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Database: UniProt
Entry: URE1_RHOS4
LinkDB: URE1_RHOS4
Original site: URE1_RHOS4 
ID   URE1_RHOS4              Reviewed;         568 AA.
AC   Q3J154; Q9RFF2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-OCT-2019, entry version 90.
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=RHOS4_19120; ORFNames=RSP_6111;
OS   Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS   158).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA   Choudhary M., Kaplan S.;
RT   "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT   sphaeroides 2.4.1.";
RL   Nucleic Acids Res. 28:862-867(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA   Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24255.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AF195122; AAF24255.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000143; ABA79480.1; -; Genomic_DNA.
DR   PIR; T50711; T50711.
DR   RefSeq; WP_011338138.1; NZ_CP030271.1.
DR   RefSeq; YP_353381.1; NC_007493.2.
DR   SMR; Q3J154; -.
DR   STRING; 272943.RSP_6111; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; ABA79480; ABA79480; RSP_6111.
DR   GeneID; 3719161; -.
DR   KEGG; rsp:RSP_6111; -.
DR   PATRIC; fig|272943.9.peg.2251; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   PhylomeDB; Q3J154; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002703; Chromosome 1.
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; Cytoplasm; Hydrolase; Metal-binding; Nickel;
KW   Reference proteome.
FT   CHAIN         1    568       Urease subunit alpha.
FT                                /FTId=PRO_0000234178.
FT   DOMAIN      131    568       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    322    322       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       136    136       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       138    138       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       219    219       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       219    219       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       248    248       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       274    274       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       362    362       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     221    221       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     219    219       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   568 AA;  60651 MW;  1DBFC54EC85F2B6E CRC64;
     MPASISRSTY ASMFGPTTGD RLRLGDTELV IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ
     RTRAEGAMDT VITNALIVDW TGIYKADVGL RDGRIAKIGK AGNPDTQPGV DIVIGPGTEI
     IAGEGRILTA GGMDAHIHFI CPQQIEDSLH SGITTMLGGG TGPAHGTLAT TCTPGPWHIG
     RMLQAADAFP INLAFAGKGN ASLPAGLEEQ VRAGASCLKL HEDWGTTPAA IDCCLSVADR
     MDVQVMIHTD TLNESGFVEN TLAAIGGRTI HAFHTEGAGG GHAPDIIKVV GAANVIPSST
     NPTMPYTANT VEEHLDMLMV CHHLDRSIPE DVAFAESRIR KETIAAEDIL HDMGAFSVIS
     SDSQAMGRVG EVITRTWQTA HKMKVQRGRL AEETGANDNQ RVRRYIAKYT INPAIAHGLS
     RHIGSVEEGK RADLVLWQPA FFGAKPDLVL LGGMIVCAQM GDPNGSIPAQ PYYSRPMFGA
     FGGALHASAV TFVSQAAEED GVGERLRLQK GTLAVQGTRD IGKADMKLNA HRPSIEVNPE
     TYEVRADGEL LTCQPLAELP LAQRYFLY
//
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