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Database: UniProt
Entry: D9QCT9_CORP2
LinkDB: D9QCT9_CORP2
Original site: D9QCT9_CORP2 
ID   D9QCT9_CORP2            Unreviewed;       565 AA.
AC   D9QCT9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
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:ADL11365.1};
GN   OrderedLocusNames=CpC231_1913 {ECO:0000313|EMBL:ADL11365.1};
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL11365.1, ECO:0000313|Proteomes:UP000000276};
RN   [1] {ECO:0000313|EMBL:ADL11365.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL11365.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21037006; DOI=10.1128/JB.01211-10;
RG   Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA   Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA   Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA   Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA   de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT   "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT   strain isolated from a cow in Israel with bovine mastitis.";
RL   J. Bacteriol. 193:323-324(2011).
RN   [2] {ECO:0000313|EMBL:ADL11365.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL11365.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA   Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA   Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P.,
RA   Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S.,
RA   Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A.,
RA   Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A.,
RA   Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L.,
RA   Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M.,
RA   Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F.,
RA   Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V.,
RA   Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R.,
RA   Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA   Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT   "Evidence for reductive genome evolution and lateral acquisition of
RT   virulence functions in two Corynebacterium pseudotuberculosis
RT   strains.";
RL   PLoS ONE 6:E18551-E18551(2011).
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; CP001829; ADL11365.1; -; Genomic_DNA.
DR   STRING; 1719.CPTC_00885; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; ADL11365; ADL11365; CpC231_1913.
DR   KEGG; cpq:CpC231_1913; -.
DR   PATRIC; fig|681645.3.peg.2004; -.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000276; 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; 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:UP000000276};
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:UP000000276}.
FT   DOMAIN      127    565       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    318    318       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       132    132       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       134    134       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       215    215       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       215    215       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       244    244       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       270    270       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       358    358       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     217    217       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     215    215       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   565 AA;  60378 MW;  4A34686A1C3E097E CRC64;
     MSRRQYAELN GPTTGDGIRL ADTELIAVVE KDLTQYGDEV SFGGGKVIRD GMGQNSRVEA
     DQVPDLVITN TIIVDYTGIY SADIAVKDGK IMKIGKAGNP DIMDNIDIIV GVGTEVIGGE
     GKIVTAGAID THIHFISPEQ VEAALDNGTT TLIGGGTGPV DSTNATTVTA GAANITKMIE
     ASRDFSVNVG FLGKGHASNP ERLREQIRAG AIGLKIHEDW GATANTIDNA LTVADEMDVQ
     VAIHTDTLNE GGFADNTIAA FKDRVIHTFH TEGAGGGHAP DILKVAGLPN VLPASTNPTL
     PFTVNTMDEH LDMIMVCHHL NADLPEDIAF ADSRIRKETI AAEDVLHDMG VLAITSSDSQ
     AMGRVGEVVL RTWQVAHRMK QQRGPLEGDT VNNDNERIKR YIAKYTINPA IAAGVADTIG
     SVEEGKLADL VVWDPAYFGV KPSIVLKSGI IARSIMGDAN ASIPTPQPRT MRYSFGARGA
     AAGRTSVTFL PTAAFEAGIP EKLGIDRKFV EAKNMREISK ADLKYNNATP DIKVDPETYE
     LTVDGKKVTS EAATELPMTQ RYFLF
//
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