ID J2RM29_9PSED Unreviewed; 219 AA.
AC J2RM29;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=PMI28_05276 {ECO:0000313|EMBL:EJM50339.1};
OS Pseudomonas sp. GM48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144330 {ECO:0000313|EMBL:EJM50339.1, ECO:0000313|Proteomes:UP000007293};
RN [1] {ECO:0000313|EMBL:EJM50339.1, ECO:0000313|Proteomes:UP000007293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM48 {ECO:0000313|EMBL:EJM50339.1,
RC ECO:0000313|Proteomes:UP000007293};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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|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}.
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:EJM50339.1}.
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DR EMBL; AKJM01000147; EJM50339.1; -; Genomic_DNA.
DR RefSeq; WP_007991692.1; NZ_AKJM01000147.1.
DR AlphaFoldDB; J2RM29; -.
DR PATRIC; fig|1144330.3.peg.5162; -.
DR OrthoDB; 9797527at2; -.
DR Proteomes; UP000007293; 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 GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00884; beta_CA_cladeB; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR045066; Beta_CA_cladeB.
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:SF42; CARBONIC ANHYDRASE 1; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ SEQUENCE 219 AA; 23408 MW; C9E6095F51B25337 CRC64;
MKALIDGFLK FQKEAFPQRT DLFKHLATTQ HPGTLFITCS DSRVVPELLT QQEPGELFVI
RNAGNIVPSY SPHPGGVSAT VEYAVAVLGV TDIVICGHSD CGAMTAVAKC TCMDHLPAVS
GWLQHAESAK VINEGRPHAS EAAKVISMVR ENVIAQLANI QTHPSVRLAQ EKGLLNLHGW
VYDIETGSID ALDADSRSFV SLVEHPGTCA VSAKAIKAA
//
