(data stored in ACNUC1104 zone)

SWISSPROT: URE2_SACEN

ID   URE2_SACEN              Reviewed;         122 AA.
AC   A4F7F6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Urease subunit beta {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 {ECO:0000255|HAMAP-Rule:MF_01954};
GN   Name=ureB {ECO:0000255|HAMAP-Rule:MF_01954};
GN   OrderedLocusNames=SACE_0635;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01954};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01954}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {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}.
DR   EMBL; AM420293; CAL99980.1; -; Genomic_DNA.
DR   RefSeq; WP_009950042.1; NZ_PDBV01000001.1.
DR   SMR; A4F7F6; -.
DR   STRING; 405948.SACE_0635; -.
DR   EnsemblBacteria; CAL99980; CAL99980; SACE_0635.
DR   KEGG; sen:SACE_0635; -.
DR   eggNOG; ENOG4105KI2; Bacteria.
DR   eggNOG; COG0832; LUCA.
DR   HOGENOM; HOG000077770; -.
DR   KO; K01429; -.
DR   OMA; FYEVNDA; -.
DR   OrthoDB; 1755809at2; -.
DR   BioCyc; SERY405948:SACE_RS03120-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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;
DR   PRODOM; A4F7F6.
DR   SWISS-2DPAGE; A4F7F6.
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN         1    122       Urease subunit beta.
FT                                /FTId=PRO_1000070773.
SQ   SEQUENCE   122 AA;  13238 MW;  9C1B178B3C309A71 CRC64;
     MRPGEIITGD GPVPLNPGRP RVRITVVNRA DRAVQVGSHY HFAAVNEGLE FDRAAAWGHR
     LDVPAGTAVR FEPGVEREVR LVPVGGSRRV PGLRPEYAGE LDGRGHEPTA PNYGEKGQGH
     FE
//

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