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Database: UniProt
Entry: URE1_FRACC
LinkDB: URE1_FRACC
Original site: URE1_FRACC 
ID   URE1_FRACC              Reviewed;         575 AA.
AC   Q2JES6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-OCT-2019, entry version 88.
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=Francci3_0832;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000249; ABD10216.1; -; Genomic_DNA.
DR   RefSeq; WP_011435285.1; NZ_LRTJ01000051.1.
DR   SMR; Q2JES6; -.
DR   STRING; 106370.Francci3_0832; -.
DR   EnsemblBacteria; ABD10216; ABD10216; Francci3_0832.
DR   GeneID; 32155821; -.
DR   KEGG; fra:Francci3_0832; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; FSP106370:G1G5U-865-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001937; 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    575       Urease subunit alpha.
FT                                /FTId=PRO_0000239875.
FT   DOMAIN      138    575       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    329    329       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       143    143       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       145    145       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       226    226       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       226    226       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       255    255       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       281    281       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       369    369       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     228    228       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     226    226       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   575 AA;  60100 MW;  94389AA0821A0C59 CRC64;
     MSRLDRSRYA ALYGPTVGDR IRLADTDLFI EVTEDRSRGP AGTGTGDEAV FGGGKVIRES
     MGQSLATRAE GAPDLVITGA VVLDHWGVVK ADVGIRDGRI VALGKAGNPD TMDGVHPELV
     MGPGTEIIAG NGKILTAGAV DCHVHLICPQ QVPEALGAGI TTLIGGGTGP AEGTKATTVT
     PGSWNLARML SALDDWPVNV VLLGKGNTVS DESMWEQLRA GAAGFKLHED WGTTPAAIDA
     CLRVADAAGV QVALHSDTLN EAGFVEDTLA AIAGRAIHAY HTEGAGGGHA PDIITVAAAG
     NVLPSSTNPT RPHTVNTLDE HLDMLMVCHH LNPSVPEDLA FAESRIRPST IAAEDILHDL
     GAISMIGSDS QAMGRIGEVV LRTWQTAHVM KLRRGSLAGD DRADNTRARR YIAKYTICPA
     VAHGLDAEIG SVEPGKLADL VLYDPAFFGV RPSLVLKGGF IAWAAMGDAN ASIPTPQPVL
     PRPMWGAARG PAAASSLIFV APAAIEDGLP GRLGLATPVV PVADVRRRGK ADLPENTATP
     DIRVDPDTFT VTVDGEAIEA DPVSELPMTQ RYFLF
//
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