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Database: UniProt
Entry: A0A0P4RBW1_9ACTN
LinkDB: A0A0P4RBW1_9ACTN
Original site: A0A0P4RBW1_9ACTN 
ID   A0A0P4RBW1_9ACTN        Unreviewed;       673 AA.
AC   A0A0P4RBW1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   31-JUL-2019, entry version 25.
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:GAO11055.1};
GN   ORFNames=TPA0598_07_07790 {ECO:0000313|EMBL:GAO11055.1};
OS   Streptomyces sp. NBRC 110027.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1546107 {ECO:0000313|EMBL:GAO11055.1, ECO:0000313|Proteomes:UP000048965};
RN   [1] {ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|Proteomes:UP000048965};
RA   Komaki H., Ichikawa N., Katano-Makiyama Y., Hosoyama A., Hashimoto M.,
RA   Uohara A., Kitahashi Y., Ohji S., Kimura A., Yamazoe A., Igarashi Y.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110027.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAO11055.1, ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|EMBL:GAO11055.1,
RC   ECO:0000313|Proteomes:UP000048965};
RX   PubMed=26380643; DOI=10.1186/s40793-015-0046-5;
RA   Komaki H., Ichikawa N., Hosoyama A., Fujita N., Igarashi Y.;
RT   "Draft genome sequence of marine-derived Streptomyces sp. TP-A0598, a
RT   producer of anti-MRSA antibiotic lydicamycins.";
RL   Stand. Genomic Sci. 10:58-58(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: May form a heterohexamer of 3 UreC (alpha) and 3 UreAB
CC       (gamma/beta) subunits. May also form a heterotrimer of UreA
CC       (gamma), UreB (beta) and UreC (alpha) subunits. Three
CC       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,
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAO11055.1}.
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DR   EMBL; BBNO01000007; GAO11055.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAO11055; GAO11055; TPA0598_07_07790.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000048965; 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   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; 1.
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:UP000048965};
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}.
FT   DOMAIN      183    673       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION        1     22       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      137    162       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    374    374       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       188    188       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       190    190       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       271    271       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       271    271       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       300    300       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       326    326       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       414    414       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     273    273       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     271    271       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   673 AA;  72116 MW;  43F52AE60083CE73 CRC64;
     MSNYRTTLSS GRSASSPENS AASNVLKRAE YATLYGPTTK DRVRLADTAL TVEIEADWSG
     GPKHSGNEMI FGGGKVIRES MGMSHIARDG DAAGRKPVDT VITGALILDW WGVVKADVGL
     RDGEIVAIGK AYNPETMDPI PDDEFERPTR TSPSDELPVQ PTNFVVGPST EVISGNGRIL
     TAGGVDTHVH FICPEQIHEA LASGVTTLIG GGTGPAEGST ATTVTPGEWH ITRVFESLDA
     YPVNIGLLGK GSTVNTDALN EQVDAGVIGF KVHEDWGATP AVIDAALDVC ESRKVQLALH
     ADSLNESGFL DSTRSAFKER SVHIFHVEGA GGGHAPDMIE LVKETNVLPA STNPTRPLTV
     NTVKEHIDMM VVCHHLNPDI PADMAFADSR IRPSTMAAED LLHDMGAISM MSSDAQAMGR
     IGEMVMRTWQ TAHVMKSRYG PLKEDLANAK VRPIADDTDH SHNADRLIPN DNYRARRYVA
     KYTINPAITH GIDGHVGSVE TGKLADLVLW EPKFFGVKMH MVLKGGQLAY AQVGDANASI
     TTPQPFLPRA VWGATGGSPQ SNSYNFVAPG VADRLNSRVV TVQDSSGNVT EMTIGGLGLA
     KKFVDISTSI RDVTKADMKL NDTVPESLNV DHNSFEVTIG GETTGDARTE LNGATVPRAY
     VTEVPMAQRY FLF
//
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