ID   Q8ZRS0_SALTY            Unreviewed;       220 AA.
AC   Q8ZRS0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 130.
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=yadF {ECO:0000313|EMBL:AAL19135.1};
GN   OrderedLocusNames=STM0171 {ECO:0000313|EMBL:AAL19135.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL19135.1, ECO:0000313|Proteomes:UP000001014};
RN   [1] {ECO:0000313|EMBL:AAL19135.1, ECO:0000313|Proteomes:UP000001014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720
RC   {ECO:0000313|Proteomes:UP000001014};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0007829|PDB:3QY1}
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC.
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Brunzelle J.S., Wawrzak Z., Onopriyenko O., Anderson W.F., Savchenko A.;
RT   "1.54A Resolution Crystal Structure of a Beta-Carbonic Anhydrase from
RT   Salmonella enterica subsp. enterica serovar Typhimurium str. LT2.";
RL   Submitted (MAR-2011) to the PDB data bank.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006468; AAL19135.1; -; Genomic_DNA.
DR   RefSeq; NP_459176.1; NC_003197.2.
DR   RefSeq; WP_000651591.1; NC_003197.2.
DR   PDB; 3QY1; X-ray; 1.54 A; A/B=1-220.
DR   PDBsum; 3QY1; -.
DR   AlphaFoldDB; Q8ZRS0; -.
DR   SMR; Q8ZRS0; -.
DR   STRING; 99287.STM0171; -.
DR   PaxDb; 99287-STM0171; -.
DR   GeneID; 1251689; -.
DR   KEGG; stm:STM0171; -.
DR   PATRIC; fig|99287.12.peg.181; -.
DR   HOGENOM; CLU_053879_3_0_6; -.
DR   OMA; WHYIIET; -.
DR   PhylomeDB; Q8ZRS0; -.
DR   BioCyc; SENT99287:STM0171-MONOMER; -.
DR   EvolutionaryTrace; Q8ZRS0; -.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
DR   CDD; cd00883; beta_CA_cladeA; 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: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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3QY1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW   Metal-binding {ECO:0007829|PDB:3QY1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3QY1"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3QY1"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3QY1"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3QY1"
SQ   SEQUENCE   220 AA;  24821 MW;  66554450930596DD CRC64;
     MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL
     FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHSG CGGIKAAVEN PELGLINNWL
     LHIRDIWLKH SSLLGKMPEE QRLDALYELN VMEQVYNLGH STIMQSAWKR GQNVTIHGWA
     YSINDGLLRD LDVTATNRET LENGYHKGIS ALSLKYIPHQ
//