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Database: UniProt
Entry: F9ZXE3_METMM
LinkDB: F9ZXE3_METMM
Original site: F9ZXE3_METMM 
ID   F9ZXE3_METMM            Unreviewed;       567 AA.
AC   F9ZXE3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   11-DEC-2019, entry version 58.
DE   RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953};
GN   OrderedLocusNames=Metme_2540 {ECO:0000313|EMBL:AEG00931.1};
OS   Methylomonas methanica (strain MC09).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG00931.1, ECO:0000313|Proteomes:UP000008888};
RN   [1] {ECO:0000313|EMBL:AEG00931.1, ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|EMBL:AEG00931.1,
RC   ECO:0000313|Proteomes:UP000008888};
RX   PubMed=22123758; DOI=10.1128/JB.06267-11;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA   Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA   Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L., Murrell J.C.;
RT   "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT   methanica MC09.";
RL   J. Bacteriol. 193:7001-7002(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MC09;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA   Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA   Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L.Y., Murrell C.;
RT   "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT   methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT   "Complete sequence of Methylomonas methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS01119912};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|SAAS:SAAS00317636}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Three heterotrimers associate to form the active enzyme.
CC       {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700, ECO:0000256|SAAS:SAAS00548017}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|RuleBase:RU004158, ECO:0000256|SAAS:SAAS00849550}.
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DR   EMBL; CP002738; AEG00931.1; -; Genomic_DNA.
DR   RefSeq; WP_013819167.1; NC_015572.1.
DR   STRING; 857087.Metme_2540; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; AEG00931; AEG00931; Metme_2540.
DR   KEGG; mmt:Metme_2540; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; MMET857087:G1GY2-2555-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000008888; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|SAAS:SAAS00317631};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00317628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008888}.
FT   DOMAIN          129..567
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        320
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-52, ECO:0000256|PROSITE-
FT                   ProRule:PRU00700"
FT   METAL           134
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           136
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           217
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           217
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           246
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           272
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           360
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         219
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         217
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   567 AA;  60409 MW;  3D5EF5432A00A1EA CRC64;
     MSKISRQAYA DMFGPTTGDR VRLADTDLIL EVEADYTVYG DEVKFGGGKV IRDGMGQSQL
     GSEHSVDLVI TNALIIDYWG IVKADVGVKD GRIFKIGKAG NPDIQPGVDI VVGPGTEVIA
     GEGHILTAGG IDAHIHFICP QQIEEALCSG VTTMIGGGTG PATGTNATTC TPGPWHIQQM
     LKAVDGLPMN IGLLGKGNAS LPSALEEQVL AGAMGLKLHE DWGTTPAAID CCLSVAEDYD
     VQVAIHTDTL NESGFVEDTI AAFKGRTIHT YHTEGAGGGH APDIIKACGL ANVLPSSTNP
     TRPYTINTVD EHLDMLMVCH HLDPSIPEDV AFAESRIRRE TIAAEDILHD LGAFSMISSD
     SQAMGRVGEV IIRTWQTAHK MKVQRGALSG DPAANDNQRI KRYIAKYTIN PAISHGISHE
     VGSIEAGKLA DLVLWQPAFF GVKPSLILKG GLIASAPMGD PNASIPTPQP VHYRPMFGSF
     GRAAANNSMI FLPQVAVNSG VAGQLALQKR VGTVRNTRNI GKADMKLNDY QPVMEVCSQT
     YQVRADGVLL TCEPAVVLPM AQRYFLF
//
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