ID A4T7D8_MYCGI Unreviewed; 571 AA.
AC A4T7D8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 123.
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=Mflv_1685 {ECO:0000313|EMBL:ABP44167.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP44167.1};
RN [1] {ECO:0000313|EMBL:ABP44167.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP44167.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP44167.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP44167.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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};
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|ARBA:ARBA00004897,
CC ECO:0000256|HAMAP-Rule:MF_01953}.
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}.
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}.
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DR EMBL; CP000656; ABP44167.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T7D8; -.
DR STRING; 350054.Mflv_1685; -.
DR MEROPS; M38.982; -.
DR KEGG; mgi:Mflv_1685; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_11; -.
DR OrthoDB; 9802793at2; -.
DR UniPathway; UPA00258; UER00370.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR01792; urease_alph; 1.
DR PANTHER; PTHR43440; UREASE; 1.
DR PANTHER; PTHR43440:SF1; UREASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01953};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01953};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01953}.
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"
FT BINDING 140
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 142
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 220
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 220
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 249
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 275
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 363
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
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; 60637 MW; 9FB269D3B53E7455 CRC64;
MGHRISRSHY AELYGPTTGD RVRLADTELL AKVEHDATVY GDESVFGGGK TMREGMAVHG
DITNADGALD FVITNVLIID AVLGIRKADI GIRDGRIAGI GKSGNPRTMD GVDPDLVIGA
GTDIRAGEGM IATAGGIDVH VHFDSAGLVE EAISSGITTM IGGGLGPVTV GITTSGPNNL
ARMLRAAEGF PMNFGFIANG SASSTAPLIE QGLAGAIGYK IHEDWGATPA AIRASLDAGD
ELDLQVQIHT DTLNESGFFE DTMRAIGGRP IHTYHAEGAG GGHAPDIMRV VGEPYCLPSS
TNPTNPYTLN TFDEHLDMVM VCHHLSPRIP EDVAFAESRI RRETIAAEDV LHDLGAISAM
GSDSQGMGRI GETIARTWQL ASHMRATRGP LPGDEGTGAD NARILRYVAK LTINPARLFG
IDHEVGSLEP GKLADIVLWE PKFFGIRPEV VFKGGFPAWS VMGEANASLM TCEPLRYRPQ
WAAFGRAPAD VSVNFVAGAA IDAGLGQQLG LDTRLVACRG ARALTKADLL HNDHLPDIRI
EPDTYRVTVD GQPCVSTPMT EVPLGRRYTL K
//
