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Database: UniProt
Entry: A0A0W0VPB4_9GAMM
LinkDB: A0A0W0VPB4_9GAMM
Original site: A0A0W0VPB4_9GAMM 
ID   A0A0W0VPB4_9GAMM        Unreviewed;       352 AA.
AC   A0A0W0VPB4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   ORFNames=Llon_0758 {ECO:0000313|EMBL:KTD21593.1};
OS   Legionella londiniensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD21593.1, ECO:0000313|Proteomes:UP000054997};
RN   [1] {ECO:0000313|EMBL:KTD21593.1, ECO:0000313|Proteomes:UP000054997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD21593.1,
RC   ECO:0000313|Proteomes:UP000054997};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217}.
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:KTD21593.1}.
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DR   EMBL; LNYK01000014; KTD21593.1; -; Genomic_DNA.
DR   RefSeq; WP_058528769.1; NZ_UGON01000002.1.
DR   AlphaFoldDB; A0A0W0VPB4; -.
DR   STRING; 45068.Llon_0758; -.
DR   PATRIC; fig|45068.5.peg.807; -.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000054997; Unassembled WGS sequence.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF83; CARBONIC ANHYDRASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054997};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   352 AA;  39771 MW;  56C8EF7A2C881125 CRC64;
     MRNAASGALA FQKNEFKKRQ ALFQQLNKQQ DPSVLFITCS DSRIDPNLIT QSEPGELFVI
     RNAGNIIPPF NGNQASGEAA TIEYALTVLN VREIIVCGHS QCGAMQGLIN PESLEHLPSV
     KSWLRHSEKA RMGLNKHSTQ VEQLADAIKT NVLAQIDHLK TYPIVQQKIS MEKLSVQGWV
     YDIKSGNISA YDAAKEEFLP LKKAMRNDVE RSEARMKLPA IARAEAEIFL SKLIKCANLR
     DFCHTLQLAS LTTQDAQRFI WHQIKETVAM RLYAEYAHLF KSANHETFLD LLKIGENTQF
     RTIGVSQKSM QSSEGYRQYC SRILAQEGLF ASKTQKTIET PREHTAHHKP LF
//
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