ID C7ME08_BRAFD Unreviewed; 270 AA.
AC C7ME08;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Bfae_20070 {ECO:0000313|EMBL:ACU85815.1};
OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU85815.1, ECO:0000313|Proteomes:UP000001919};
RN [1] {ECO:0000313|EMBL:ACU85815.1, ECO:0000313|Proteomes:UP000001919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX PubMed=21304631; DOI=10.4056/sigs.492;
RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachybacterium faecium type strain
RT (Schefferle 6-10).";
RL Stand. Genomic Sci. 1:3-11(2009).
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; CP001643; ACU85815.1; -; Genomic_DNA.
DR RefSeq; WP_015776024.1; NC_013172.1.
DR RefSeq; YP_003155405.1; NC_013172.1.
DR AlphaFoldDB; C7ME08; -.
DR STRING; 446465.Bfae_20070; -.
DR KEGG; bfa:Bfae_20070; -.
DR PATRIC; fig|446465.5.peg.1991; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_1_11; -.
DR OrthoDB; 9801055at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001919; 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:UP000001919}.
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT ACT_SITE 183
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 10..11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ SEQUENCE 270 AA; 29024 MW; 9146335D6FF07D91 CRC64;
MNNAPIGIFD SGVGGLTVAR AVLDQLPQEE LVYIGDTAHG PYGPRPIAEV RSLALEIMDE
LVGHGVKMLV IACNTASAAV LRDARERYDV PVIEVIQPAV RRAVAATRNR RVGVIATEGT
VTSRAYEDAF AAAPDLTLTA QACPRFVEFV ENGVVSGREV VEMAEEYLAP VREAEVDTLV
LGCTHYPMLA GPISYVMGPD VTLVSSAEET ALDVYSQLQA TEQLRETQRP PRHVFSQTAF
GTGSENFARL SRRFLGPTLE TTASLPAVLA
//
