ID A3LZZ4_PICST Unreviewed; 268 AA.
AC A3LZZ4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 88.
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 Name=NCE3 {ECO:0000313|EMBL:ABN68430.2};
GN ORFNames=PICST_50363 {ECO:0000313|EMBL:ABN68430.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68430.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68430.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000502; ABN68430.2; -; Genomic_DNA.
DR RefSeq; XP_001386459.2; XM_001386422.1.
DR AlphaFoldDB; A3LZZ4; -.
DR STRING; 322104.A3LZZ4; -.
DR GeneID; 4841058; -.
DR KEGG; pic:PICST_50363; -.
DR eggNOG; KOG1578; Eukaryota.
DR HOGENOM; CLU_053879_3_1_1; -.
DR InParanoid; A3LZZ4; -.
DR OMA; EDLFHVH; -.
DR OrthoDB; 5392875at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
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:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00883; beta_CA_cladeA; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
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.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 268 AA; 29930 MW; 50E50D864E1F774E CRC64;
MGRANILHYQ LEHDHETDLS TTPPDSLELN NNVIKSKKQR PNNFPFTLSK DSTKSEFFEN
NQFYVDNLKH NHSTQVFDSN AKGQSPHTLW IGCSDSRAGE SCLATLPGEV FVHRNIANVV
NASDVSSQGV IQFAIDVLKV KKIIVCGHTD CGGIWASLSS KKIGGVLDLW LNPVRHIRAA
NLALLSEFNN DPKKKAKKLA ELNVISSVTA LKRHPSASMA LKNGEIEVWG MMYDVATGYL
SEVEIPDDEF EDLFHIHDEH LDDEFNPH
//
