ID Q5K8R3_CRYNJ Unreviewed; 239 AA.
AC Q5K8R3;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 2.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN OrderedLocusNames=CNL04780 {ECO:0000313|EMBL:AAW46503.2};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW46503.2, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW46503.2, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU003956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000943,
CC ECO:0000256|RuleBase:RU003956};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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DR EMBL; AE017352; AAW46503.2; -; Genomic_DNA.
DR RefSeq; XP_568020.1; XM_568020.1.
DR AlphaFoldDB; Q5K8R3; -.
DR STRING; 214684.Q5K8R3; -.
DR PaxDb; 214684-Q5K8R3; -.
DR EnsemblFungi; AAW46503; AAW46503; CNL04780.
DR VEuPathDB; FungiDB:CNL04780; -.
DR eggNOG; KOG1578; Eukaryota.
DR HOGENOM; CLU_053879_3_2_1; -.
DR InParanoid; Q5K8R3; -.
DR OrthoDB; 5392875at2759; -.
DR Proteomes; UP000002149; Chromosome 12.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR CDD; cd00883; beta_CA_cladeA; 1.
DR Gene3D; 6.10.140.610; -; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003956};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Zinc {ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 239 AA; 26703 MW; A370A73553C2A992 CRC64;
MPFHAEPLKP SEEIDMDLGH SVAAQKFKEI REVLEGNRYW ARKVTSEEPE FMAEQVMGQA
PNFLWIGCAD SRVPEVTIMA RKPGDVFVQR NVANQFKPED DSSQALLNYA IMNVGVTHVM
VVGHTGCGGC IAAFDQPIPT VENPGATPLV RYLEPIIRLK HSLPEGSDVN DLIKENVKMA
VKNVVNSPTI QEAWEKARKG EFREVFVHGW LYDLSTGNIV DLNVTQGPHP FVDDRVPRT
//
