ID A0A074J840_9RHOB Unreviewed; 270 AA.
AC A0A074J840;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=TP2_07220 {ECO:0000313|EMBL:KEO52724.1};
OS Thioclava pacifica DSM 10166.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353537 {ECO:0000313|EMBL:KEO52724.1, ECO:0000313|Proteomes:UP000027432};
RN [1] {ECO:0000313|EMBL:KEO52724.1, ECO:0000313|Proteomes:UP000027432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10166 {ECO:0000313|EMBL:KEO52724.1,
RC ECO:0000313|Proteomes:UP000027432};
RA Lai Q., Shao Z.;
RT "Thioclava pacifica DSM 10166 Genome Sequencing.";
RL Submitted (JUL-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:KEO52724.1}.
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DR EMBL; AUND01000023; KEO52724.1; -; Genomic_DNA.
DR RefSeq; WP_038076844.1; NZ_AUND01000023.1.
DR AlphaFoldDB; A0A074J840; -.
DR STRING; 1353537.TP2_07220; -.
DR eggNOG; COG0796; Bacteria.
DR OrthoDB; 9801055at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000027432; 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; IPR004391; Glu_race.
DR PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1.
DR PANTHER; PTHR21198:SF3; 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.
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:UP000027432}.
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 7..8
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 195..196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ SEQUENCE 270 AA; 29210 MW; 2270EC9FB8866195 CRC64;
MAVGVFDSGL GGLTVYDACA KRLPDVAFCY YGDNAHAPYG VRDADDIFNL TCAGVERLWD
EGCDLVILAC NTASAAALKR MQETWIPEGK RVLGVFVPMI EALTERKWGD NSPPREVAVK
HVALFATPAT VASRAFQREL AFRAIGVDVE AQPCGGVVDA IETGDEILAE ALVKSHVEAL
KRRMPHPEAA ILGCTHYPLM QKTFQEALGA NVDVYSQANL VAESLADYLT RRPEFIGAGT
TSKFLTTGDP ASVSSHATQF LRYPIRFEAA
//
