ID C6XQK9_HIRBI Unreviewed; 278 AA.
AC C6XQK9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Hbal_0921 {ECO:0000313|EMBL:ACT58615.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT58615.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP001678; ACT58615.1; -; Genomic_DNA.
DR RefSeq; WP_015826765.1; NC_012982.1.
DR AlphaFoldDB; C6XQK9; -.
DR STRING; 582402.Hbal_0921; -.
DR KEGG; hba:Hbal_0921; -.
DR eggNOG; COG3338; Bacteria.
DR HOGENOM; CLU_039326_0_2_5; -.
DR OrthoDB; 5327615at2; -.
DR Proteomes; UP000002745; 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:UP000002745};
KW Signal {ECO:0000256|RuleBase:RU367011};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 20..278
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025099257"
FT DOMAIN 56..278
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 278 AA; 30614 MW; F76DD9FE4BA859B1 CRC64;
MHKRLFTFAL LATSMFGLAA NAFAPPKNNG GHNEHSQAQT FHQTNGHTNT KSHENIHWAY
SGPRGPAHWG EKDPANATCK TGTQQSPIDM QHTISAFANA PQIDWTPIKN GEVINNGHTL
QLNVHDAGGL VQNGKTYKLI QFHFHTPSEH TIHGRHFPME AHFVHKAEDG SLAVVGVMFA
EGANNTQLDP LWWSAPSSPG SASVAFNLDI EDLLPTNRAA FRYQGSLTTP PCSEIVDWTV
LQTPLNVSKT QIAAFRALFG DNARPTQPLY RRYVLETP
//
