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Database: UniProt
Entry: URE1_MICLC
LinkDB: URE1_MICLC
Original site: URE1_MICLC 
ID   URE1_MICLC              Reviewed;         571 AA.
AC   C5C8U3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   16-OCT-2019, entry version 63.
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=Mlut_03440;
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC
OS   3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus
OS   lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=465515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC   NCTC 2665 / VKM Ac-2230;
RX   PubMed=19948807; DOI=10.1128/jb.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F.,
RA   Dover L.G., Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N.,
RA   Lapidus A., Lowry S.R., Lykidis A., Mahillon J., Markowitz V.,
RA   Mavromatis K., Mukamolova G.V., Oren A., Rokem J.S., Smith M.C.,
RA   Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
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; CP001628; ACS29895.1; -; Genomic_DNA.
DR   RefSeq; WP_010079477.1; NZ_LS483396.1.
DR   SMR; C5C8U3; -.
DR   STRING; 465515.Mlut_03440; -.
DR   MEROPS; M38.982; -.
DR   PRIDE; C5C8U3; -.
DR   EnsemblBacteria; ACS29895; ACS29895; Mlut_03440.
DR   GeneID; 7986066; -.
DR   KEGG; mlu:Mlut_03440; -.
DR   PATRIC; fig|465515.4.peg.324; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; MLUT465515:G1GEW-337-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000738; 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; 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; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nickel;
KW   Reference proteome.
FT   CHAIN         1    571       Urease subunit alpha.
FT                                /FTId=PRO_1000216198.
FT   DOMAIN      132    571       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    323    323       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       137    137       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       139    139       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       220    220       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       220    220       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       249    249       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       275    275       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       363    363       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     222    222       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     220    220       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   571 AA;  61595 MW;  6085DF31D56DFE5E CRC64;
     MSFEISREQY ASLYGPTTGD AIRLADTELF AVVEEDLTTP GEEAVFGGGK VIRDGMGQNS
     QLVRDVGVPD LVITNVVVID WTGIYKADIA VRDAHIVAIG KAGNPHTMDG VDIVIGVATD
     VISGEGKILT AGGIDTHVHF ISPDQIETAL SSGLTTMIGG GTGPSESSKA TTITPGEWNI
     HTMLRSFEHW PMNFGLLGKG HGSSISPMAE QIRAGAIGLK VHEDWGATPS SINTALQVAD
     EYDVQVAIHT DTLNESGFVE DTRAAIDGRV IHTFHTEGAG GGHAPDIIEL AQYPNILPAS
     TNPTLPYTTN TVEEHVDMLM VAHHLNADLP EDVAFADSRI RQETIAAEDV LQDMGIFSMT
     SSDSQAMGRV GEVLIRTWQV ADSMKRQRGP LPEDEGTAGD NHRIKRYVSK YTINPAIAHG
     IADSVGSVEV GKFADLVLWE PQFFGVKPDL VIKGGQMVYG VVGDPNGSIP TPQPRWYRRS
     FGAYGQAVHT SAITFMSEAS IRAGLPRALG LQKTIRAVHG IRDLTKADMR HNGETPRLEV
     DPETYEVRVD GEPVTCEPQD VLPMAQRYFL F
//
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