ID   I3TH06_TISMK            Unreviewed;       248 AA.
AC   I3TH06;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-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   Name=icfA {ECO:0000313|EMBL:AFK52044.1};
GN   OrderedLocusNames=TMO_0205 {ECO:0000313|EMBL:AFK52044.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52044.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK52044.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52044.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(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}.
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DR   EMBL; CP003236; AFK52044.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TH06; -.
DR   STRING; 1110502.TMO_0205; -.
DR   KEGG; tmo:TMO_0205; -.
DR   PATRIC; fig|1110502.3.peg.213; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_053879_4_2_5; -.
DR   Proteomes; UP000005258; 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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   248 AA;  25249 MW;  BF69CED9BE5FCD17 CRC64;
     MPHPSSPHLS SHPRIGRRSF LGLLGAGATT LAVGGTAPSW AADPLPRPVV TGDAALARLM
     AGNARWAEGK PEARDPMAGR DARARAQYPI AAIISCADSR IAPELAFDQG PGEVFVVRLA
     GNFANDDGIA SLEYAVAVLG VPLVMVLGHS GCGAVSATID VIRNGTILPG HLPGLIDAMR
     PGIEPVVLSS ATGRPAADLL ADATIGNVRH TLSTLADATP VLSQAIADTR VKAVGGVYDI
     ATGKVTLV
//