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Database: UniProt
Entry: F8A814_THEID
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ID   F8A814_THEID            Unreviewed;       567 AA.
AC   F8A814;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   08-MAY-2019, entry version 59.
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=Thein_1137 {ECO:0000313|EMBL:AEH45007.1};
OS   Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC   Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales;
OC   Thermodesulfobacteriaceae; Thermodesulfatator.
OX   NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH45007.1, ECO:0000313|Proteomes:UP000006793};
RN   [1] {ECO:0000313|Proteomes:UP000006793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC   {ECO:0000313|Proteomes:UP000006793};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Saunders L., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEH45007.1, ECO:0000313|Proteomes:UP000006793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC   {ECO:0000313|Proteomes:UP000006793};
RX   PubMed=22768359; DOI=10.4056/sigs.2665915;
RA   Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA   Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA   Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D.,
RA   Chang Y.J., Brambilla E.M., Rohde M., Spring S., Goker M.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT   bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL   Stand. Genomic Sci. 6:155-164(2012).
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}.
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DR   EMBL; CP002683; AEH45007.1; -; Genomic_DNA.
DR   RefSeq; WP_013907749.1; NC_015681.1.
DR   STRING; 667014.Thein_1137; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; AEH45007; AEH45007; Thein_1137.
DR   KEGG; tid:Thein_1137; -.
DR   PATRIC; fig|667014.3.peg.1171; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; TIND667014:G1GYJ-1173-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000006793; 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   Complete proteome {ECO:0000313|Proteomes:UP000006793};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006793}.
FT   DOMAIN      129    567       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    320    320       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       134    134       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       136    136       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       217    217       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       217    217       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       246    246       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       272    272       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       360    360       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     219    219       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     217    217       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   567 AA;  61943 MW;  F7755A58690FAD80 CRC64;
     MKIDRKKYAE LYGPTVGDKI RLGDTELIIE IEKDFTTYGE EVVFGAGKNI RDGMGQTNTK
     IDAPDLVITN VIILDYTGIV KADIGIKNGY ICGIGKAGNP DTMDNVTPGL EIGPFTEIIS
     GEGLIATAGA VDKHVHFISP QIVYEALSNG VTTLIGGGDG PTTGTNATNA TPGPWNIHRM
     LEAIEEFPVN IGLIGKGNSS NPKMLIEQLK EGAMGFKIHE DWGATPNVID VVLDVADEYD
     VMVALHTDTP NEAGYVENTI ASLKGRTIHT YHSEGAGGGH APDILRIAGL PNVLPSSTTP
     TLPATINTVT EHVDMLIVCH HLKPEVPEDV AFAKSRIRAQ TILAEDVLHD MGVISIVSSD
     SQAMGRIGET VLRTWQMAHS MKVQRGKLPE DSEGNDNFRV KRYIAKYTIN PAIACGVSKY
     VGSIEPGKLA DIVLWDPKFF GVKPSLVLKS GFVVWSLMGD ANASIPTCEP YMYKPMFGSF
     GKARQTLSLT FVSKLAYEND IKNKLKLNRQ FKPVEECRQI GKKNMIFNDF VGEVYVDPKT
     YEVFVNGTKI ESNFMKELPL AQRYFLF
//
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