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NameCarbonic anhydrase 5B, mitochondrial
Synonyms
  • 4.2.1.1
  • CA-VB
  • Carbonate dehydratase VB
  • Carbonic anhydrase VB
Gene NameCA5B
OrganismHuman
Amino acid sequence
>lcl|BSEQ0012521|Carbonic anhydrase 5B, mitochondrial
MVVMNSLRVILQASPGKLLWRKFQIPRFMPARPCSLYTCTYKTRNRALHPLWESVDLVPG
GDRQSPINIRWRDSVYDPGLKPLTISYDPATCLHVWNNGYSFLVEFEDSTDKSVIKGGPL
EHNYRLKQFHFHWGAIDAWGSEHTVDSKCFPAELHLVHWNAVRFENFEDAALEENGLAVI
GVFLKLGKHHKELQKLVDTLPSIKHKDALVEFGSFDPSCLMPTCPDYWTYSGSLTTPPLS
ESVTWIIKKQPVEVDHDQLEQFRTLLFTSEGEKEKRMVDNFRPLQPLMNRTVRSSFRHDY
VLNVQAKPKPATSQATP
Number of residues317
Molecular Weight36433.43
Theoretical pI7.91
GO Classification
Functions
  • carbonate dehydratase activity
  • zinc ion binding
Processes
  • small molecule metabolic process
  • bicarbonate transport
  • one-carbon metabolic process
Components
  • mitochondrial matrix
  • mitochondrion
General FunctionZinc ion binding
Specific FunctionReversible hydration of carbon dioxide.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID4587223
UniProtKB IDQ9Y2D0
UniProtKB Entry NameCAH5B_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0012522|Carbonic anhydrase 5B, mitochondrial (CA5B)
ATGGTGGTGATGAACAGCCTGAGGGTCATTCTTCAAGCCTCTCCAGGCAAATTGCTGTGG
AGAAAGTTCCAGATTCCGAGATTCATGCCAGCGAGGCCCTGCAGCCTCTATACTTGTACT
TACAAAACCCGGAACCGAGCCTTGCATCCACTCTGGGAGAGCGTGGACCTGGTTCCTGGG
GGCGATCGCCAGTCACCCATCAACATTCGGTGGAGGGACAGTGTTTATGATCCCGGCTTA
AAACCACTGACCATCTCTTATGACCCAGCCACCTGCCTCCACGTCTGGAATAATGGGTAC
TCTTTCCTCGTGGAATTTGAAGATTCTACAGATAAATCAGTGATCAAGGGAGGACCCCTG
GAACACAACTACCGATTGAAGCAGTTCCATTTTCACTGGGGGGCCATCGATGCCTGGGGT
TCTGAGCACACCGTGGACAGCAAATGCTTCCCAGCAGAGCTGCACTTAGTGCATTGGAAC
GCAGTCAGATTTGAAAACTTTGAGGATGCAGCACTGGAAGAAAATGGTTTGGCTGTGATA
GGAGTATTTTTAAAGCTAGGCAAACATCATAAGGAGCTACAGAAATTAGTGGATACTTTG
CCGTCAATTAAGCATAAGGACGCCCTTGTGGAATTTGGGTCATTTGACCCTTCCTGCCTG
ATGCCTACCTGCCCAGATTACTGGACCTACTCAGGGTCTCTGACTACCCCACCCCTCTCC
GAGTCTGTCACCTGGATCATTAAGAAGCAACCAGTAGAGGTTGATCATGATCAGCTTGAG
CAATTTCGGACCCTGCTTTTCACTTCCGAAGGGGAGAAAGAGAAAAGAATGGTGGACAAC
TTCCGCCCCCTTCAGCCACTGATGAATCGCACTGTTCGTTCATCCTTCCGGCATGATTAT
GTGCTGAATGTACAAGCGAAACCCAAGCCGGCCACCAGCCAAGCAACCCCCTAA
GenBank Gene IDAB021660
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:1378
Chromosome LocationX
LocusNot Available
References
  1. Fujikawa-Adachi K, Nishimori I, Taguchi T, Onishi S: Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome x. J Biol Chem. 1999 Jul 23;274(30):21228-33. 10409679
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  4. Kohler K, Hillebrecht A, Schulze Wischeler J, Innocenti A, Heine A, Supuran CT, Klebe G: Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste. Angew Chem Int Ed Engl. 2007;46(40):7697-9. 17705204
  5. 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. 17314045
  6. 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. 19186056
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