCATTAATCCTAGCAACAGGTGGA
GAAGCAATGGTTAGAGCTGCTTATTCATCAGGAACACCAGCTATAGGTGTTGGACCAGGA
AATGGACCAGCTTTCATAGATAAGAGTGCAGATGTTAAGTTAGCAGTTAAGAGAATATTA
GATTCTAAAACTTTTGATAATGGAACAATATGTGCTTCAGAACAATCAATAGTAGTTGAA
AAAGCTATGGAAGATGAAGTTGTTAGAGAATTAAAAGAACAAGGAGCTTACTTCTTAACT
GAAGAACAAGCAAATCAACTATCTAAATTTGTAATGAGAGCAAATGGAACTATGAACCCA
CAAATAGTTGGAAAAACTCCACAAGACATAGCTAAGTTAGCTGGTTTAGAAGGAATTCCA
TCTTGGGCAAGAGTTTTAGTTCCAAGAGAGTGCCATGTTGGACATAAGTATCCATTCTCA
AGAGAAAAGTTAACAACTATTTTAACTTTCTTTGTAGAAGAGAATGTAGATGCTGTATTA
AATAGATGTAGAGAAATATTACTAAATGAAGGAGCTGGACATACATTCTGTATGCATGCA
AATAATGAGGAGCTTGTTAAGAGATTCGCATTAGAAATGCCAGTTTCAAGAATGGTAGTA
AATTCACCAGGAGCTCTTGGTGGAATAGGAGCTACAATCAACTTAGTACCTGCCTTAACT
TTAGGATGTGGTGCAGTTGGAGGAAGTTCTACATCACACAACATAGGACCATTAGATTTA
ATGAATACAAGAAATGTAGCTTATGGAATTAGAGAACTTGAAGATATTAGAGAGTTAGCT
GTAGGAGCTACAAAGGAAGTTTCCGCAAGTTTAGACTTAGGCGACAAGGAAGAGTTAATA
AACTTATTAGTTAAGAAGATTATTGAGGAACTTAAGTAA
Enzyme 2 GenBank Gene ID BA000016 Link Image
Enzyme 2 GeneCard ID hemX Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus CPE1434
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15858
Enzyme 3 Name Uroporphyrinogen-III methyltransferase/synthase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name hemD
Enzyme 3 Protein Sequence >Uroporphyrinogen-III methyltransferase/synthase 
MSKKAYIIGAGPGDEELLTLKAINALQKCTAVLYDRLVGNNILNYLNDDCEIYYCGKEPG
CHYKTQEEINESIVELAKKGHVVGRVKGGDPYVFGRGGEEVLALVEENIPFEVIPGVTSP
ISVLNYAGIPITHRGLAQSFHIVTGMSARTLNVNWKALSKENGTLVFMMGLSNLETIVEK
LLENGKDIETPCGVVMRGTTSKQRKVIGTLENICKKVREAKLESPCIIVVGDVVSLNEKL
SWYENLPLFGANICLTRSKEQSKEIKWKLKELGAEVTEINSIKIKETAYNLDEYINTLEK
YDHIVFTSVNAVNVFFDYLVKNRVDIRKIKADFAVLGKATKKALIARGIVPSIMAHSFTA
EGLFEVLKDNIKEGEEVLIPCSSLSREYLFDNLASLGAKCHRVNIYDTICGDVKNPRAFK
EVDMVLYTSPSTVKNMIDMIGLEALKEKVSIAIGPITLKALNESGIEGKMCKTHCGDGFL
SEIEGIWQEVKK
Enzyme 3 Number of Residues 492
Enzyme 3 Molecular Weight 54466.8
Enzyme 3 Theoretical pI 6.70
Enzyme 3 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrinogen-III synthase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole biosynthetic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 3 General Function Involved in methyltransferase activity
Enzyme 3 Specific Function S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 110674539 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q0TQG5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q0TQG5_CLOP1 Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1479 bp 
ATGGAGTTTTTAGATAAAGACTTAGTTTCCATACAGGAAACTAGGGGACTTATAAGAAAG
GCTAAAGAAGCTCAAAGTAAGTTAGCCCGTATGAGTCAACAAGACATAGATAGAATAGTT
AAAGCTATATCTGATGCTGCTTATGAAAATTCTGAAAAACTTGCTAAGATGGCAAATGAG
GAAACAGGATTTGGTAAATGGGAAGATAAAGTATTAAAAAATGTTTTTGCTGCAAGAACA
GTTTATGAATCAATAAAGGATACAAAAACTGTTGGAATAGTAGAGGAAAATGTTGAGAAA
AGAGCATTTAAAATTATGGTGCCAGTAGGAGTAGTTGCAGGACTTATACCATCAACAAAT
CCAACTTCAACAGCAATCTACAAAGCTATGATTTCAATAAAAGCTAGAAATGCAATTGTT
TTATCACCACATCCAAGTGCAAAAAAATGTATTATTGAAACAGCTAAGATAATAGCTAAG
GCTGCTGAGAGAGCAGGTTGTCCAGAAGGAGCTATAGGATGCATTACAGTACCTTCAATA
GAAGGAACTAATGAACTTATGAAGAATAAAGATACTTCATTAATCCTAGCAACAGGTGGA
GAAGCAATGGTTAGAGCTGCTTATTCATCAGGAACACCAGCTATAGGTGTTGGACCAGGA
AATGGACCAGCATTCATAGATAAGAGTGCGGATGTTAAGTTAGCAGTTAAGAGAATATTA
GATTCTAAAACTTTTGATAATGGAACAATATGTGCTTCAGAACAATCAATAGTAGTTGAA
AAAGCTATGGAAGATGAAGTTGTTAGAGAATTAAAAGAACAAGGAGCTTACTTCTTAACT
GAAGAACAAGCAAATCAACTATCTAAATTTGTAATGAGAGCAAATGGAACTATGAATCCA
CAAATAGTTGGAAAAACTCCTCAAGACATAGCTAAATTAGCTGGTTTAGAAGGAATTCCA
TCTTGGGCAAGAGTTTTAATTCCAAGAGAGTGCCATGTTGGACATAAGTATCCATTCTCA
AGAGAAAAGTTAACAACTATTTTAACTTTCTTTGTAGAAGAGAATGTAGATGCTGTATTA
AATAGATGTAGAGAAATATTACTAAATGAAGGAGCTGGACATACATTCTGTATGCATGCA
AATAATGAGGAGCTTGTTAAGAGATTCGCATTAGAAATGCCGGTTTCAAGAATGGTAGTA
AATTCACCAGGAGCTCTTGGTGGAATAGGAGCTACAATCAACTTAGTACCTGCCTTAACA
TTAGGATGTGGTGCAGTTGGAGGAAGTTCTACATCACATAACATAGGACCATTAGATTTA
ATGAATACGAGAAATGTAGCTTATGGAGTTAGAGAACTTGAAGATATTAGAGAGTTAGCT
GTAGGAGCTACAAAGGAAGTTGCTGCAAGTTTAGATTTAGGTGACAAGGAAGAATTAATA
AACTTATTAGTTAAGAAGATTATTGAGGAACTTAAGTAA
Enzyme 3 GenBank Gene ID CP000246 Link Image
Enzyme 3 GeneCard ID hemD Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus CPF_1687
Enzyme 3 SNPs SNPJam Report Link Image
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 15859
Enzyme 4 Name Uroporphyrinogen-III methyltransferase/synthase
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name hemD
Enzyme 4 Protein Sequence >Uroporphyrinogen-III methyltransferase/synthase 
MSKKAYIIGAGPGDEELLTLKAINALQKCTAVLYDRLVGNNILNYLNDDCEIYYCGKEPG
CHYKTQEEINESIVELAKKGHIVGRVKGGDPYVFGRGGEEVLALVEENIPFEVIPGVTSP
ISVLNYAGIPITHRGLAQSFHIVTGMSARTLNVNWKALSKENGTLVFMMGLSNLETIVEK
LLENGKDIETPCGVVMRGTTSKQRKVIGTLENICKKVREAKLESPCIIVVGDVVSLNEKL
SWYEKLPLFGANICLTRSKEQSKEIKWKLKELGAEVTEINSIKIKETSENLDEYINTLEK
YDHIVFTSVNAVNVFFDYLVKKRVDIRKIKADFAVLGKATKKALIARGIVPSIMAHSFTA
EGLFEVLKDNIKEGEEVLIPCSSLSREYLFDNLASLGAKCHRVNIYDTICGDVKNPRAFK
EVDMVLYTSPSTVKNMIDMIGLESLKEKVSIAIGPITLKALNESGIEGKMCKTHCGDGFL
SEIEGIWQEVKK
Enzyme 4 Number of Residues 492
Enzyme 4 Molecular Weight 54506.9
Enzyme 4 Theoretical pI 6.90
Enzyme 4 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrinogen-III synthase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole biosynthetic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 4 General Function Involved in methyltransferase activity
Enzyme 4 Specific Function S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 110684371 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q0ST17 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q0ST17_CLOPS Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1479 bp 
ATGAGTAAAAAAGCATATATAATAGGGGCAGGTCCTGGAGATGAAGAGTTATTAACACTT
AAAGCAATAAATGCATTACAAAAATGCACAGCTGTCTTATATGATAGATTAGTTGGAAAC
AATATACTTAATTACTTAAATGATGACTGTGAGATTTACTATTGTGGAAAAGAGCCAGGA
TGTCATTATAAAACACAGGAAGAGATAAATGAAAGTATAGTTGAACTTGCTAAAAAAGGT
CATATTGTTGGTAGAGTAAAAGGTGGAGATCCCTATGTTTTTGGAAGAGGTGGAGAAGAA
GTATTAGCCTTAGTAGAAGAAAACATACCTTTTGAAGTTATTCCAGGGGTTACTTCACCT
ATTTCTGTTTTAAATTATGCAGGGATACCAATAACACATAGAGGATTAGCACAGAGTTTT
CATATTGTAACAGGAATGTCAGCAAGAACTTTAAATGTAAATTGGAAAGCTTTATCAAAA
GAAAATGGAACCTTAGTATTTATGATGGGGCTTTCAAATTTAGAGACAATTGTTGAGAAA
CTTTTAGAAAATGGTAAAGATATAGAAACTCCTTGTGGAGTAGTAATGAGAGGAACAACT
TCAAAGCAAAGAAAGGTTATTGGAACATTAGAAAATATATGTAAAAAGGTTAGAGAAGCT
AAGTTAGAGTCACCTTGTATAATAGTTGTTGGTGATGTTGTTTCATTAAATGAAAAACTT
TCATGGTATGAAAAATTACCTCTATTTGGAGCTAATATTTGTTTAACAAGATCTAAGGAA
CAATCTAAAGAGATTAAGTGGAAATTAAAAGAGTTAGGTGCAGAAGTAACAGAAATAAAC
TCTATAAAAATAAAAGAAACTTCAGAAAATTTAGATGAATATATTAATACTTTAGAAAAA
TATGATCATATAGTATTTACTTCAGTAAATGCTGTTAATGTATTCTTTGATTATTTAGTG
AAAAAAAGAGTTGATATAAGAAAAATAAAAGCAGATTTTGCTGTACTAGGAAAAGCAACT
AAAAAAGCTTTAATAGCTAGAGGAATTGTACCAAGCATAATGGCTCATTCATTTACAGCG
GAAGGTTTATTTGAAGTTTTAAAAGATAATATTAAAGAAGGAGAAGAAGTCTTAATTCCA
TGCTCTTCTTTAAGTAGAGAATATTTGTTTGATAATTTAGCTTCTTTAGGAGCAAAATGT
CATAGAGTTAATATTTATGATACTATATGCGGAGATGTTAAAAATCCAAGAGCTTTCAAG
GAAGTTGATATGGTATTATACACAAGTCCTTCAACGGTTAAAAACATGATTGATATGATT
GGACTTGAATCTCTTAAAGAGAAAGTAAGTATAGCTATAGGACCTATAACCTTAAAAGCT
TTAAATGAAAGTGGAATTGAAGGGAAAATGTGCAAAACACATTGTGGGGATGGATTTTTA
AGTGAAATTGAAGGTATATGGCAAGAGGTTAAAAAATAA
Enzyme 4 GenBank Gene ID CP000312 Link Image
Enzyme 4 GeneCard ID hemD Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus CPR_1421
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 15860
Enzyme 5 Name Siroheme synthase
Enzyme 5 Synonyms
  1. Uroporphyrinogen-III C-methyltransferase
  2. Urogen III methylase
  3. SUMT
  4. Uroporphyrinogen III methylase
  5. UROM
  6. Precorrin-2 dehydrogenase
  7. Sirohydrochlorin ferrochelatase
Enzyme 5 Gene Name cysG
Enzyme 5 Protein Sequence >Siroheme synthase 
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTL
VEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRS
PLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRGRVKQQFATMGERRRFWE
KLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ
QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK
GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHL
KTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVID
GTLTQLGELAQQMNSPSLIIIGRVVGLRDKLNWFSNH
Enzyme 5 Number of Residues 457
Enzyme 5 Molecular Weight 49951.0
Enzyme 5 Theoretical pI 6.13
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 5 General Function Involved in methyltransferase activity
Enzyme 5 Specific Function Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • siroheme + 2 H+ = sirohydrochlorin + Fe2+ [RN:R02864]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 85674542 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P0AEA8 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CYSG_ECOLI Link Image
Enzyme 5 PDB ID 1PJT Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1374 bp 
ATGGAAAGTAAGAACAAGCTAAAGCGTGGGCTAAGTACCCGCCACATACGCTTTATGGCA
CTGGGTTCAGCAATTGGCACCGGGCTGTTTTACGGTTCGGCAGACGCCATCAAAATGGCC
GGTCCGAGCGTGTTGTTGGCCTATATTATCGGTGGTATCGCGGCGTATATCATTATGCGT
GCGCTGGGGGAAATGTCGGTACATAACCCGGCCGCCAGCTCTTTCTCGCGTTATGCGCAG
GAAAACCTCGGCCCGCTGGCAGGTTACATTACCGGCTGGACCTACTGCTTTGAAATCCTT
ATTGTCGCCATCGCCGATGTGACCGCTTTTGGTATCTATATGGGTGTCTGGTTCCCGACG
GTGCCGCACTGGATTTGGGTACTGAGCGTGGTGCTGATCATTTGCGCCGTAAACCTGATG
AGCGTGAAGGTATTCGGTGAGCTGGAATTCTGGTTCTCGTTCTTTAAAGTCGCCACCATC
ATCATCATGATTGTCGCCGGTTTCGGCATCATCATCTGGGGGATTGGCAACGGCGGGCAA
CCGACCGGTATTCATAACCTGTGGAGCAACGGCGGCTTCTTCAGTAACGGCTGGCTTGGC
ATGGTAATGTCGTTGCAAATGGTGATGTTTGCTTACGGTGGGATCGAAATTATCGGGATT
ACCGCCGGTGAAGCGAAAGATCCTGAGAAATCGATACCGCGTGCGATTAACTCCGTGCCG
ATGCGTATTCTGGTGTTCTACGTCGGTACGCTGTTCGTCATTATGTCTATCTACCCGTGG
AATCAGGTTGGCACTGCCGGTAGCCCGTTCGTGCTGACGTTCCAGCATATGGGCATTACC
TTTGCCGCCAGCATTCTTAACTTTGTTGTGCTGACTGCTTCGCTGTCGGCAATTAACAGT
GATGTATTTGGCGTAGGCCGTATGCTCCACGGTATGGCAGAGCAGGGCAGCGCGCCGAAA
ATTTTCAGCAAAACGTCGCGTCGCGGTATTCCGTGGGTTACGGTGCTGGTGATGACTACC
GCGCTGCTGTTTGCGGTGTATCTGAACTACATCATGCCGGAAAACGTCTTCCTGGTGATC
GCTTCGCTGGCAACCTTCGCCACGGTGTGGGTGTGGATTATGATCCTGCTGTCGCAAATT
GCCTTCCGTCGCCGTTTGCCGCCAGAAGAAGTTAAGGCGCTGAAATTTAAAGTGCCGGGT
GGGGTAGCAACGACCATCGGCGGGCTGATTTTCCTGCTCTTTATTATCGGGTTGATTGGT
TATCACCCGGATACGCGTATCTCGCTGTATGTCGGTTTCGCGTGGATTGTTGTGCTGTTG
ATTGGCTGGATGTTTAAACGCCGCCACGATCGTCAGCTGGCTGAAAACCAGTAA
Enzyme 5 GenBank Gene ID AP009048 Link Image
Enzyme 5 GeneCard ID cysG Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus b3368
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Bell AI, Gaston KL, Cole JA, Busby SJ: Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP. Nucleic Acids Res. 1989 May 25;17(10):3865-74. [PubMed Link Image]
  2. Peakman T, Crouzet J, Mayaux JF, Busby S, Mohan S, Harborne N, Wootton J, Nicolson R, Cole J: Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome. Eur J Biochem. 1990 Jul 31;191(2):315-23. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Warren MJ, Stolowich NJ, Santander PJ, Roessner CA, Sowa BA, Scott AI: Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase. FEBS Lett. 1990 Feb 12;261(1):76-80. [PubMed Link Image]
  6. Warren MJ, Roessner CA, Santander PJ, Scott AI: The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase. Biochem J. 1990 Feb 1;265(3):725-9. [PubMed Link Image]
  7. Spencer JB, Stolowich NJ, Roessner CA, Scott AI: The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase. FEBS Lett. 1993 Nov 29;335(1):57-60. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15861
Enzyme 6 Name Putative uroporphyrinogen-III C-methyltransferase
Enzyme 6 Synonyms
  1. Urogen-III methylase
  2. ORF X
Enzyme 6 Gene Name hemX
Enzyme 6 Protein Sequence >Putative uroporphyrinogen-III C-methyltransferase 
MTEQEKTSAVVEETREAVDTTSQPVATEKKSKNNTALILSAVAIAIALAAGIGLYGWGKQ
QAVNQTATSDALANQLTALQKAQESQKAELEGIIKQQAAQLKQANRQQETLAKQLDEVQQ
KVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITV
RRAITDDIASLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDGEELSSSIS
EWRINLQKSWQNFMDNFITIRRRDDTAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEE
TYRQALENVSTWVRAYYDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQAMLEKLMQTR
VRNLLAQPAAGTTEAKPAPAPQADTPAAAPQGE
Enzyme 6 Number of Residues 393
Enzyme 6 Molecular Weight 42962.6
Enzyme 6 Theoretical pI 4.41
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Coenzyme transport and metabolism
Enzyme 6 Specific Function S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • (1) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1 [RN:R07237]
  • (2) S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2 [RN:R07238]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 37-57
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1736416 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P09127 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HEMX_ECOLI Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1182 bp 
ATGACCTGTTCAACTTCATTAAGCGGCAAAAACAGGATTGTCCTTATCGCTGGCATTCTG
ATGATTGCCACAACATTACGCGTCACCTTTACCGGCGCAGCACCGTTACTGGATACGATT
CGTTCCGCTTACTCGCTGACGACAGCGCAAACCGGCTTATTGACCACCCTGCCATTATTG
GCCTTTGCGCTAATCTCACCTTTGGCTGCCCCGGTAGCGCGACGTTTTGGTATGGAACGT
AGCCTGTTTGCCGCGTTACTTTTGATCTGTGCTGGTATCGCAATTCGCTCTCTCCCTTCG
CCTTACTTATTATTTGGCGGTACAGCGGTCATTGGCGGTGGGATTGCATTAGGCAATGTC
TTACTGCCAGGATTAATTAAACGCGATTTCCCTCATTCCGTCGCCAGACTTACCGGCGCA
TATTCCCTGACAATGGGAGCTGCAGCGGCACTGGGATCGGCTATGGTCGTGCCGCTGGCT
TTGAACGGTTTTGGCTGGCAAGGCGCGTTGCTCATGCTGATGTGTTTTCCTCTGCTGGCT
CTTTTTTTATGGCTGCCACAGTGGCGAAGTCAACAACATGCAAATTTGAGTACCTCGCGC
GCCTTACATACTCGGGGTATCTGGCGTTCACCGCTTGCCTGGCAGGTCACATTGTTTCTT
GGGATCAACTCACTGGTCTATTACGTGATTATTGGCTGGCTTCCGGCGATCCTCATCAGT
CACGGCTATAGCGAAGCACAGGCGGGTTCACTGCATGGTTTGCTGCAACTAGCCACAGCA
GCACCCGGTTTGCTGATCCCACTTTTCTTACATCATGTGAAAGATCAGCGTGGTATTGCA
GCGTTCGTTGCCTTGATGTGCGCAGTGGGCGCGGTTGGGCTCTGCTTTATGCCAGCGCAC
GCGATCACCTGGACTCTGCTTTTCGGTTTTGGTTCCGGCGCAACAATGATACTGGGGTTG
ACGTTCATTGGTCTGCGGGCTAGTTCTGCGCATCAGGCGGCGGCACTCTCGGGGATGGCA
CAATCCGTCGGGTATTTGTTGGCAGCCTGTGGGCCGCCGCTGATGGGTAAAATACACGAT
GCTAACGGTAACTGGTCTGTACCACTTATGGGTGTTGCCATACTTTCACTACTGATGGCG
ATTTTCGGACTTTGCGCCGGGAGAGACAAAGAAATTCGCTAA
Enzyme 6 GenBank Gene ID AP009048 Link Image
Enzyme 6 GeneCard ID hemX Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus b3803
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Sasarman A, Echelard Y, Letowski J, Tardif D, Drolet M: Nucleotide sequence of the hemX gene, the third member of the Uro operon of Escherichia coli K12. Nucleic Acids Res. 1988 Dec 23;16(24):11835. [PubMed Link Image]
  2. Alefounder PR, Abell C, Battersby AR: The sequence of hemC, hemD and two additional E. coli genes. Nucleic Acids Res. 1988 Oct 25;16(20):9871. [PubMed Link Image]
  3. Daniels DL, Plunkett G 3rd, Burland V, Blattner FR: Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science. 1992 Aug 7;257(5071):771-8. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed Link Image]
  7. Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO: Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005 Oct 14;280(41):34409-19. Epub 2005 Aug 3. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16700
Enzyme 7 Name Siroheme synthase
Enzyme 7 Synonyms
  1. Uroporphyrinogen-III C-methyltransferase
  2. Urogen III methylase
  3. SUMT
  4. Uroporphyrinogen III methylase
  5. UROM
  6. Precorrin-2 dehydrogenase
  7. Sirohydrochlorin ferrochelatase
Enzyme 7 Gene Name cysG
Enzyme 7 Protein Sequence >Siroheme synthase 
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTL
VEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRS
PLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRGRVKQQFATMGERRRFWE
KLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ
QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK
GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHL
KTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVID
GTLTQLGELAQQMNSPSLIIIGRVVGLRDKLNWFSNH
Enzyme 7 Number of Residues 457
Enzyme 7 Molecular Weight 49951.0
Enzyme 7 Theoretical pI 6.13
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 7 General Function Involved in methyltransferase activity
Enzyme 7 Specific Function Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • siroheme + 2 H+ = sirohydrochlorin + Fe2+ [RN:R02864]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 169887823 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID B1X716 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CYSG_ECODH Link Image
Enzyme 7 PDB ID 1PJT Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1374 bp 
ATGGAAAGTAAGAACAAGCTAAAGCGTGGGCTAAGTACCCGCCACATACGCTTTATGGCA
CTGGGTTCAGCAATTGGCACCGGGCTGTTTTACGGTTCGGCAGACGCCATCAAAATGGCC
GGTCCGAGCGTGTTGTTGGCCTATATTATCGGTGGTATCGCGGCGTATATCATTATGCGT
GCGCTGGGGGAAATGTCGGTACATAACCCGGCCGCCAGCTCTTTCTCGCGTTATGCGCAG
GAAAACCTCGGCCCGCTGGCAGGTTACATTACCGGCTGGACCTACTGCTTTGAAATCCTT
ATTGTCGCCATCGCCGATGTGACCGCTTTTGGTATCTATATGGGTGTCTGGTTCCCGACG
GTGCCGCACTGGATTTGGGTACTGAGCGTGGTGCTGATCATTTGCGCCGTAAACCTGATG
AGCGTGAAGGTATTCGGTGAGCTGGAATTCTGGTTCTCGTTCTTTAAAGTCGCCACCATC
ATCATCATGATTGTCGCCGGTTTCGGCATCATCATCTGGGGGATTGGCAACGGCGGGCAA
CCGACCGGTATTCATAACCTGTGGAGCAACGGCGGCTTCTTCAGTAACGGCTGGCTTGGC
ATGGTAATGTCGTTGCAAATGGTGATGTTTGCTTACGGTGGGATCGAAATTATCGGGATT
ACCGCCGGTGAAGCGAAAGATCCTGAGAAATCGATACCGCGTGCGATTAACTCCGTGCCG
ATGCGTATTCTGGTGTTCTACGTCGGTACGCTGTTCGTCATTATGTCTATCTACCCGTGG
AATCAGGTTGGCACTGCCGGTAGCCCGTTCGTGCTGACGTTCCAGCATATGGGCATTACC
TTTGCCGCCAGCATTCTTAACTTTGTTGTGCTGACTGCTTCGCTGTCGGCAATTAACAGT
GATGTATTTGGCGTAGGCCGTATGCTCCACGGTATGGCAGAGCAGGGCAGCGCGCCGAAA
ATTTTCAGCAAAACGTCGCGTCGCGGTATTCCGTGGGTTACGGTGCTGGTGATGACTACC
GCGCTGCTGTTTGCGGTGTATCTGAACTACATCATGCCGGAAAACGTCTTCCTGGTGATC
GCTTCGCTGGCAACCTTCGCCACGGTGTGGGTGTGGATTATGATCCTGCTGTCGCAAATT
GCCTTCCGTCGCCGTTTGCCGCCAGAAGAAGTTAAGGCGCTGAAATTTAAAGTGCCGGGT
GGGGTAGCAACGACCATCGGCGGGCTGATTTTCCTGCTCTTTATTATCGGGTTGATTGGT
TATCACCCGGATACGCGTATCTCGCTGTATGTCGGTTTCGCGTGGATTGTTGTGCTGTTG
ATTGGCTGGATGTTTAAACGCCGCCACGATCGTCAGCTGGCTGAAAACCAGTAA
Enzyme 7 GenBank Gene ID CP000948 Link Image
Enzyme 7 GeneCard ID cysG Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus ECDH10B_3544
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available