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Database: UniProt
Entry: A0A2A6FLB1_9RHIZ
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ID   A0A2A6FLB1_9RHIZ        Unreviewed;       570 AA.
AC   A0A2A6FLB1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   11-DEC-2019, entry version 13.
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   ECO:0000313|EMBL:PDQ22750.1};
GN   ORFNames=CN311_02070 {ECO:0000313|EMBL:PDQ22750.1};
OS   Mesorhizobium sanjuanii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=2037900 {ECO:0000313|EMBL:PDQ22750.1, ECO:0000313|Proteomes:UP000219182};
RN   [1] {ECO:0000313|EMBL:PDQ22750.1, ECO:0000313|Proteomes:UP000219182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSA136 {ECO:0000313|EMBL:PDQ22750.1,
RC   ECO:0000313|Proteomes:UP000219182};
RA   Sannazzaro A.I., Torres Tejerizo G.A., Fontana F., Cumpa Velazquez L.M.,
RA   Hansen L., Pistorio M., Estrella M.J.;
RT   "Mesorhizobum sanjuanii sp. nov. isolated from nodules of Lotus tenuis in
RT   saline-alkaline lowlands of Flooding Pampa.";
RL   Submitted (SEP-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PDQ22750.1}.
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DR   EMBL; NWQG01000010; PDQ22750.1; -; Genomic_DNA.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000219182; Unassembled WGS sequence.
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}.
FT   DOMAIN          131..570
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        322
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           136
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           138
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           219
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           219
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           248
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           274
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           362
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         221
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         219
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   570 AA;  60609 MW;  EA4534850C79743D CRC64;
     MARITRAAYA QMYGPTVGDR VRLADTELFI EVEKDFTLHG EEVKFGGGKV IRDGMGQSQV
     SRAQGAVDTV ITNALVVDAV AGIVKADIGL RDGRIAAIGK AGNPDTQSGV TIIIGPGTEI
     IAGEGKILTA GGFDAHIHFI CPQQIEEALM SGITTMLGGG TGPAHGTLAT TCTPGPWHMA
     RMIQSFDAFP MNIGLSGKGN ASLPAALEEM VLAGACSLKL HEDWGTTPAA IDCCLSVADD
     YDVQVMIHTD TLNESGFVEN TVAAIKGRTI HAFHTEGAGG GHAPDIIKVC GLPNVIPSST
     NPTRPYTVNT LAEHLDMLMV CHHLSPSIPE DIAFAESRIR KETIAAEDIL HDIGAFSIIS
     SDSQAMGRVG EVAIRCWQTA DKMKRQRGSL PQERGDNDNF RVRRYIAKYT INPAIAHGLS
     KEIGSVAVGK RADLVLWNPA FFGVKPEMVL VGGSIAAAPM GDPNASIPTP QPMHYRPMFG
     AYGKALTNSS VTFVSRAAFD SGLQGRLGVD KQMVAVENTR GGIGKHSMVL NDATPHVEVD
     PETYEVRADG ELLTCEPATV LPMAQRYFLF
//
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