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Identification
HMDB Protein ID HMDBP02404
Secondary Accession Numbers
  • 7897
  • HMDBP04954
Name Carbonic anhydrase 5A, mitochondrial
Synonyms
  1. CA-VA
  2. Carbonate dehydratase VA
  3. Carbonic anhydrase VA
Gene Name CA5A
Protein Type Unknown
Biological Properties
General Function Involved in carbonate dehydratase activity
Specific Function Reversible hydration of carbon dioxide. Low activity.
Pathways Not Available
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
mitochondrial matrix
Component
mitochondrion
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
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. Mitochondrion
Gene Properties
Chromosome Location 16
Locus 16q24.3
SNPs CA5A
Gene Sequence
>918 bp
ATGTTGGGGAGGAACACTTGGAAGACCTCAGCTTTCTCCTTCTTGGTTGAGCAGATGTGG
GCCCCTCTCTGGAGTCGTTCGATGAGGCCAGGGCGATGGTGTTCTCAGCGTTCCTGTGCA
TGGCAAACCAGCAATAACACTTTGCACCCACTCTGGACGGTCCCGGTCTCCGTGCCAGGG
GGCACCCGGCAGTCTCCTATTAACATCCAGTGGAGGGACAGCGTCTATGACCCCCAGCTG
AAGCCACTCAGGGTCTCCTATGAAGCGGCATCCTGCCTGTACATCTGGAACACTGGCTAC
CTCTTCCAGGTGGAATTTGACGATGCCACCGAGGCATCAGGAATTAGTGGTGGGCCCTTG
GAAAACCACTACAGACTGAAGCAATTTCACTTCCACTGGGGAGCAGTGAACGAGGGGGGC
TCAGAGCACACAGTGGACGGCCACGCGTACCCTGCAGAGCTGCATTTAGTTCACTGGAAT
TCTGTGAAATACCAAAATTACAAGGAAGCTGTCGTGGGAGAGAATGGTTTGGCTGTGATA
GGCGTGTTTTTAAAGCTCGGGGCCCATCATCAGACGCTGCAGAGGCTGGTGGACATCTTG
CCGGAAATAAAACATAAGGACGCGCGGGCGGCCATGCGCCCCTTCGACCCCTCCACTCTG
CTGCCCACCTGCTGGGATTACTGGACCTACGCGGGCTCGCTCACCACCCCGCCGCTGACC
GAGTCGGTCACCTGGATCATCCAGAAGGAGCCCGTTGAAGTGGCCCCAAGCCAGCTCTCT
GCATTTCGTACTCTCCTGTTTTCTGCTCTTGGTGAAGAGGAGAAGATGATGGTGAACAAC
TATCGCCCACTTCAACCCTTGATGAACCGGAAGGTCTGGGCGTCCTTCCAGGCCACTAAT
GAGGGCACAAGGTCCTAG
Protein Properties
Number of Residues 305
Molecular Weight 34750.21
Theoretical pI 7.602
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Carbonic anhydrase 5A, mitochondrial
MLGRNTWKTSAFSFLVEQMWAPLWSRSMRPGRWCSQRSCAWQTSNNTLHPLWTVPVSVPG
GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPL
ENHYRLKQFHFHWGAVNEGGSEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVI
GVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTLLPTCWDYWTYAGSLTTPPLT
ESVTWIIQKEPVEVAPSQLSAFRTLLFSALGEEEKMMVNNYRPLQPLMNRKVWASFQATN
EGTRS
GenBank ID Protein 187952273
UniProtKB/Swiss-Prot ID P35218
UniProtKB/Swiss-Prot Entry Name CAH5A_HUMAN
PDB IDs Not Available
GenBank Gene ID BC137405
GeneCard ID CA5A
GenAtlas ID CA5A
HGNC ID HGNC:1377
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. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. Nagao Y, Platero JS, Waheed A, Sly WS: Human mitochondrial carbonic anhydrase: cDNA cloning, expression, subcellular localization, and mapping to chromosome 16. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7623-7. [PubMed:8356065 ]
  10. Nagao Y, Batanian JR, Clemente MF, Sly WS: Genomic organization of the human gene (CA5) and pseudogene for mitochondrial carbonic anhydrase V and their localization to chromosomes 16q and 16p. Genomics. 1995 Aug 10;28(3):477-84. [PubMed:7490083 ]