MURI_CORGL
ID MURI_CORGL Reviewed; 273 AA.
AC Q9XDZ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258};
GN OrderedLocusNames=Cgl2509, cg2762;
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].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=10386367; DOI=10.1111/j.1574-6968.1999.tb13619.x;
RA Malathi K.C., Wachi M., Nagai K.;
RT "Isolation of the murI gene from Brevibacterium lactofermentum ATCC 13869
RT encoding D-glutamate racemase.";
RL FEMS Microbiol. Lett. 175:193-196(1999).
RN [2]
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 [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=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).
CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00258};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA78374.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB99902.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAF21172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020624; BAA78374.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000036; BAB99902.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927155; CAF21172.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_601711.1; NC_003450.3.
DR AlphaFoldDB; Q9XDZ7; -.
DR SMR; Q9XDZ7; -.
DR STRING; 196627.cg2762; -.
DR KEGG; cgb:cg2762; -.
DR KEGG; cgl:Cgl2509; -.
DR PATRIC; fig|196627.13.peg.2442; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_1_11; -.
DR OMA; MPWGPRT; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR HAMAP; MF_00258; Glu_racemase; 1.
DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR InterPro; IPR001920; Asp/Glu_race.
DR InterPro; IPR018187; Asp/Glu_racemase_AS_1.
DR InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR InterPro; IPR004391; Glu_race.
DR PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; SSF53681; 2.
DR TIGRFAMs; TIGR00067; glut_race; 1.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..273
FT /note="Glutamate racemase"
FT /id="PRO_0000095468"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 190
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 17..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 49..50
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 191..192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT CONFLICT 144
FT /note="V -> E (in Ref. 1; BAA78374)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="Q -> L (in Ref. 1; BAA78374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29230 MW; B332C3DB9A1477C1 CRC64;
MIERPVPGAD APIGIFDSGV GGLTVARTII DQLPHESVIY IGDTANGPYG PLPIAKVREH
AIRIADELVE RGCKMIVIAC NTASAAFLRD ARERYSVPVV EVILPAVRRA VASTRNGKVG
VIGTVGTINS GAYQDLFSAS PSIVVNAVAC PRFVDFVERG ITSGRQILNI AQDYLEPLQA
EGVDTLVLGC THYPLLSGVI QLAMGDHVSL VSSAEETAKD VLRILSQQDL LADPDMHPEP
SYSFESTGDP EIFAQLSRRF LGPIVSQVRQ NEG
