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Database: UniProt
Entry: A0A0C3MEA4_9PORP
LinkDB: A0A0C3MEA4_9PORP
Original site: A0A0C3MEA4_9PORP 
ID   A0A0C3MEA4_9PORP        Unreviewed;       572 AA.
AC   A0A0C3MEA4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   11-DEC-2019, entry version 32.
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:KIO44793.1};
GN   ORFNames=BA92_07140 {ECO:0000313|EMBL:KIO44793.1}, DMB45_10550
GN   {ECO:0000313|EMBL:PXZ43241.1};
OS   Sanguibacteroides justesenii.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Sanguibacteroides.
OX   NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO44793.1, ECO:0000313|Proteomes:UP000031980};
RN   [1] {ECO:0000313|EMBL:KIO44793.1, ECO:0000313|Proteomes:UP000031980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO44793.1,
RC   ECO:0000313|Proteomes:UP000031980};
RA   Sydenham T.V., Hasman H., Justensen U.S.;
RT   "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT   genome.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PXZ43241.1, ECO:0000313|Proteomes:UP000248308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ43241.1,
RC   ECO:0000313|Proteomes:UP000248308};
RX   PubMed=25814588;
RA   Sydenham T.V., Hasman H., Justesen U.S.;
RT   "Draft Genome Sequences of Sanguibacteroides justesenii, gen. nov., sp.
RT   nov., Strains OUH 308042T (= ATCC BAA-2681T) and OUH 334697 (= ATCC BAA-
RT   2682), Isolated from Blood Cultures from Two Different Patients.";
RL   Genome Announc. 3:e00005-15(2015).
RN   [3] {ECO:0000313|EMBL:PXZ43241.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ43241.1};
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA   Winkler M.E.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:KIO44793.1}.
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DR   EMBL; JPIU01000038; KIO44793.1; -; Genomic_DNA.
DR   EMBL; QJPL01000006; PXZ43241.1; -; Genomic_DNA.
DR   RefSeq; WP_041504204.1; NZ_QJPL01000006.1.
DR   EnsemblBacteria; KIO44793; KIO44793; BA92_07140.
DR   OrthoDB; 157757at2; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000031980; Unassembled WGS sequence.
DR   Proteomes; UP000248308; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031980}.
FT   DOMAIN          134..572
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        325
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           139
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           141
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           222
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           222
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           251
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           277
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           365
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         224
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         222
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   572 AA;  61518 MW;  7EA815D3D97FE7D4 CRC64;
     MAQITRQQYN DLYGPTVGDK IRLGDTDLYV EIEKDLCVYG DEVIYGGGKT LRDGMGLANT
     LTSEGGTLDL VITNVTIIDP KLGVIKADVG IKDGKIAGIG KAGNPNIMQG VTPELVTGAA
     TDAISGEHLI LTAAAIDGHV HMIAPQQAYH CLSNGVTTLV GGGVGPTDGT NGTTITSGTW
     NMKRMLQAID GLPVNYGFLG KGNCSVRRPL VEQMLAGACG FKIHEDWGST PAAIRETMGV
     ADEFDVQVAI HTDTLNESGF VEDTIAAIDG RTIHTYHTEG AGGGHAPDLL KVASLANVLP
     SSTNPTLPFG INSQAELFDM IMVCHNLNPK IPSDVSFAES RVRPETQAAE NVLHDLGVIS
     MISSDSQAMG RVGENFMRAF QMASYMKQVR GKLSEDSAEN DNFRVLRYLA KLTINPAITY
     GFSDILGSIE KGKMADLVLW EPQFFGTKPK LVLKGGMINW AIMGDPNASL PTPQPVYYRP
     MYGSFGSAMP NSCISFVSRA SHDAGIKEKY GLQRIVYPVH GCRQIGKPHM VLNGNMPKID
     INPETFEVLV DGKSAYIPTA KKFPLAQLYW FS
//
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