URE1_CORGL
ID URE1_CORGL Reviewed; 570 AA.
AC Q79VJ3; Q9L420; Q9RHM4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953};
GN OrderedLocusNames=Cgl0086, cg0115;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=11328647; DOI=10.3109/10425170009033989;
RA Puskas L.G., Inui M., Yukawa H.;
RT "Structure of the urease operon of Corynebacterium glutamicum.";
RL DNA Seq. 11:383-394(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=10930756; DOI=10.1111/j.1574-6968.2000.tb09248.x;
RA Nolden L., Beckers G., Moeckel B., Pfefferle W., Nampoothiri K.M.,
RA Kraemer R., Burkovski A.;
RT "Urease of Corynebacterium glutamicum: organization of corresponding genes
RT and investigation of activity.";
RL FEMS Microbiol. Lett. 189:305-310(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15516578; DOI=10.1128/jb.186.22.7645-7652.2004;
RA Beckers G., Bendt A.K., Kraemer R., Burkovski A.;
RT "Molecular identification of the urea uptake system and transcriptional
RT analysis of urea transporter- and urease-encoding genes in Corynebacterium
RT glutamicum.";
RL J. Bacteriol. 186:7645-7652(2004).
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:0000255|HAMAP-Rule:MF_01953};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01953};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- INDUCTION: By urea and nitrogen starvation.
CC {ECO:0000269|PubMed:11328647, ECO:0000269|PubMed:15516578}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- DISRUPTION PHENOTYPE: Cells are urease negative and are no longer able
CC to transport urea. {ECO:0000269|PubMed:10930756,
CC ECO:0000269|PubMed:11328647}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
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DR EMBL; AB029154; BAA88554.1; -; Genomic_DNA.
DR EMBL; AJ251883; CAB81937.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97479.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18654.1; -; Genomic_DNA.
DR RefSeq; NP_599338.1; NC_003450.3.
DR RefSeq; WP_011013378.1; NC_006958.1.
DR AlphaFoldDB; Q79VJ3; -.
DR SMR; Q79VJ3; -.
DR STRING; 196627.cg0115; -.
DR MEROPS; M38.982; -.
DR KEGG; cgb:cg0115; -.
DR KEGG; cgl:Cgl0086; -.
DR PATRIC; fig|196627.13.peg.87; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_11; -.
DR OMA; CHHLSHD; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000582; 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; IPR005848; Urease_asu.
DR InterPro; IPR017951; Urease_asu_c.
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; PS51368; UREASE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..570
FT /note="Urease subunit alpha"
FT /id="PRO_0000234152"
FT DOMAIN 132..570
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 323
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 137
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 139
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
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:0000255|HAMAP-Rule:MF_01953"
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:0000255|HAMAP-Rule:MF_01953"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 249
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 275
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 363
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT MOD_RES 220
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT CONFLICT 40
FT /note="I -> V (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..134
FT /note="GI -> AL (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="S -> A (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 259..263
FT /note="VEDTI -> CGRH (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="R -> G (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="H -> N (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="D -> E (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="R -> G (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> G (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..307
FT /note="PTLPY -> QRFRN (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="V -> L (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="G -> D (in Ref. 1; BAA88554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 61452 MW; 2C5F5D9F7F5FBB2E CRC64;
MSFEISRKQY TDLYGPTVGD SVRLADTELF LCVEKDYAAI GEEVAFGGGK VIRDGMGQNG
TLVRDVDIPD TVITNVIVLD YTGVYKADVA LRDGKIFRIG KAGNPNVMEN VDIVIGVATD
IIAGEGKILT AGGIDTHVHF LGTDQVNTAL ASGITTMIGG GTGPSQASMA TTVTPGQWNT
YNMLSAFEGM PMNFGILGKG HGSSKSPLAE QVRAGAIGLK IHEDWGATPS SINTALEVAD
DMDIQVALHS DTLNEAGFVE DTIEAIAGRV IHTFHTEGAG GGHAPDLIRV AALPNVLPAS
TNPTLPYTRN TVEEHLDMVM VAHHLNPDIP EDVAFADSRI RAETIAAEDV LHDMGIFSIT
SSDSQAMGRV GETITRTWQV ADHMKRTRGS LTGDAPYNDN NRLRRFIAKY TINPAIAHGV
DYVVGSVEEG KFADLVLWDP KFFGVKPDLV IKGGLMVNSL MGDSNGSIPT PQPRTLRNTW
GAFGQAVSRS SITFLSQDAI DANVPDLLNL RKQIRGVRGV RNLTKRDMKL NAEMPDIRVD
PETYQVFVNG ELITSKPAET VPMARRYFLF
