ID A0A2Z5T0Y6_9CYAN Unreviewed; 273 AA.
AC A0A2Z5T0Y6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=RGRSB_0167 {ECO:0000313|EMBL:BBA78786.1};
OS cyanobacterium endosymbiont of Rhopalodia gibberula.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1763363 {ECO:0000313|EMBL:BBA78786.1, ECO:0000313|Proteomes:UP000264686};
RN [1] {ECO:0000313|EMBL:BBA78786.1, ECO:0000313|Proteomes:UP000264686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RgSB {ECO:0000313|EMBL:BBA78786.1};
RX PubMed=29026213; DOI=10.1038/s41598-017-13578-8;
RA Nakayama T., Inagaki Y.;
RT "Genomic divergence within non-photosynthetic cyanobacterial endosymbionts
RT in rhopalodiacean diatoms.";
RL Sci. Rep. 7:13075-13075(2017).
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}.
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DR EMBL; AP018341; BBA78786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5T0Y6; -.
DR KEGG; cer:RGRSB_0167; -.
DR Proteomes; UP000264686; Chromosome.
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:SF265; CARBONIC ANHYDRASE; 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.
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:UP000264686};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 53..273
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 273 AA; 31344 MW; 7716E55F369C3534 CRC64;
MINAIIGPNS PDRPTEIMDR RSFLKSIPVG LAGTSFSLSF PSLLAAIGKE NHSEWDYQNP
EQWGDISEEY RVCKTGKQQS PIDLQSPIKS HIGHVEIFYK EIPLRIINNG HTIQVNSVPG
NFIIVDDQKF ELLQFHFHHP SEHTVNGKNY PMEIHLVHRN QQGSLAVLGV SLKQGQEHQT
LQLIWDNIPS RKSAEKLISD RYISLNKLLP TSFDSYRYFG SLTTPPCSEI VYWIVFREPL
EVSLRQIQRF KQIFSSNARP VQPINRRFIL TSL
//