GenomeNet

Database: UniProt
Entry: S3HEK9_9RHIZ
LinkDB: S3HEK9_9RHIZ
Original site: S3HEK9_9RHIZ 
ID   S3HEK9_9RHIZ            Unreviewed;       569 AA.
AC   S3HEK9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   11-DEC-2019, entry version 47.
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:EPE97272.1};
GN   ORFNames=RGCCGE502_14525 {ECO:0000313|EMBL:EPE97272.1};
OS   Rhizobium grahamii CCGE 502.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae;
OC   Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=990285 {ECO:0000313|EMBL:EPE97272.1, ECO:0000313|Proteomes:UP000014411};
RN   [1] {ECO:0000313|EMBL:EPE97272.1, ECO:0000313|Proteomes:UP000014411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE 502 {ECO:0000313|EMBL:EPE97272.1,
RC   ECO:0000313|Proteomes:UP000014411};
RX   PubMed=23144400; DOI=10.1128/JB.01785-12;
RA   Althabegoiti M.J., Lozano L., Torres-Tejerizo G., Ormeno-Orrillo E.,
RA   Rogel M.A., Gonzalez V., Martinez-Romero E.;
RT   "Genome sequence of Rhizobium grahamii CCGE502, a broad-host-range symbiont
RT   with low nodulation competitiveness in Phaseolus vulgaris.";
RL   J. Bacteriol. 194:6651-6652(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|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, ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|SAAS:SAAS00317636}.
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_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700, ECO:0000256|SAAS:SAAS00548017}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|RuleBase:RU004158, ECO:0000256|SAAS:SAAS00849550}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPE97272.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AEYE02000015; EPE97272.1; -; Genomic_DNA.
DR   RefSeq; WP_016554915.1; NZ_AEYE02000015.1.
DR   STRING; 990285.RGCCGE502_14525; -.
DR   EnsemblBacteria; EPE97272; EPE97272; RGCCGE502_14525.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000014411; Unassembled WGS sequence.
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   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, ECO:0000256|PIRSR:PIRSR611612-51,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00317628}.
FT   DOMAIN          131..569
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        321
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-52, ECO:0000256|PROSITE-
FT                   ProRule:PRU00700"
FT   METAL           136
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           138
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           218
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           218
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           247
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           273
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           361
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         220
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         218
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   569 AA;  60683 MW;  AB8142035593D75D CRC64;
     MPYKISRVAY AGMFGPTTGD KVRLADTELF IEIEKDFTTY GEEVKFGGGK VIRDGMGQSQ
     ATRAQGAVDT VITNVVIIDH TGIVKADIGL KNGRIAAIGK AGNPDTQPGV NIIVGPSTEA
     IAGEGKIITA GGMDAHIHYI CPQQIEEALM SGVTCMLGGG SGPAHGTLAT TCTGAWHIER
     MIESFDGFPM NLALAGKGNA SLPAALEEMV LAGASSLKLH EDWGTTPAAI DCCLSVADEY
     DIQVMIHTDT LNESGFVEDT IGALKGRTIH AFHTEGAGGG HAPDIIKICG QSNVIPSSTN
     PTRPYTVNTV AEHLDMLMVC HHLSPSIPED IAFAESRIRK ETIAAEDILH DIGAFSIISS
     DSQAMGRVGE VAIRTWQTAD KMKRQRGRLK EETGENDNFR IRRYIAKYTI NPAIAQGLSH
     EIGSVEVGKR ADLVLWNPAF FGVKPEMVLL GGSIAAAPMG DPNASIPTPQ PMHYRPMFAA
     HGKLRTNSSV TFVSQASLDA GLKSRLGVAK SLVAVKNTRG GISKASMVHN SLTPHIEVDP
     ETYEVRADGE LLTCEPATVL PMAQRYFLF
//
DBGET integrated database retrieval system