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Database: UniProt
Entry: H0BY93_9BURK
LinkDB: H0BY93_9BURK
Original site: H0BY93_9BURK 
ID   H0BY93_9BURK            Unreviewed;       101 AA.
AC   H0BY93;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Urease subunit beta {ECO:0000256|HAMAP-Rule:MF_01954};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01954};
DE   AltName: Full=Urea amidohydrolase subunit beta {ECO:0000256|HAMAP-Rule:MF_01954};
GN   Name=ureB {ECO:0000256|HAMAP-Rule:MF_01954};
GN   ORFNames=KYG_11834 {ECO:0000313|EMBL:EHL22544.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL22544.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL22544.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL22544.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
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:0000256|ARBA:ARBA00000242, ECO:0000256|HAMAP-
CC         Rule:MF_01954};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01954}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01954}.
CC   -!- SIMILARITY: Belongs to the urease beta subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01954}.
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DR   EMBL; AGTS01000078; EHL22544.1; -; Genomic_DNA.
DR   RefSeq; WP_008905052.1; NZ_AGTS01000078.1.
DR   AlphaFoldDB; H0BY93; -.
DR   STRING; 512030.KYG_11834; -.
DR   PATRIC; fig|512030.4.peg.2327; -.
DR   OrthoDB; 9797217at2; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000003485; Unassembled WGS sequence.
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; Urease, beta subunit; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR002019; Urease_beta-like.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   NCBIfam; TIGR00192; urease_beta; 1.
DR   PANTHER; PTHR33569; UREASE; 1.
DR   PANTHER; PTHR33569:SF1; UREASE; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   SUPFAM; SSF51278; Urease, beta-subunit; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01954};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01954};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485}.
SQ   SEQUENCE   101 AA;  11048 MW;  9D2B63B7B19C56AE CRC64;
     MIPGELLTDS GEHPLNTGRR TLTLVVRNTG DRPIQVGSHY HFAETNNALG FDRAAARGMR
     LNIASGTAVR FEPGQERTVE LVDYAGERRV YGFQGLVHGA L
//
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