ID A0A1V6QEZ3_9EURO Unreviewed; 291 AA.
AC A0A1V6QEZ3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=PENANT_c005G05856 {ECO:0000313|EMBL:OQD87774.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD87774.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD87774.1}.
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DR EMBL; MDYN01000005; OQD87774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QEZ3; -.
DR STRING; 416450.A0A1V6QEZ3; -.
DR OrthoDB; 5392875at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
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:UP000191672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
FT REGION 43..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 31451 MW; 1CC894E76031F527 CRC64;
MTFTRLAGQT GFIARAAGIA SDSSSYVLKT RLRVSPTSFP APRTVPFSTS TPLRCANHKS
SGAETPSANT PDAKSQTDAG DHTDRYAAAL RNNKEWAAQT AREHPDLFPT LATGQTPQIL
WIGCSDSRCP ETTFLGLKPG DVFVHRNIAN VLHPGDLSSA AAIEYAVQYL RVKHVIVCGH
TACGGVAAAM GNKNLGILDP WLLPLRQLRE RNLELLQTLS PDEAAMKLAE LNVREGLNIV
KQKGVVLNAI QERGLELHGL IYDVGSGVLS ELDTQDSEEV IRARLTAFKT E
//
