ID M7XDU1_RHOT1 Unreviewed; 201 AA.
AC M7XDU1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU003956};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU003956};
DE AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN ORFNames=RHTO_01204 {ECO:0000313|EMBL:EMS21989.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21989.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS21989.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS21989.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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|RuleBase:RU003956};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; KB722653; EMS21989.1; -; Genomic_DNA.
DR RefSeq; XP_016273108.1; XM_016414887.1.
DR AlphaFoldDB; M7XDU1; -.
DR GeneID; 27365217; -.
DR eggNOG; ENOG502RXIV; Eukaryota.
DR HOGENOM; CLU_084253_4_0_1; -.
DR OrthoDB; 1420433at2759; -.
DR Proteomes; UP000016926; 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 CDD; cd03379; beta_CA_cladeD; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR43175:SF3; CARBON DISULFIDE HYDROLASE; 1.
DR PANTHER; PTHR43175; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 201 AA; 22016 MW; C151C290968A9B61 CRC64;
MASHIASMAE TAAAKFATQP DLKGKSFADT ELAVNNSNFI KTYPVLVGEK GKLHLMPRRG
IAIICCMDAR LDPNAMTGLE VGDAHIIRNG GGRAADALRS LIGSQEALQT REIILIHHED
CGYSHASTPV IQATLKHRTP ESAHALIDAL ALQEFKEDSK HTSVKADVEY LRNHPLIHPD
SKDKISGWWY SVKNGELKRV C
//
