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URE32_BRUME
ID   URE32_BRUME             Reviewed;         100 AA.
AC   Q8YHZ6;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Urease subunit gamma 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00739};
GN   Name=ureA2 {ECO:0000255|HAMAP-Rule:MF_00739}; OrderedLocusNames=BMEI0649;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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   -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00739}.
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DR   EMBL; AE008917; AAL51830.1; -; Genomic_DNA.
DR   PIR; AC3333; AC3333.
DR   RefSeq; WP_002964469.1; NZ_GG703780.1.
DR   AlphaFoldDB; Q8YHZ6; -.
DR   SMR; Q8YHZ6; -.
DR   STRING; 224914.BMEI0649; -.
DR   EnsemblBacteria; AAL51830; AAL51830; BMEI0649.
DR   GeneID; 45052376; -.
DR   KEGG; bme:BMEI0649; -.
DR   KEGG; bmel:DK63_778; -.
DR   PATRIC; fig|224914.52.peg.815; -.
DR   eggNOG; COG0831; Bacteria.
DR   OMA; MNLAPRE; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000419; Chromosome I.
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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..100
FT                   /note="Urease subunit gamma 2"
FT                   /id="PRO_0000098001"
SQ   SEQUENCE   100 AA;  10943 MW;  FABF969BACC53D05 CRC64;
     MHLTPREFDK LVIHMLSDVA LKRKNKGLKL NHPEAVAVLS AYVLDGAREG KTVEEVMDGA
     RSVLKADDVM DGVPDLLPLI QVEAVFSDGS RLVSLHNPIT
 
 
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