ID H5YLZ9_9BRAD Unreviewed; 246 AA.
AC H5YLZ9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=Bra471DRAFT_04432 {ECO:0000313|EMBL:EHR03648.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR03648.1};
RN [1] {ECO:0000313|EMBL:EHR03648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR03648.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CM001442; EHR03648.1; -; Genomic_DNA.
DR RefSeq; WP_007610900.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YLZ9; -.
DR HOGENOM; CLU_053879_4_2_5; -.
DR OrthoDB; 9797527at2; -.
DR Proteomes; UP000005774; Chromosome.
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; cd03378; beta_CA_cladeC; 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:SF13; CARBONIC ANHYDRASE 2; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..246
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003601892"
SQ SEQUENCE 246 AA; 25853 MW; 539C8CF83F274898 CRC64;
MCDKCNESPH EMIAPSRRSA MLLGASALGL ALTGRAFAKE TKAPPKPQNV LSPDASLKRL
TEGNARYVDG VSRRHDFKHE REALVGGQNP FAAVLSCADS RIAPEYAFDT GRGDLFVCRV
AGNFAGTETI ASMEYAVAVL NTPLILVLGH DACGAVDATL KAIKDNKPPP GHIPSLVDAI
TPAAKTAMQQ GGDVLDKAIR QNVIDNVAKL KSATPILNAA VEQGKLKVVG GIYRLTTGTV
DVIAQG
//