ID A0A162ZH48_9FLAO Unreviewed; 295 AA.
AC A0A162ZH48;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00014628, ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN ORFNames=AWE51_09070 {ECO:0000313|EMBL:KZS39791.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS39791.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS39791.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS39791.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU367011}.
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:RU367011};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367011};
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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:KZS39791.1}.
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DR EMBL; LQRT01000024; KZS39791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162ZH48; -.
DR STRING; 1642818.AWE51_09070; -.
DR OrthoDB; 5327615at2; -.
DR Proteomes; UP000076715; 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; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF266; CARBONIC ANHYDRASE 2, ISOFORM A; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000076715};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 68..295
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 295 AA; 32981 MW; DE239FA9CFEB3A58 CRC64;
MKNTNLTVST NRHVKISILV ALLFLSLSLL ISCNNEEVGI ETFESNAIST SEMELASSYF
GKASASDCNF EYGDDPQGPE FWSTLCNGAW VDCAGNVQSP INIITDSVIE DGDINNININ
YTESKTDIFN NGHTLQFTYD QGSSASLNNI DYDLIQFHFH TGSEHTINGK QYPMEMHLVH
QDPITKLLGV VGIFFEEGKK NEVLSKYLSV LPKEEGGQYV SRSKFKVEDL LPGNMEFYTY
DGSLTTPGCS EIVTWYVVKE SITASAEQLS RFESIMHKNY RPVQDLNGRT VRTKS
//