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Database: UniProt
Entry: URE1_ACTP2
LinkDB: URE1_ACTP2
Original site: URE1_ACTP2 
ID   URE1_ACTP2              Reviewed;         572 AA.
AC   A3N2R4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   16-OCT-2019, entry version 87.
DE   RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953};
GN   OrderedLocusNames=APL_1616;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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:0000255|HAMAP-Rule:MF_01953};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01953};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01953}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000255|HAMAP-
CC       Rule:MF_01953}.
DR   EMBL; CP000569; ABN74700.1; -; Genomic_DNA.
DR   RefSeq; WP_009874593.1; NC_009053.1.
DR   SMR; A3N2R4; -.
DR   STRING; 416269.APL_1616; -.
DR   PRIDE; A3N2R4; -.
DR   EnsemblBacteria; ABN74700; ABN74700; APL_1616.
DR   GeneID; 4850391; -.
DR   KEGG; apl:APL_1616; -.
DR   PATRIC; fig|416269.6.peg.1682; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   BioCyc; APLE416269:G1G87-1719-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001432; 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; Cytoplasm; Hydrolase; Metal-binding; Nickel;
KW   Reference proteome.
FT   CHAIN         1    572       Urease subunit alpha.
FT                                /FTId=PRO_1000070642.
FT   DOMAIN      136    572       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    327    327       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       141    141       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       143    143       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       224    224       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       224    224       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       253    253       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       279    279       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       367    367       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     226    226       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     224    224       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   572 AA;  61835 MW;  112EC338450B5F55 CRC64;
     MALTIPRSQY VATYGPTVGD KVRLGDTDLW ATIEQDFLTK GDECKFGGGK SVRDGMAQSS
     TSTRDNPNVL DFALTNVMII DAKLGIIKAD IGIRDGRIVG IGQAGNPDTM DNVTPNMIIG
     ASTEVHNGAH LIATAGGIDT HIHWICPQQA QHAIENGITT MIGGGSGPAD GTHATTCTPG
     KFNIERMFQA CEALPVNIGF FGKGNCSMLE PLKEQVVAGA LGLKIHEDWG ATPAVIDAAL
     KVADEMDVQV AIHTDTLNES GFLEDTMKAI NGRVIHTFHT EGAGGGHAPD IIKAAMYPNV
     LPASTNPTRP FTVNTIDEHL DMLMVCHHLD KRVPEDVAFA DSRIRPETIA AEDILHDMGV
     FSIMSSDSQA MGRVGEVVTR TWQTADKMKA QRGALGDEGN DNFRIKRYIA KYTINPAIAH
     GISQYVGSLE VGKLADIVLW KPQFFGVKPE FVMKKGFISF AKMGDPNASI PTPQPVFYRP
     MFGANAKANT ESAVYFVSQA SVDANIKAQY GIQKETLAVK GCRDVGKKDL VHNNATPEIT
     VDPERYEVRV DGEHITCEPA TKVPLAQRYF LF
//
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