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Database: UniProt
Entry: URE1_AZOSB
LinkDB: URE1_AZOSB
Original site: URE1_AZOSB 
ID   URE1_AZOSB              Reviewed;         568 AA.
AC   A1KBB4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-OCT-2019, entry version 80.
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=azo3504;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Azoarcus.
OX   NCBI_TaxID=62928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte
RT   Azoarcus sp. strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL96120.1; -; Genomic_DNA.
DR   RefSeq; WP_011767226.1; NC_008702.1.
DR   SMR; A1KBB4; -.
DR   STRING; 62928.azo3504; -.
DR   MEROPS; M38.982; -.
DR   PRIDE; A1KBB4; -.
DR   EnsemblBacteria; CAL96120; CAL96120; azo3504.
DR   KEGG; azo:azo3504; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; ASP62928:AZO_RS17600-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002588; 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    568       Urease subunit alpha.
FT                                /FTId=PRO_1000073697.
FT   DOMAIN      130    568       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    321    321       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       135    135       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       137    137       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       218    218       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       218    218       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       247    247       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       273    273       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       361    361       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     220    220       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     218    218       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   568 AA;  60295 MW;  8CCE7D3F3DF1E3D5 CRC64;
     MAKITRRAYA EMFGPTTGDK LRLADTELII EVEKDYTIYG EEVKFGGGKV IRDGMGQGQQ
     LAAEIADTII TNALIVDAVA GIVKADVGLK DGRIWKIGKG GNPDIQPGVT IPVGAGTEVI
     AGEGMILTAG GIDSHIHWIC PQQIDEALMS GVTTMLGGGT GPATGTYATT CTPGPWHIHR
     MLEAADAFPM NMGFFGKGNA SLPGPLKEQV EAGVIGLKLH EDWGTTPAAI DNCLTVADEM
     DVQVAIHTDT LNESGFVETT LAAFKGRTIH TFHTEGAGGG HAPDIIKAVG QANVLPSSTN
     PTRPYTVNTI DEHLDMLMVC HHLDPAIAED VAFAESRIRR ETIAAEDILH DTGAFSMMSS
     DSQAMGRVGE VVIRTWQTAH KMKVQRGALA EDAGKGNDNF RIKRYIAKYT INPAITHGIA
     HVVGSIEEGK LADLVLWKPA FFGVKPSLIL KGGMIAAAAM GDANASIPTP QPVHYRPMFG
     SYGKALKTSV TFVSQAALAN PAVAALQLSK PLVAVQGCRT VQKADMVHNG ATPAIDVDPE
     TYVVRADGEL LVCEPASELP MAQRYFLF
//
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