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Human Metabolome Database Version 2.5

 

Showing metabocard for D-4'-Phosphopantothenate (HMDB01016)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-12 12:06:31
Accession Number HMDB01016
Secondary Accession Numbers Not Available
Common Name D-4'-Phosphopantothenate
Description HMDB01016 D-4'-Phosphopantothenate is a product of enzyme pantothenate kinase [EC 2.7.1.33] in pantothenate and CoA biosynthesis pathway (KEGG).
Synonyms
  1. (R)-4'-phosphopantothenate
  2. 4'-P-Pantothenate
  3. 4'-phosphopantothenate
  4. D-4'-Phosphopantothenate
  5. D-4'-Phosphopantothenic acid
Chemical IUPAC Name 3-(2-hydroxy-3,3-dimethyl-4-phosphonooxy-butanoyl)aminopropanoic acid
Chemical Formula C9H18NO8P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acid Phosphates
  • Amino Ketones
Sub Class
  • Non-protetypic phospho-amino acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • secondary carboxylic acid amide
  • phosphoric acid ester
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 299.215
Monoisotopic Molecular Weight 299.076996
Isomeric SMILES CC(C)(COP(O)(O)=O)C(O)C(=O)NCCC(O)=O
Canonical SMILES CC(C)(COP(O)(O)=O)C(O)C(=O)NCCC(O)=O
KEGG Compound ID C03492 Link Image
BioCyc ID 4-P-PANTOTHENATE Link Image
BiGG ID 41952 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01016 Link Image
Metagene Link HMDB01016 Link Image
METLIN ID 3427 Link Image
PubChem Compound 41635 Link Image
PubChem Substance 6304 Link Image
ChEBI ID 15905 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C9H18NO8P/c1-9(2,5-18-19(15,16)17)7(13)8(14)10-4-3-6(11)12/h7,13H,3-5H2,1-2H3,(H,10,14)(H,11,12)(H2,15,16,17)
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.09 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.52 [Predicted by ALOGPS]; -2.6 [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 Not Available
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 (Predicted from LogP)
  • mitochondria
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
Pantothenate and CoA Biosynthesis SMP00027 Link Image map00770 Link Image
General References Not Available
Metabolic Enzymes
  1. Pantothenate kinase 4
  2. Pantothenate kinase 2, mitochondrial
  3. Pantothenate kinase 1
  4. Pantothenate kinase 3
  5. Phosphopantothenoylcysteine synthetase
  6. Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c)
Enzyme 1 [top]
Enzyme 1 ID 6312
Enzyme 1 Name Pantothenate kinase 4
Enzyme 1 Synonyms
  1. hPanK4
  2. Pantothenic acid kinase 4
Enzyme 1 Gene Name PANK4
Enzyme 1 Protein Sequence >Pantothenate kinase 4
MAECGASGSGSSGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAK
VRSFDHSGKDTEREHEPPYEISVQEEITARLHFIKFENTYIEACLDFIKDHLVNTETKVI
QATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQ
TNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLH
LASRGQHSNVDMLVRDVYGGAHQTLGLSGNLIASSFGKSATADQEFSKEDMAKSLLHMIS
NDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLG
AIGAFLKGAEQDNPNQYSWGENYAGSSGLMSASPELGPAQRARSGTFDLLEMDRLERPLV
DLPLLLDPPSYVPDTVDLTDDALARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKF
RQKYWNKLQTLRQQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPG
VVRSLDALGWEERQLALVKGLLAGNVFDWGAKAVSAVLESDPYFGFEEAKRKLQERPWLV
DSYSEWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALNDV
THSESLIVAERIAGMDPVVHSALQEERLLLVQTGSSSPCLDLSRLDKGLAALVRERGADL
VVIEGMGRAVHTNYHAALRCESLKLAVIKNAWLAERLGGRLFSVIFKYEVPAE
Enzyme 1 Number of Residues 773
Enzyme 1 Molecular Weight 85990.1
Enzyme 1 Theoretical pI 6.22
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • pantothenate kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • coenzyme A biosynthetic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
Component
Enzyme 1 General Function Involved in pantothenate kinase activity
Enzyme 1 Specific Function Plays a role in the physiological regulation of the intracellular CoA concentration
Enzyme 1 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 1 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 7023024 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NVE7 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PANK4_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2322 bp
ATGGCGGAGTGTGGAGCGAGCGGCAGCGGGAGCAGCGGGGACAGTCTGGACAAGAGCATC
ACGCTGCCCCCCGACGAGATCTTCCGCAACCTGGAGAACGCCAAGCGCTTCGCCATCGAC
ATAGGCGGGTCGTTAACCAAGCTGGCCTACTATTCAACGGTACAGCACAAAGTCGCCAAG
GTGCGGTCTTTCGACCACTCCGGAAAGGACACAGAACGTGAACATGAGCCGCCCTATGAG
ATTTCAGTTCAAGAAGAGATCACTGCTCGACTGCACTTCATTAAGTTTGAGAATACCTAC
ATCGAAGCCTGCCTGGACTTCATCAAAGACCATCTCGTCAACACAGAGACCAAGGTCATC
CAGGCGACCGGGGGCGGGGCCTACAAGTTCAAGGACCTCATCGAAGAGAAGCTGCGGCTG
AAAGTCGACAAGGAGGACGTGATGACGTGCCTGATTAAGGGGTGCAACTTCGTGCTCAAG
AACATCCCCCATGAGGCCTTCGTGTACCAGAAGGATTCCGACCCTGAGTTCCGGTTCCAG
ACCAACCACCCCCACATTTTCCCCTATCTTCTTGTCAATATCGGCTCTGGAGTCTCCATC
GTGAAGGTGGAGACGGAGGACAGGTTCGAGTGGGTCGGCGGCAGCTCCATTGGAGGCGGC
ACCTTCTGGGGGCTTGGCGCTCTGCTCACCAAAACGAAGAAGTTTGACGAGCTCCTGCAC
CTGGCCTCGAGGGGCCAGCACAGCAATGTGGACATGCTGGTGCGGGACGTCTACGGCGGC
GCCCACCAGACTCTCGGGCTGAGCGGGAACCTCATCGCCAGCAGCTTCGGGAAGTCGGCC
ACCGCCGACCAAGAGTTCTCCAAAGAAGACATGGCGAAGAGCCTGCTGCACATGATCAGC
AACGACATTGGGCAGCTGGCCTGCCTCCACGCACGGCTGCACAGCCTGGACCGCGTGTAC
TTTGGAGGCTTCTTTATCCGGGGCCACCCCGTGACCATGCGCACCATCACCTATAGCATC
AACTTCTTCTCCAAGGGGGAAGTGCAGGCGCTGTTTCTGAGGCACGAAGGCTACCTGGGA
GCCATCGGAGCGTTCCTGAAAGGAGCTGAGCAGGACAATCCTAACCAGTACAGCTGGGGA
GAGAACTATGCAGGCAGCTCCGGGCTGATGAGTGCATCACCCGAGCTCGGCCCGGCGCAG
CGGGCGCGGAGTGGCACTTTTGACTTGCTGGAAATGGACCGGCTGGAGAGGCCACTGGTT
GACCTGCCGCTCCTCCTGGACCCGCCCTCCTACGTGCCCGACACGGTGGACCTCACCGAT
GACGCTCTGGCCCGAAAATACTGGCTCACCTGCTTTGAGGAGGCCCTGGACGGGGTAGTG
AAGCGCGCAGTGGCGAGCCAGCCAGACTCTGTGGATGCAGCCGAGAGGGCGGAGAAGTTC
CGGCAGAAGTACTGGAACAAGCTTCAGACCCTGAGGCAGCAGCCCTTCGCCTATGGGACC
CTGACCGTGCGCAGCCTGCTGGACACCAGGGAGCACTGTCTGAACGAGTTCAACTTCCCG
GATCCCTACTCCAAAGTGAAGCAGCGGGAGAATGGCGTGGCGCTGAGGTGCTTCCCCGGG
GTCGTGCGCTCCCTGGACGCGCTGGGCTGGGAGGAACGGCAGCTGGCGCTGGTGAAAGGC
CTCCTGGCGGGGAATGTCTTCGACTGGGGGGCCAAAGCCGTGTCTGCTGTCCTTGAATCC
GACCCCTACTTTGGGTTTGAAGAAGCAAAGAGGAAGTTACAAGAAAGACCCTGGCTCGTG
GATTCCTACAGCGAGTGGCTTCAGAGATTAAAGGGGCCCCCTCATAAATGTGCCTTAATT
TTCGCAGATAACAGTGGAATAGACATCATTTTGGGAGTCTTCCCCTTTGTCAGGGAGCTA
CTCCTTAGAGGGACAGAGGTCATCCTGGCGTGCAACTCAGGCCCCGCCCTGAACGACGTG
ACCCACAGCGAGTCCCTCATCGTGGCAGAGCGTATTGCGGGCATGGACCCTGTCGTGCAC
TCTGCGCTCCAGGAAGAGAGGCTGCTGCTGGTGCAGACGGGCTCCAGCTCCCCGTGCCTC
GACCTCAGCCGCCTGGATAAGGGGCTGGCCGCACTGGTGCGGGAGCGTGGCGCGGATCTG
GTGGTCATCGAGGGCATGGGCCGTGCTGTCCACACAAACTACCACGCAGCCCTGCGCTGC
GAGAGCCTCAAGCTGGCCGTCATCAAGAACGCGTGGCTGGCCGAGCGGCTGGGCGGCCGG
CTCTTCAGCGTCATCTTCAAGTACGAGGTCCCAGCCGAGTGA
Enzyme 1 GenBank Gene ID AK001644 Link Image
Enzyme 1 GeneCard ID PANK4 Link Image
Enzyme 1 GenAtlas ID PANK4 Link Image
Enzyme 1 HGNC ID HGNC:19366 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p36.32
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [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. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6313
Enzyme 2 Name Pantothenate kinase 2, mitochondrial
Enzyme 2 Synonyms
  1. hPanK2
  2. Pantothenic acid kinase 2
Enzyme 2 Gene Name PANK2
Enzyme 2 Protein Sequence >Pantothenate kinase 2, mitochondrial
MRRLGPFHPRVHWAAPPSLSSGLHRLLFLRGTRIPSSTTLSPPRHDSLSLDGGTVNPPRV
REPTGREAFGPSPASSDWLPARWRNGRGGRPRARLCSGWTAAEEARRNPTLGGLLGRQRL
LLRMGGGRLGAPMERHGRASATSVSSAGEQAAGDPEGRRQEPLRRRASSASVPAVGASAE
GTRRDRLGSYSGPTSVSRQRVESLRKKRPLFPWFGLDIGGTLVKLVYFEPKDITAEEEEE
EVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDMPAFIQMGR
DKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQC
YYFENPADSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFG
LCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEK
REAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDY
WSKGQLKALFSEHEGYFGAVGALLELLKIP
Enzyme 2 Number of Residues 570
Enzyme 2 Molecular Weight 62679.9
Enzyme 2 Theoretical pI 9.64
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • pantothenate kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • coenzyme A biosynthetic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
Component
Enzyme 2 General Function Involved in pantothenate kinase activity
Enzyme 2 Specific Function May be the master regulator of the CoA biosynthesis
Enzyme 2 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 2 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 23452046 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BZ23 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PANK2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1713 bp
ATGAGGAGGCTCGGGCCCTTCCACCCACGCGTCCATTGGGCGGCGCCGCCATCACTCTCT
TCTGGGCTACACCGCCTTCTCTTCCTCCGCGGAACCCGGATCCCCTCCTCCACCACCCTC
TCCCCGCCCCGTCACGATAGCCTCTCATTGGACGGAGGCACGGTCAATCCTCCTCGAGTT
AGGGAGCCGACTGGACGCGAGGCCTTTGGGCCGTCCCCAGCCTCGTCGGATTGGCTTCCT
GCGCGTTGGCGCAACGGAAGAGGCGGCCGGCCGAGGGCGCGCCTCTGCTCTGGCTGGACC
GCCGCGGAGGAGGCGAGAAGGAATCCGACGCTGGGGGGCTTGCTCGGGCGGCAGCGACTG
CTGCTGCGGATGGGAGCGGGCCGGCTCGGCGCGCCCATGGAGCGCCACGGCAGGGCTTCC
GCCACCTCCGTCTCGTCGGCTGGGGAGCAGGCGGCCGGGGACCCCGAAGGGCGGCGGCAG
GAGCCACTGCGGCGCCGGGCGAGCAGCGCGTCGGTGCCCGCGGTCGGGGCCTCGGCTGAG
GGCACGAGGCGGGATCGACTGGGCTCTTACAGCGGCCCCACCTCGGTCTCCCGCCAGCGC
GTCGAAAGCCTGAGGAAAAAGCGGCCGCTTTTTCCATGGTTTGGACTGGATATCGGTGGA
ACTCTGGTCAAGCTGGTATATTTTGAACCCAAAGACATCACTGCTGAAGAAGAAGAGGAA
GAGGTGGAAAGTCTTAAAAGTATTCGGAAGTACCTGACCTCCAATGTGGCTTATGGGTCT
ACAGGCATTCGGGACGTGCACCTCGAGCTGAAGGACCTGACTCTGTGTGGACGCAAAGGC
AATCTGCACTTTATACGCTTTCCCACTCATGACATGCCTGCTTTTATTCAAATGGGCAGA
GATAAAAACTTCTCGAGTCTCCACACTGTCTTTTGTGCCACTGGAGGTGGAGCGTACAAA
TTTGAGCAGGATTTTCTCACAATAGGTGATCTTCAGCTTTGCAAACTGGATGAACTAGAT
TGCTTGATCAAAGGAATTTTATACATTGACTCAGTCGGATTCAATGGACGGTCACAGTGC
TATTACTTTGAAAACCCTGCTGATTCTGAAAAGTGTCAGAAGTTACCATTTGATTTGAAA
AATCCGTATCCTCTGCTTCTGGTGAACATTGGCTCAGGGGTTAGCATCTTAGCAGTATAT
TCCAAAGATAATTACAAACGGGTCACAGGTACTAGTCTTGGAGGAGGAACTTTTTTTGGT
CTCTGCTGTCTTCTTACTGGCTGTACCACTTTTGAAGAAGCTCTTGAAATGGCATCTCGT
GGAGATAGCACCAAAGTGGATAAACTAGTACGAGATATTTATGGAGGGGACTATGAGAGG
TTTGGACTGCCAGGCTGGGCTGTGGCTTCAAGCTTTGGAAACATGATGAGCAAGGAGAAG
CGAGAGGCTGTCAGTAAAGAGGACCTGGCCAGAGCGACTTTGATCACCATCACCAACAAC
ATTGGCTCAATAGCAAGAATGTGTGCCCTTAATGAAAACATTAACCAGGTGGTATTTGTT
GGAAATTTCTTGAGAATTAATACGATCGCCATGCGGCTTTTGGCATATGCTTTGGATTAT
TGGTCCAAGGGGCAGTTGAAAGCACTTTTTTCGGAACACGAGGGTTATTTTGGAGCTGTT
GGAGCACTCCTTGAGCTGTTGAAGATCCCGTGA
Enzyme 2 GenBank Gene ID AF494409 Link Image
Enzyme 2 GeneCard ID PANK2 Link Image
Enzyme 2 GenAtlas ID PANK2 Link Image
Enzyme 2 HGNC ID HGNC:15894 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 20p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hortnagel K, Prokisch H, Meitinger T: An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. Hum Mol Genet. 2003 Feb 1;12(3):321-7. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Ching KH, Westaway SK, Gitschier J, Higgins JJ, Hayflick SJ: HARP syndrome is allelic with pantothenate kinase-associated neurodegeneration. Neurology. 2002 Jun 11;58(11):1673-4. [PubMed Link Image]
  12. Hayflick SJ, Westaway SK, Levinson B, Zhou B, Johnson MA, Ching KH, Gitschier J: Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome. N Engl J Med. 2003 Jan 2;348(1):33-40. [PubMed Link Image]
  13. Nicholas AP, Earnst KS, Marson DC: Atypical Hallervorden-Spatz disease with preserved cognition and obtrusive obsessions and compulsions. Mov Disord. 2005 Jul;20(7):880-6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6314
Enzyme 3 Name Pantothenate kinase 1
Enzyme 3 Synonyms
  1. hPanK
  2. hPanK1
  3. Pantothenic acid kinase 1
Enzyme 3 Gene Name PANK1
Enzyme 3 Protein Sequence >Pantothenate kinase 1
MLKLVGGGGGQDWACSVAGTSLGGEEAAFEVARPGDQGKAGGGSPGWGCAGIPDSAPGAG
VLQAGAVGPARGGQGAEEVGESAGGGEERRVRHPQAPALRLLNRKPQGGSGEIKTPENDL
QRGRLSRGPRTAPPAPGMGDRSGQQERSVPHSPGAPVGTSAAAVNGLLHNGFHPPPVQPP
HVCSRGPVGGSDAAPQRLPLLPELQPQPLLPQHDSPAKKCRLRRRMDSGRKNRPPFPWFG
MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTM
CGRKGNLHFIRFPSCAMHRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHK
LDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKKPYCLDNPYPMLLVNMGSGVS
ILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYG
GDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENID
RVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALLELFKMTDDK
Enzyme 3 Number of Residues 598
Enzyme 3 Molecular Weight 64338.9
Enzyme 3 Theoretical pI 7.61
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • pantothenate kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • coenzyme A biosynthetic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
Component
Enzyme 3 General Function Involved in pantothenate kinase activity
Enzyme 3 Specific Function Plays a role in the physiological regulation of the intracellular CoA concentration
Enzyme 3 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 3 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 23510400 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TE04 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PANK1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1797 bp
ATGTTGAAACTCGTCGGTGGCGGTGGCGGGCAGGACTGGGCATGCTCAGTGGCGGGGACC
AGTCTGGGAGGCGAGGAAGCCGCGTTTGAAGTCGCGCGGCCTGGGGATCAGGGGAAGGCG
GGCGGCGGGAGCCCCGGCTGGGGGTGCGCGGGGATCCCCGATTCCGCGCCCGGGGCTGGC
GTGCTCCAGGCCGGCGCCGTGGGGCCGGCGCGCGGGGGGCAGGGCGCAGAGGAGGTGGGG
GAGTCGGCAGGAGGAGGGGAGGAGCGCCGGGTTCGCCATCCCCAGGCGCCGGCTCTGCGG
CTGCTGAATCGGAAGCCGCAGGGAGGATCCGGGGAAATAAAGACGCCGGAGAATGACCTC
CAGCGAGGCCGCCTGAGCCGGGGCCCGCGCACAGCCCCGCCAGCCCCCGGCATGGGCGAC
CGCAGCGGGCAGCAGGAGCGCTCGGTCCCGCACTCTCCAGGGGCCCCCGTGGGCACCAGC
GCCGCCGCTGTGAACGGGCTGCTGCACAACGGCTTCCATCCGCCGCCAGTCCAGCCGCCG
CACGTCTGCAGCCGGGGTCCAGTGGGCGGCAGCGACGCGGCGCCCCAGCGCCTCCCGCTC
CTGCCGGAGCTGCAGCCGCAGCCACTGCTCCCTCAGCATGACTCCCCGGCCAAGAAATGC
CGGCTGCGGAGGAGGATGGACTCGGGGAGAAAGAACAGGCCGCCATTCCCATGGTTTGGC
ATGGACATCGGTGGAACGCTGGTTAAATTGGTGTATTTCGAGCCGAAGGATATTACAGCC
GAAGAGGAGCAAGAGGAAGTGGAGAACCTGAAGAGCATCCGGAAGTATTTGACTTCTAAT
ACTGCTTATGGGAAAACTGGGATCCGAGACGTCCACCTGGAACTGAAAAACCTGACCATG
TGTGGACGCAAAGGGAACCTGCACTTCATCCGCTTTCCCAGCTGTGCTATGCACAGGTTC
ATTCAGATGGGCAGCGAGAAGAACTTCTCTAGCCTTCACACCACCCTCTGTGCCACAGGA
GGCGGGGCTTTCAAATTCGAAGAGGACTTCAGAATGATTGCTGACCTGCAGCTGCATAAA
CTGGATGAACTGGACTGTCTGATTCAGGGCCTGCTTTATGTCGACTCTGTTGGCTTCAAC
GGCAAGCCAGAATGTTACTATTTTGAAAATCCCACAAATCCTGAATTGTGTCAAAAAAAG
CCGTACTGCCTTGATAACCCATACCCTATGTTGCTGGTTAACATGGGCTCAGGTGTCAGC
ATTCTAGCCGTGTACTCCAAGGACAACTATAAAAGAGTTACAGGGACCAGTCTTGGAGGT
GGAACATTCCTAGGCCTATGTTGCTTGCTGACTGGTTGTGAGACCTTTGAAGAAGCTCTG
GAAATGGCAGCTAAAGGCGACAGCACCAATGTTGATAAACTGGTGAAGGACATTTACGGA
GGAGACTATGAACGATTTGGCCTTCAAGGATCTGCTGTAGCATCAAGCTTTGGCAACATG
ATGAGTAAAGAAAAGCGAGATTCCATCAGCAAGGAAGACCTCGCCCGGGCCACATTGGTC
ACCATCACCAACAACATTGGCTCCATTGCTCGGATGTGCGCGTTGAATGAGAACATAGAC
AGAGTTGTGTTTGTTGGAAATTTTCTCAGAATCAATATGGTCTCCATGAAGCTGCTGGCA
TATGCCATGGATTTTTGGTCCAAAGGACAACTGAAAGCTCTGTTTTTGGAACATGAGGGT
TATTTTGGAGCCGTTGGGGCACTGTTGGAACTGTTCAAAATGACTGATGACAAGTAG
Enzyme 3 GenBank Gene ID NM_148977.1 Link Image
Enzyme 3 GeneCard ID PANK1 Link Image
Enzyme 3 GenAtlas ID PANK1 Link Image
Enzyme 3 HGNC ID HGNC:8598 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 10q23.31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ni X, Ma Y, Cheng H, Jiang M, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human pantothenate kinase gene. Int J Biochem Cell Biol. 2002 Feb;34(2):109-15. [PubMed Link Image]
  2. Ramaswamy G, Karim MA, Murti KG, Jackowski S: PPARalpha controls the intracellular coenzyme A concentration via regulation of PANK1alpha gene expression. J Lipid Res. 2004 Jan;45(1):17-31. Epub 2003 Oct 1. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. 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]
  5. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6315
Enzyme 4 Name Pantothenate kinase 3
Enzyme 4 Synonyms
  1. hPanK3
  2. Pantothenic acid kinase 3
Enzyme 4 Gene Name PANK3
Enzyme 4 Protein Sequence >Pantothenate kinase 3
MKIKDAKKPSFPWFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGS
TGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTFIQMGRDKNFSTLQTVLCATGGGAYK
FEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKMPFNLD
DPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASK
GDSTQADKLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNN
IGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAV
GALLGLPNFS
Enzyme 4 Number of Residues 370
Enzyme 4 Molecular Weight 41093.7
Enzyme 4 Theoretical pI 6.52
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • pantothenate kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • coenzyme A biosynthetic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
Component
Enzyme 4 General Function Involved in pantothenate kinase activity
Enzyme 4 Specific Function Plays a role in the physiological regulation of the intracellular CoA concentration
Enzyme 4 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 4 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 10434655 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9H999 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PANK3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1113 bp
ATGAAGATCAAAGATGCCAAGAAACCCTCTTTCCCATGGTTTGGCATGGACATTGGGGGA
ACTCTAGTAAAGCTCTCGTACTTTGAACCTATTGATATCACAGCAGAGGAAGAGCAAGAA
GAAGTTGAGAGTTTAAAAAGTATTCGGAAATATTTGACTTCTAACGTGGCATATGGATCC
ACCGGCATTCGGGATGTACACCTTGAACTGAAAGATTTAACACTTTTTGGCCGAAGAGGG
AACTTGCACTTTATCAGGTTTCCAACCCAGGACCTGCCTACTTTTATCCAAATGGGAAGA
GATAAAAACTTCTCAACATTGCAGACGGTGCTATGTGCTACAGGAGGTGGTGCTTACAAG
TTTGAAAAAGATTTTCGCACAATTGGAAACCTCCACCTGCACAAACTGGATGAACTTGAC
TGCCTTGTAAAGGGCTTGCTGTATATAGACTCTGTCAGTTTCAATGGACAAGCCGAGTGC
TATTATTTTGCTAATGCCTCAGAACCTGAGCGATGCCAAAAGATGCCTTTTAACCTGGAT
GATCCCTATCCACTGCTTGTAGTGAACATTGGCTCAGGAGTCAGTATTTTAGCAGTCCAT
TCCAAAGACAACTATAAACGAGTGACTGGGACAAGCCTTGGAGGGGGTACCTTTCTGGGT
TTATGCAGTTTATTGACTGGCTGTGAAAGTTTTGAAGAGGCTCTTGAAATGGCATCCAAA
GGTGATAGCACACAAGCTGACAAGCTGGTCCGTGATATTTATGGAGGAGATTATGAAAGA
TTTGGTTTGCCAGGTTGGGCTGTAGCATCTAGTTTTGGGAATATGATTTATAAGGAGAAG
CGAGAATCTGTTAGTAAAGAAGATCTGGCAAGAGCTACTTTAGTTACTATCACCAATAAC
ATTGGTTCTGTGGCACGAATGTGTGCTGTTAATGAGAAAATAAACAGAGTTGTCTTTGTT
GGAAACTTTTTACGTGTCAATACCCTCTCAATGAAACTTTTGGCATATGCACTGGATTAC
TGGTCAAAAGGTCAACTAAAAGCATTGTTTCTAGAACATGAGGGTTACTTTGGAGCAGTT
GGTGCACTTCTTGGGCTGCCAAATTTCAGCTAA
Enzyme 4 GenBank Gene ID AK022961 Link Image
Enzyme 4 GeneCard ID PANK3 Link Image
Enzyme 4 GenAtlas ID PANK3 Link Image
Enzyme 4 HGNC ID HGNC:19365 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5q34
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. 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]
  3. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8529
Enzyme 5 Name Phosphopantothenoylcysteine synthetase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PPCS
Enzyme 5 Protein Sequence >Phosphopantothenoylcysteine synthetase
MFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLE
TDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEE
KIVDNLQSRHTAFIGDRN
Enzyme 5 Number of Residues 138
Enzyme 5 Molecular Weight 15645.0
Enzyme 5 Theoretical pI 5.71
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 55665120 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q5VVM0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q5VVM0_HUMAN Link Image
Enzyme 5 PDB ID 1P9O Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >417 bp
ATGTTTTACCTGGCTGCGGCTGTGTCAGATTTCTATGTTCCTGTCTCTGAAATGCCTGAA
CACAAGATCCAGTCATCTGGGGGCCCACTGCAGATAACAATGAAGATGGTGCCAAAACTG
CTTTCTCCTTTGGTTAAAGATTGGGCTCCCAAAGCATTTATAATTTCCTTTAAGTTGGAG
ACTGACCCCGCCATTGTAATTAATCGAGCTCGGAAGGCTTTGGAAATTTATCAGCATCAA
GTGGTGGTGGCTAATATCCTTGAGTCACGACAGTCCTTTGTGTTTATTGTAACCAAAGAC
TCGGAAACCAAGTTATTGCTATCAGAGGAAGAAATAGAAAAAGGCGTAGAGATAGAAGAG
AAGATAGTGGATAATCTTCAGTCTCGACACACAGCTTTTATAGGTGACAGAAACTGA
Enzyme 5 GenBank Gene ID AL445669 Link Image
Enzyme 5 GeneCard ID PPCS Link Image
Enzyme 5 GenAtlas ID PPCS Link Image
Enzyme 5 HGNC ID HGNC:25686 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p34.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16513
Enzyme 6 Name Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name PANK2
Enzyme 6 Protein Sequence >Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c)
MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDS
VGFNGRSQCYYFENPADSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGT
SLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASS
FGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM
RLLAYALDYWSKGQLKALFSEHEGYFGAVGALLELLKIP
Enzyme 6 Number of Residues 279
Enzyme 6 Molecular Weight 30754
Enzyme 6 Theoretical pI 5.88
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • pantothenate kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • coenzyme A biosynthesis
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B1AK33 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B1AK33_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AL353194 Link Image
Enzyme 6 GeneCard ID B1AK33 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 20
Enzyme 6 Locus 20p13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available