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Database: UniProt
Entry: A0A132SE04_9MYCO
LinkDB: A0A132SE04_9MYCO
Original site: A0A132SE04_9MYCO 
ID   A0A132SE04_9MYCO        Unreviewed;       571 AA.
AC   A0A132SE04;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   11-DEC-2019, entry version 23.
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:KWX57267.1};
GN   ORFNames=ASJ79_11945 {ECO:0000313|EMBL:KWX57267.1};
OS   Mycobacterium sp. NAZ190054.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX57267.1, ECO:0000313|Proteomes:UP000070146};
RN   [1] {ECO:0000313|EMBL:KWX57267.1, ECO:0000313|Proteomes:UP000070146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX57267.1,
RC   ECO:0000313|Proteomes:UP000070146};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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:KWX57267.1}.
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DR   EMBL; LMVQ01000564; KWX57267.1; -; Genomic_DNA.
DR   RefSeq; WP_067962254.1; NZ_LMVQ01000564.1.
DR   EnsemblBacteria; KWX57267; KWX57267; ASJ79_11945.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000070146; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070146}.
FT   DOMAIN          135..571
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        323
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           140
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           142
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           220
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           220
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           249
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           275
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           363
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         222
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         220
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   571 AA;  60657 MW;  8E87DD2402682E66 CRC64;
     MAHRITRRHY AELYGPTTGD RVRLADTELL AEVEHDATVY GDESVFGGGK TMREGMAVHG
     DLTNADGALD FVITNVLIVD AVLGIRKADI GIRNGRIAGI GKSGNPRTMD GVDPELVIGA
     STDIRAGEGM IATAGAIDVH VHFDSAGLVE EAISSGITTM IGGGLGPVTV GITSSGPNNL
     ARMLRAAEGF PMNFGFIGNG SASSTAPLIE QGLAGAIGYK IHEDWGATPA AIRASLDAGD
     ELDLQVQIHT DTLNESGFFE DTMAAIGGRP IHTYHAEGAG GGHAPDIMRV VGQPYCLPSS
     TNPTNPFTLN TFDEHLDMVM VCHHLNPRIP EDVAFAESRI RRETIAAEDV LHDMGAISAM
     GSDSQGMGRI GETIARTWQL ASHMRATRGP LSGDEGTGAD NARILRYVAK LTINPAKLFG
     IDHEVGSLEP GKLADIVLWE PKFFGIRPEV VFKGGFPAWS VMGEANASLM TCEPLRYRPQ
     WAAFGRTPAD VSVNFVAGAA VEAGLGERLG LDTRLVACRG ARALTKADLL HNDYLPDISI
     EPDTYRVTVD GEPCVSTPMS QVPLGRRYTL K
//
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