ID U7MYB3_9CORY Unreviewed; 277 AA.
AC U7MYB3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Glutamate racemase {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
GN Name=murI {ECO:0000256|HAMAP-Rule:MF_00258};
GN ORFNames=HMPREF1290_00175 {ECO:0000313|EMBL:ERS75115.1};
OS Corynebacterium sp. KPL1989.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203622 {ECO:0000313|EMBL:ERS75115.1, ECO:0000313|Proteomes:UP000017102};
RN [1] {ECO:0000313|EMBL:ERS75115.1, ECO:0000313|Proteomes:UP000017102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1989 {ECO:0000313|EMBL:ERS75115.1,
RC ECO:0000313|Proteomes:UP000017102};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1989.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC biosynthesis. {ECO:0000256|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:0000256|ARBA:ARBA00001602, ECO:0000256|HAMAP-
CC Rule:MF_00258};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00258}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000256|HAMAP-Rule:MF_00258}.
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:ERS75115.1}.
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DR EMBL; AXLR01000001; ERS75115.1; -; Genomic_DNA.
DR RefSeq; WP_021354064.1; NZ_KI515716.1.
DR AlphaFoldDB; U7MYB3; -.
DR GeneID; 42781831; -.
DR PATRIC; fig|1203622.3.peg.167; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_1_11; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000017102; Unassembled WGS sequence.
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 Gene3D; 3.40.50.1860; -; 2.
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 NCBIfam; TIGR00067; glut_race; 1.
DR PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1.
DR PANTHER; PTHR21198:SF2; GLUTAMATE RACEMASE; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; Aspartate/glutamate racemase; 2.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00258};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00258};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258};
KW Reference proteome {ECO:0000313|Proteomes:UP000017102}.
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT ACT_SITE 192
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 19..20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 51..52
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 193..194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ SEQUENCE 277 AA; 29556 MW; 8163E03538A23204 CRC64;
MSNRTPRQLD REAPIGIFDS GVGGLTVART IMDQLPNESV LYIGDTAHGP YGPLPIAQVR
SHAQRVADEL VERGCKMLVI ACNTATAAFL HDARERYDVP VVEVIQPAVR RAMATTRNGK
IGVIGTEGTV KSGAYQDMFR LNPAVTAQAV ACPAFVDFVE RGITSGRQIL GVAQGYVEPL
QSAGVDTLVL GCTHYPLLSG VLQLAIGENV TLVSSAEETA KDVLRHLTEL DLLATGKKQQ
RIFESTGDPE KFAELSQRFL GLGVGEVTRS ATGVGKA
//
