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Showing Protein Carbonic anhydrase 1 (HMDBP02057)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 26 metabolites
Identification
HMDB Protein ID HMDBP02057
Secondary Accession Numbers
  • 7536
Name Carbonic anhydrase 1
Synonyms
  1. CA-I
  2. CAB
  3. Carbonate dehydratase I
  4. Carbonic anhydrase B
  5. Carbonic anhydrase I
Gene Name CA1
Protein Type Unknown
Biological Properties
General Function Involved in carbonate dehydratase activity
Specific Function Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.
Pathways
  • Betazole Action Pathway
  • Cimetidine Action Pathway
  • Esomeprazole Action Pathway
  • Famotidine Action Pathway
  • Gastric Acid Production
  • Lafutidine H2-Antihistamine Action
  • Lansoprazole Action Pathway
  • Metiamide Action Pathway
  • Nizatidine Action Pathway
  • Omeprazole Action Pathway
  • Pantoprazole Action Pathway
  • Pirenzepine Action Pathway
  • Rabeprazole Action Pathway
  • Ranitidine Action Pathway
  • Roxatidine acetate Action Pathway
Reactions
Hydrogen carbonate → CO(2) + Water details
Hydrogen carbonate → Carbon dioxide + Water details
GO Classification
Biological Process
small molecule metabolic process
bicarbonate transport
one-carbon metabolic process
Cellular Component
cytosol
Golgi apparatus
Component
cell part
intracellular part
cytoplasm
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
carbonate dehydratase activity
transition metal ion binding
zinc ion binding
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
Molecular Function
metal ion binding
zinc ion binding
carbonate dehydratase activity
Process
metabolic process
cellular metabolic process
one-carbon metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 8
Locus 8q21.2
SNPs CA1
Gene Sequence 
>786 bp
ATGGCAAGTCCAGACTGGGGATATGATGACAAAAATGGTCCTGAACAATGGAGCAAGCTG
TATCCCATTGCCAATGGAAATAACCAATCCCCTGTTGATATTAAAACCAGTGAAACCAAA
CATGACACCTCTCTGAAACCTATTAGTGTCTCCTACAACCCAGCCACAGCCAAAGAAATT
ATCAATGTGGGGCATTCTTTCCATGTAAATTTTGAGGACAACGATAACCGATCAGTGCTG
AAAGGTGGTCCTTTCTCTGACAGCTACAGGCTCTTTCAGTTTCATTTTCACTGGGGCAGT
ACAAATGAGCATGGTTCAGAACATACAGTGGATGGAGTCAAATATTCTGCCGAGCTTCAC
GTAGCTCACTGGAATTCTGCAAAGTACTCCAGCCTTGCTGAAGCTGCCTCAAAGGCTGAT
GGTTTGGCAGTTATTGGTGTTTTGATGAAGGTTGGTGAGGCCAACCCAAAGCTGCAGAAA
GTACTTGATGCCCTCCAAGCAATTAAAACCAAGGGCAAACGAGCCCCATTCACAAATTTT
GACCCCTCTACTCTCCTTCCTTCATCCCTGGATTTCTGGACCTACCCTGGCTCTCTGACT
CATCCTCCTCTTTATGAGAGTGTAACTTGGATCATCTGTAAGGAGAGCATCAGTGTCAGC
TCAGAGCAGCTGGCACAATTCCGCAGCCTTCTATCAAATGTTGAAGGTGATAACGCTGTC
CCCATGCAGCACAACAACCGCCCAACCCAACCTCTGAAGGGCAGAACAGTGAGAGCTTCA
TTTTGA
Protein Properties
Number of Residues 261
Molecular Weight 28870.0
Theoretical pI 7.117
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Carbonic anhydrase 1
MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEI
INVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELH
VAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNF
DPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
GenBank ID Protein 29600
UniProtKB/Swiss-Prot ID P00915
UniProtKB/Swiss-Prot Entry Name CAH1_HUMAN
PDB IDs
GenBank Gene ID X05014
GeneCard ID CA1
GenAtlas ID CA1
HGNC ID HGNC:1368
References
General References
  1. 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:15489334 ]
  2. Barlow JH, Lowe N, Edwards YH, Butterworth PH: Human carbonic anhydrase I cDNA. Nucleic Acids Res. 1987 Mar 11;15(5):2386. [PubMed:3104879 ]
  3. Lowe N, Brady HJ, Barlow JH, Sowden JC, Edwards M, Butterworth PH: Structure and methylation patterns of the gene encoding human carbonic anhydrase I. Gene. 1990 Sep 14;93(2):277-83. [PubMed:2121614 ]
  4. Giraud N, Marriq C, Laurent-Tabusse G: [Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)]. Biochimie. 1974;56(8):1031-43. [PubMed:4217196 ]
  5. Andersson B, Nyman PO, Strid L: Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem Biophys Res Commun. 1972 Aug 7;48(3):670-7. [PubMed:4625868 ]
  6. Lin KT, Deutsch HF: Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. J Biol Chem. 1973 Mar 25;248(6):1885-93. [PubMed:4632246 ]
  7. Lin KT, Deutsch HF: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem. 1974 Apr 25;249(8):2329-37. [PubMed:4207120 ]
  8. Briganti F, Mangani S, Scozzafava A, Vernaglione G, Supuran CT: Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction? J Biol Inorg Chem. 1999 Oct;4(5):528-36. [PubMed:10550681 ]
  9. Temperini C, Scozzafava A, Vullo D, Supuran CT: Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme. Chemistry. 2006 Sep 18;12(27):7057-66. [PubMed:16807956 ]
  10. Temperini C, Scozzafava A, Vullo D, Supuran CT: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design. J Med Chem. 2006 May 18;49(10):3019-27. [PubMed:16686544 ]
  11. Temperini C, Innocenti A, Scozzafava A, Mastrolorenzo A, Supuran CT: Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV. Bioorg Med Chem Lett. 2007 Feb 1;17(3):628-35. Epub 2006 Nov 15. [PubMed:17127057 ]
  12. Crocetti L, Maresca A, Temperini C, Hall RA, Scozzafava A, Muhlschlegel FA, Supuran CT: A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases. Bioorg Med Chem Lett. 2009 Mar 1;19(5):1371-5. doi: 10.1016/j.bmcl.2009.01.038. Epub 2009 Jan 19. [PubMed:19186056 ]
  13. Maresca A, Temperini C, Vu H, Pham NB, Poulsen SA, Scozzafava A, Quinn RJ, Supuran CT: Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc. 2009 Mar 4;131(8):3057-62. doi: 10.1021/ja809683v. [PubMed:19206230 ]
  14. Di Fiore A, Monti SM, Hilvo M, Parkkila S, Romano V, Scaloni A, Pedone C, Scozzafava A, Supuran CT, De Simone G: Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide. Proteins. 2009 Jan;74(1):164-75. doi: 10.1002/prot.22144. [PubMed:18618712 ]
  15. Kannan KK, Fridborg K, Bergsten PC, Liljas A, Lovgren S, Petef M, Strandberg B, Waara I, Adler L, Falkbring SO, Gothe PO, Nyman PO: Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications. J Mol Biol. 1972 Feb 14;63(3):601-4. [PubMed:4622589 ]
  16. Kannan KK, Notstrand B, Fridborg K, Lovgren S, Ohlsson A, Petef M: Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution. Proc Natl Acad Sci U S A. 1975 Jan;72(1):51-5. [PubMed:804171 ]
  17. Kannan KK, Ramanadham M, Jones TA: Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann N Y Acad Sci. 1984;429:49-60. [PubMed:6430186 ]
  18. Kumar V, Kannan KK, Sathyamurthi P: Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes. Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):731-8. [PubMed:15299369 ]
  19. Kumar V, Kannan KK: Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate. J Mol Biol. 1994 Aug 12;241(2):226-32. [PubMed:8057362 ]
  20. Chakravarty S, Kannan KK: Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme. J Mol Biol. 1994 Oct 21;243(2):298-309. [PubMed:7932756 ]
  21. Ferraroni M, Tilli S, Briganti F, Chegwidden WR, Supuran CT, Wiebauer KE, Tashian RE, Scozzafava A: Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1: evidence for a second zinc binding site involving arginine coordination. Biochemistry. 2002 May 21;41(20):6237-44. [PubMed:12009884 ]
  22. Temperini C, Scozzafava A, Supuran CT: Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I. Bioorg Med Chem Lett. 2006 Oct 1;16(19):5152-6. Epub 2006 Jul 25. [PubMed:16870440 ]
  23. Jude KM, Banerjee AL, Haldar MK, Manokaran S, Roy B, Mallik S, Srivastava DK, Christianson DW: Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity. J Am Chem Soc. 2006 Mar 8;128(9):3011-8. [PubMed:16506782 ]
  24. Temperini C, Innocenti A, Guerri A, Scozzafava A, Rusconi S, Supuran CT: Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I. Bioorg Med Chem Lett. 2007 Apr 15;17(8):2210-5. Epub 2007 Feb 8. [PubMed:17314045 ]
  25. Srivastava DK, Jude KM, Banerjee AL, Haldar M, Manokaran S, Kooren J, Mallik S, Christianson DW: Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II. J Am Chem Soc. 2007 May 2;129(17):5528-37. Epub 2007 Apr 4. [PubMed:17407288 ]
  26. Omoto K, Ueda S, Goriki K, Takahashi N, Misawa S, Pagaran IG: Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam. Am J Hum Genet. 1981 Jan;33(1):105-11. [PubMed:6781336 ]
  27. Chegwidden WR, Wagner LE, Venta PJ, Bergenhem NC, Yu YS, Tashian RE: Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I. Hum Mutat. 1994;4(4):294-6. [PubMed:7866410 ]