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Database: UniProt
Entry: A0A0W0VBC0_9GAMM
LinkDB: A0A0W0VBC0_9GAMM
Original site: A0A0W0VBC0_9GAMM 
ID   A0A0W0VBC0_9GAMM        Unreviewed;       339 AA.
AC   A0A0W0VBC0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   ORFNames=Ljor_1701 {ECO:0000313|EMBL:KTD17395.1};
OS   Legionella jordanis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17395.1, ECO:0000313|Proteomes:UP000055035};
RN   [1] {ECO:0000313|EMBL:KTD17395.1, ECO:0000313|Proteomes:UP000055035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL-540 {ECO:0000313|EMBL:KTD17395.1,
RC   ECO:0000313|Proteomes:UP000055035};
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:KTD17395.1}.
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DR   EMBL; LNYJ01000011; KTD17395.1; -; Genomic_DNA.
DR   RefSeq; WP_058471153.1; NZ_RDQQ01000017.1.
DR   AlphaFoldDB; A0A0W0VBC0; -.
DR   STRING; 456.Ljor_1701; -.
DR   PATRIC; fig|456.5.peg.1817; -.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000055035; 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:UP000055035};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   339 AA;  38442 MW;  120438774C21E2AA CRC64;
     MFIKLILGFR KFQGSTFKEM ESIFELLSLG QFPEVLFITC SDSRVVPTLI IDGDPGDLFV
     VRNVGNIIPP FATHNASSEA VAIEYAIKVL KVKHIIVCGH SGCGAMEGLM KPNIGQELPT
     LASWLKHSSS VIEHFKDKQG VQLEDVVKQN ILAQIEHLKT YPVISNKLAS QELAIHGWFY
     KIKSGEIHVY DENQKEFLHF EQAVKTSLED RKNKVVKQII HHYLEQCLQP KTATEFQEAM
     RLSALIKSDL TPIWEHVKPL VEKKLWEEIG ELYSSPADQE FQALLDSGVT MKLEDLEELK
     VKLQNSSGYH QFCSQHTLFT STSDTSNANS DLENFHYPK
//
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