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Database: UniProt
Entry: G8Q506_PSEFL
LinkDB: G8Q506_PSEFL
Original site: G8Q506_PSEFL 
ID   G8Q506_PSEFL            Unreviewed;       566 AA.
AC   G8Q506;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953,
GN   ECO:0000313|EMBL:AEV60653.1};
GN   ORFNames=PSF113_0617 {ECO:0000313|EMBL:AEV60653.1};
OS   Pseudomonas fluorescens F113.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1114970 {ECO:0000313|EMBL:AEV60653.1, ECO:0000313|Proteomes:UP000005437};
RN   [1] {ECO:0000313|EMBL:AEV60653.1, ECO:0000313|Proteomes:UP000005437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F113 {ECO:0000313|EMBL:AEV60653.1,
RC   ECO:0000313|Proteomes:UP000005437};
RX   PubMed=22328765; DOI=10.1128/JB.06601-11;
RA   Redondo-Nieto M., Barret M., Morrisey J.P., Germaine K.,
RA   Martinez-Granero F., Barahona E., Navazo A., Sanchez-Contreras M.,
RA   Moynihan J.A., Giddens S.R., Coppoolse E.R., Muriel C., Stiekema W.J.,
RA   Rainey P.B., Dowling D., O'Gara F., Martin M., Rivilla R.;
RT   "Genome Sequence of the Biocontrol Strain Pseudomonas fluorescens
RT   F113.";
RL   J. Bacteriol. 194:1273-1274(2012).
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:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS01119912};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|PIRSR:PIRSR611612-51,
CC         ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
CC       ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|SAAS:SAAS00317636}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700,
CC       ECO:0000256|SAAS:SAAS00548017}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|RuleBase:RU004158,
CC       ECO:0000256|SAAS:SAAS00849550}.
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DR   EMBL; CP003150; AEV60653.1; -; Genomic_DNA.
DR   RefSeq; WP_014336351.1; NC_016830.1.
DR   STRING; 1114970.PSF113_0617; -.
DR   EnsemblBacteria; AEV60653; AEV60653; PSF113_0617.
DR   GeneID; 11828703; -.
DR   KEGG; pfe:PSF113_0617; -.
DR   PATRIC; fig|1114970.3.peg.633; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   KO; K01428; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; PFLU1114970:G1H1T-653-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000005437; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00375; Urease_alpha; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005437};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|SAAS:SAAS00317631};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00317628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005437}.
FT   DOMAIN      128    566       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    319    319       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       133    133       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       135    135       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       216    216       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       216    216       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       245    245       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       271    271       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       359    359       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     218    218       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     216    216       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   566 AA;  60666 MW;  1421C5FE7F37160F CRC64;
     MKISRQAYAD MFGPTVGDKV RLADTELWIE VEKDFTTYGE EVKFGGGKVI RDGMGQSQLL
     AAEVVDTLIT NALIIDHWGI VKADVGLKDG RIAAIGKAGN PDIQPDVTIA IGASTEVIAG
     EGMILTAGGI DTHIHFICPQ QIEEALMSGV TTMIGGGTGP ATGTNATTCT SGPWHLARML
     QAADAFPMNI GFTGKGNASL PEPLIEQVKA GAIGLKLHED WGTTPAAIDN CLSVADQYDV
     QVAIHTDTLN ESGFVETTLA AFKGRTIHTY HTEGAGGGHA PDIIKACGFA NVLPSSTNPT
     RPFTRNTIDE HLDMLMVCHH LDPSIAEDVA FAESRIRRET IAAEDILHDL GAFSMISSDS
     QAMGRVGEVI TRTWQTADKM KKQRGALPGD GEGNDNFRIK RYIAKYTINP AITHGISHEV
     GSIEVGKWAD LVLWRPAFFG VKPTLILKGG AIAASLMGDA NASIPTPQPV HYRPMFASFG
     GSRHATSLTF ISQAAAEAGL PEQLGLKKKI AVVKGCRDVQ KTDLIHNDYL PSIDVDPQTY
     QVKADGVLLW CEPAEVLPMA QRYFLF
//
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