ID A4J3X1_DESRM Unreviewed; 282 AA.
AC A4J3X1;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 OrderedLocusNames=Dred_1240 {ECO:0000313|EMBL:ABO49774.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49774.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO49774.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO49774.1,
RC ECO:0000313|Proteomes:UP000001556};
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 Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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}.
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DR EMBL; CP000612; ABO49774.1; -; Genomic_DNA.
DR AlphaFoldDB; A4J3X1; -.
DR STRING; 349161.Dred_1240; -.
DR KEGG; drm:Dred_1240; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_1_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001556; 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 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:UP000001556}.
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 25..26
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 57..58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 199..200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ SEQUENCE 282 AA; 30762 MW; 98637A085897B408 CRC64;
MNYSIYQSYL EVIFLSQRAP IGVFDSGVGG LSVARDIRKL LPLEDIIYYA DSAYCPYGDK
DPQTIRQREK AIGEFLVSQG CKLIVVACNT ASSAGLEYLR RFLKVPVVGM EPGVKPAVAA
TRNGKIGVLA TCVTIAGDRF SSLVKRYAEE TEVITQPCPG LVELIESGKL NAPETEEKLR
TFLQPILDKK ADTIVLGCTH YPFLRPMLES LAGPGVSVID TGQAVAKQVS RVLSACNLAK
NSGPLGTEQF YTSGNQTEVE EVIRTLWLRD NISVKTLPLN VK
//
