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Database: UniProt
Entry: C6D7R8_PAESJ
LinkDB: C6D7R8_PAESJ
Original site: C6D7R8_PAESJ 
ID   C6D7R8_PAESJ            Unreviewed;       570 AA.
AC   C6D7R8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 79.
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   OrderedLocusNames=Pjdr2_4326 {ECO:0000313|EMBL:ACT02948.1};
OS   Paenibacillus sp. (strain JDR-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=324057 {ECO:0000313|EMBL:ACT02948.1, ECO:0000313|Proteomes:UP000002510};
RN   [1] {ECO:0000313|Proteomes:UP000002510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510};
RX   PubMed=22675593; DOI=10.4056/sigs.2374349;
RA   Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA   Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S.,
RA   Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L.,
RA   Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.;
RT   "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL   Stand. Genomic Sci. 6:1-10(2012).
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; CP001656; ACT02948.1; -; Genomic_DNA.
DR   RefSeq; WP_015845888.1; NC_012914.1.
DR   STRING; 324057.Pjdr2_4326; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; ACT02948; ACT02948; Pjdr2_4326.
DR   KEGG; pjd:Pjdr2_4326; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; PSP324057:G1GF7-4387-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002510; 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:UP000002510};
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:UP000002510}.
FT   DOMAIN      133    570       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    324    324       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       138    138       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       140    140       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       221    221       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       221    221       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       250    250       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       276    276       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       364    364       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     221    221       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   570 AA;  60980 MW;  08E659C9302DCB0B CRC64;
     MSVIDRHRYA AMFGPTTGDA VRLADTELWA EIEKDYTVHG DECKFGGGKV IRDGMGQSSG
     ALRGEGVLDT LITNAVIIDH WGIVKADIGI KDGFIVGIGK AGNPDIMDGV TPGMIAGAST
     EVIAGEGKII TAGGIDAHIH FICPQQIETA LSSGVTTMIG GGTGPATGTN ATTVTPGAWH
     MRRMLEAAEQ FPMNLGFTGK GNASFTAPLI EQIEAGAIGL KLHEDWGTTP AAIDACLKAA
     DQYDIQVAIH TDTLNEAGFV EDTLRAIGGR TIHTYHTEGA GGGHAPDIIV AAGELNVLPS
     STNPTRPFTI NTIEEHLDML MVCHHLDSRI PEDVAFADSR IRPETIAAED ILHDIGVFSM
     ISSDSQAMGR VGEVIIRTWQ TADKMKRQRG PLSPDTVSDN FRVKRYVAKY TINPAITHGI
     SHLVGSVEVG KFADLVLWQP MFFGVKPDLV LKGGSIAYAQ MGDPNASIPT PQPVFGRPMF
     AAFGKAVHGS SITFVSQAAF DNGIDRQLGL QKRIEPVKGC RSVTKKDMIH NDATPLIEVD
     PETYRVTVDG ELVTCEPAKS LPMAQRYFLF
//
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