GenomeNet

Database: UniProt
Entry: A0A124DZI1_9MYCO
LinkDB: A0A124DZI1_9MYCO
Original site: A0A124DZI1_9MYCO 
ID   A0A124DZI1_9MYCO        Unreviewed;       573 AA.
AC   A0A124DZI1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   08-MAY-2019, entry version 28.
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:GAS87435.1};
GN   ORFNames=RMCB_1531 {ECO:0000313|EMBL:GAS87435.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS87435.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS87435.1, ECO:0000313|Proteomes:UP000069620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS87435.1,
RC   ECO:0000313|Proteomes:UP000069620};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species,
RT   M. thermoresistibile, M. fortuitum subsp. acetamidolyticum, M.
RT   canariasense, M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
RN   [2] {ECO:0000313|Proteomes:UP000069620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|Proteomes:UP000069620};
RA   Katahira K., Gotou Y., Iida K., Ogura Y., Hayashi T.;
RT   "Draft genome sequence of five rapidly growing Mycobacterium
RT   species.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:GAS87435.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; BCSX01000018; GAS87435.1; -; Genomic_DNA.
DR   RefSeq; WP_029373425.1; NZ_BCSX01000018.1.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; GCF_001570425:G1ER5-1522-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000069620; 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:UP000069620};
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:UP000069620}.
FT   DOMAIN      135    573       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    323    323       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       140    140       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       142    142       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       220    220       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       220    220       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       249    249       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       275    275       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       363    363       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     222    222       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     220    220       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   573 AA;  60647 MW;  3075346EF52FA009 CRC64;
     MTHRISRQRY AELYGPTVGD RVRLADTELL AKVEADATVY GDEAVFGGGK TMREGMAVHG
     DVTNAEGALD FVITNALIID AVLGIRKADI GIRNGRIAGI GKAGNPRTMA GVDPELIIGA
     GTDIRSGEGM IATAGAIDVH VHFDSAGLVE EAISSGITTM IGGGLGPVTV GITSSGPTNL
     ARMLKAAEAF PMNFGFLGNG SASSTAPLIE QGLAGAIGYK IHEDWGATPA AIRASLDAGD
     ELDLQVQIHS DTLNEAGFFE DTMAAIGGRP IHTYHAEGAG GGHAPDIMRV VGESYCLPSS
     TNPTNPYTLN TFDEHLDMVM VCHHLNPRIR EDVAFAESRI RRETIAAEDV LHDLGAISAM
     GSDSQGMGRI GESIARTWQL ASHMRATRGP LPEDVTSGAP ADNARILRYI AKLTINPAIL
     FGIDHEVGSL EPGKLADIVL WEPKFFGIRP EVVFKGGFPA WSVMGEANAS LMTCEPLKYR
     PQWAAYGRTP ADVSVNFVAE GAIAGGLAGK LDLQTPLVAC RGARSLTKAD LLHNNYLPDI
     SIEPDTYRVI VDGELCTSTP MTAVPLGRRY TLK
//
DBGET integrated database retrieval system