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URE22_BRUME
ID   URE22_BRUME             Reviewed;         159 AA.
AC   Q8YHZ7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Urease subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01954};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01954};
DE   AltName: Full=Urea amidohydrolase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01954};
GN   Name=ureB2 {ECO:0000255|HAMAP-Rule:MF_01954}; OrderedLocusNames=BMEI0648;
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_01954};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01954}.
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_01954}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}.
CC   -!- SIMILARITY: Belongs to the urease beta subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR   EMBL; AE008917; AAL51829.1; -; Genomic_DNA.
DR   PIR; AB3333; AB3333.
DR   RefSeq; WP_002964470.1; NZ_GG703780.1.
DR   AlphaFoldDB; Q8YHZ7; -.
DR   SMR; Q8YHZ7; -.
DR   STRING; 224914.BMEI0648; -.
DR   EnsemblBacteria; AAL51829; AAL51829; BMEI0648.
DR   GeneID; 3787946; -.
DR   KEGG; bme:BMEI0648; -.
DR   KEGG; bmel:DK63_779; -.
DR   PATRIC; fig|224914.52.peg.816; -.
DR   eggNOG; COG0832; Bacteria.
DR   OMA; VVHNTGD; -.
DR   PhylomeDB; Q8YHZ7; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000419; Chromosome I.
DR   GO; GO:0035550; C:urease complex; 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; cd00407; Urease_beta; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   Pfam; PF00699; Urease_beta; 1.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..159
FT                   /note="Urease subunit beta 2"
FT                   /id="PRO_0000234237"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   159 AA;  17763 MW;  780EDDB24A15DF16 CRC64;
     MAKEPTEAAH PQPEQTKTNH KAHRPVGGYV LAKDPIEINQ GRPRTTLTVR NTGDRPIQIG
     SHFHFFEVNR YLEFDRSKAF GLRLDIPANT AVRFEPGDEK EVTLVPFAGK RFIFGFNNLV
     DGWSGDGPTP DYQPNREIAA ERAEKLGFKS CKSGGKDAK
 
 
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