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Database: UniProt
Entry: X0QTJ1_9GAMM
LinkDB: X0QTJ1_9GAMM
Original site: X0QTJ1_9GAMM 
ID   X0QTJ1_9GAMM            Unreviewed;       632 AA.
AC   X0QTJ1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   31-JUL-2019, entry version 42.
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   ORFNames=JCM18900_12798 {ECO:0000313|EMBL:GAF54176.1};
OS   Psychrobacter sp. JCM 18900.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=1298608 {ECO:0000313|EMBL:GAF54176.1, ECO:0000313|Proteomes:UP000019500};
RN   [1] {ECO:0000313|EMBL:GAF54176.1, ECO:0000313|Proteomes:UP000019500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18900 {ECO:0000313|EMBL:GAF54176.1,
RC   ECO:0000313|Proteomes:UP000019500};
RA   Kudo T., Kidera A., Kida M., Kawauchi A., Shimizu R., Nakahara T.,
RA   Zhang X., Yamada A., Amano M., Hamada Y., Taniyama S., Arakawa O.,
RA   Yoshida A., Oshima K., Suda W., Kuwahara H., Nogi Y., Kitamura K.,
RA   Yuki M., Iida T., Moriya S., Inoue T., Hongo Y., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901,
RT   JCM 18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic
RT   Organisms.";
RL   Genome Announc. 2:e00280-14(2014).
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: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,
CC         ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
CC       ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|SAAS:SAAS00317636}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700,
CC       ECO:0000256|SAAS:SAAS00548017}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|RuleBase:RU004158,
CC       ECO:0000256|SAAS:SAAS00849550}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAF54176.1}.
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DR   EMBL; BAWG01000014; GAF54176.1; -; Genomic_DNA.
DR   STRING; 1298608.JCM18900_12798; -.
DR   EnsemblBacteria; GAF54176; GAF54176; JCM18900_12798.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000019500; 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; 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 {ECO:0000313|Proteomes:UP000019500};
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,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00317628}.
FT   DOMAIN      175    632       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION        1     24       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION       63     84       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     65     80       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    366    366       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       180    180       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       182    182       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       263    263       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       263    263       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       292    292       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       318    318       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       406    406       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     265    265       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     263    263       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   632 AA;  67842 MW;  E8CB1D1A950E71F0 CRC64;
     MGAAHPDEAS ESVTDKKVTA TSQKRVSRRI YAEHFGPTTG DKVRLADTEL WLQVEADLTS
     HKDTAVDQAD TSQSGESSSK PIAIKGEEVK FGGGKVIRDG MGQGQLLGAE VADTVITNAL
     VVDYTGIYKA DIGIKDGRIS AIGKAGNADI QPAIDIAIGG ATEIISGEGK ILTAGGVDSH
     IHFIAPQQCE TALMSGVTTM LGGGTGPAQG TLATTCTPGA YHIASMLKST DSIPMNIGLL
     GKGNVSVPAP IAEQIEAGAV GLKLHEDWGT TPQAIDNCLS VADDYDVQVA IHTDTLNESG
     YLESTLAAFK DRCIHTFHTE GAGGGHAPDI LKAIGESHVL PSSTNPTRPY TVNTIDEHLD
     MLMVCHHLSL AIAEDVAFAE SRIRQETIAA EDILHDLGAI SMMSSDSQAM GRVGEVVIRT
     WQTAHKMKVQ RGHLAPDATA NIEDEQQYIT LTDYDQSVDN DNFRIKRYIA KYTINPAITH
     GISDMVGSIE VGKWADMVLW SPKFFGVKPE CIIKGGLIAA VPMGDINASI PTPQPVHYRP
     MFATYPKSVA QTSITFMSQA AIDKQVDKQL GLTKVIQPVH GIRKIRKSDM RFNSYCPDMD
     INPETYEVRA DGKTLTCEPA DVLPMAQRYF LF
//
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