ID   URE3_VIBPH              Reviewed;         100 AA.
AC   Q9FAS7;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Urease subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_00739};
DE   AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
GN   Name=ureA {ECO:0000255|HAMAP-Rule:MF_00739};
OS   Vibrio parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=TH3996;
RX   PubMed=10992480; DOI=10.1128/iai.68.10.5742-5748.2000;
RA   Park K.-S., Iida T., Yamaichi Y., Oyagi T., Yamamoto K., Honda T.;
RT   "Genetic characterization of DNA region containing the trh and ure genes of
RT   Vibrio parahaemolyticus.";
RL   Infect. Immun. 68:5742-5748(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TH3996;
RX   PubMed=19075025; DOI=10.1128/iai.01184-08;
RA   Okada N., Iida T., Park K.-S., Goto N., Yasunaga T., Hiyoshi H.,
RA   Matsuda S., Kodama T., Honda T.;
RT   "Identification and characterization of a novel type III secretion system
RT   in trh-positive Vibrio parahaemolyticus strain TH3996 reveal genetic
RT   lineage and diversity of pathogenic machinery beyond the species level.";
RL   Infect. Immun. 77:904-913(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00739};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00739}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Three heterotrimers associate to form the active enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_00739}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}.
CC   -!- INDUCTION: By urea. {ECO:0000269|PubMed:10992480}.
CC   -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00739}.
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DR   EMBL; AB455531; BAB13786.1; -; Genomic_DNA.
DR   RefSeq; WP_005499469.1; NZ_UHIL01000002.1.
DR   AlphaFoldDB; Q9FAS7; -.
DR   SMR; Q9FAS7; -.
DR   UniPathway; UPA00258; UER00370.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_00739; Urease_gamma; 1.
DR   InterPro; IPR012010; Urease_gamma.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PIRSF; PIRSF001223; Urease_gamma; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..100
FT                   /note="Urease subunit gamma"
FT                   /id="PRO_0000098058"
SQ   SEQUENCE   100 AA;  11121 MW;  8C17DD4937E7AA45 CRC64;
     MELTPREKDK LLLFTAGLVA ERRRARGLKL NYPEAIALIS CEIMEGARDG RTVAELMSYG
     RTILTAEDVM EGVPEMITDI QVECTFPDGT KLVSIHDPIV