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Entry: A0A0K0Y1Y1_9RHOB
LinkDB: A0A0K0Y1Y1_9RHOB
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ID   A0A0K0Y1Y1_9RHOB        Unreviewed;       569 AA.
AC   A0A0K0Y1Y1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-MAY-2019, entry version 27.
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=ureC1 {ECO:0000313|EMBL:AKS44943.1};
GN   Synonyms=ureC {ECO:0000256|HAMAP-Rule:MF_01953};
GN   ORFNames=OSB_03770 {ECO:0000313|EMBL:AKS44943.1};
OS   Octadecabacter temperatus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Octadecabacter.
OX   NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS44943.1, ECO:0000313|Proteomes:UP000067444};
RN   [1] {ECO:0000313|EMBL:AKS44943.1, ECO:0000313|Proteomes:UP000067444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB1 {ECO:0000313|EMBL:AKS44943.1,
RC   ECO:0000313|Proteomes:UP000067444};
RX   PubMed=26358607;
RA   Voget S., Billerbeck S., Simon M., Daniel R.;
RT   "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT   Mesophilic Species of the Genus Octadecabacter.";
RL   Genome Announc. 3:e01051-15(2015).
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; CP012160; AKS44943.1; -; Genomic_DNA.
DR   RefSeq; WP_049833380.1; NZ_FSRP01000001.1.
DR   EnsemblBacteria; AKS44943; AKS44943; OSB_03770.
DR   KEGG; otm:OSB_03770; -.
DR   PATRIC; fig|1458307.3.peg.380; -.
DR   KO; K01428; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; GCF_900142425:G1FOB-1186-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000067444; 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:UP000067444};
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:UP000067444}.
FT   DOMAIN      131    569       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    322    322       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       136    136       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       138    138       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       248    248       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       274    274       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       362    362       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     219    219       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   569 AA;  60648 MW;  62AE37C5ACDD4EAB CRC64;
     MPREIPRAQY AAMFGPTTGD KVRLADTDLI IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ
     VTRAGGAVDT VITNALIVDH SGIYKADVAL KDGLIHAIGK AGNPDTQSGV DIIIGPGTEI
     IAGEGRILTA GGVDSHIHFI CPQQMEDSLH SGVTTCFGGG TGPAHGTLAT TCTPGPWHIG
     RMLQSFDGIT MNIGLSGKGN ASQPDALVEM VQAGACALKL HEDWGTTPAA IDCCLGVADD
     LDVQVMIHTD TLNESGFVEH TVGAMKGRTI HAFHTEGAGG GHAPDIIKIC GHDNVIPSST
     NPTRPFTVNT LEEHLDMLMV CHHLDKSIPE DIAFAESRIR RETIAAEDIL HDIGAFSIIA
     SDSQAMGRVG EVLIRTWQTA DKMKKQRGAL TDETGDNDNM RVRRYIAKYT INPAIAQGVG
     HVIGDISVGK RADLVLWDTA FFGVKPEMVL MAGSIVVAQM GDPNASIPTP QPVYTRPMFG
     QYGSAQQHTS VSFVSGVAQD AGLRETLGLA KQTVAVKNTR TIGKSDMVLN DATPSVEVDP
     ETYEVRADGE LLTCQPADVL PMAQRYFMF
//
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