ID A0A823QFJ8_CAMCO Unreviewed; 247 AA. AC A0A823QFJ8; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. 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=EGY89_02030 {ECO:0000313|EMBL:EAH6088553.1}; OS Campylobacter coli. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195 {ECO:0000313|EMBL:EAH6088553.1, ECO:0000313|Proteomes:UP000562567}; RN [1] {ECO:0000313|EMBL:EAH6088553.1, ECO:0000313|Proteomes:UP000562567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSIS11815446 {ECO:0000313|EMBL:EAH6088553.1, RC ECO:0000313|Proteomes:UP000562567}; RG NARMS: The National Antimicrobial Resistance Monitoring System; RL Submitted (NOV-2018) 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:EAH6088553.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AABIGR010000002; EAH6088553.1; -; Genomic_DNA. DR RefSeq; WP_002871893.1; NZ_CXZA01000444.1. DR UniPathway; UPA00219; -. DR Proteomes; UP000562567; Unassembled WGS sequence. DR GO; GO:0016853; F:isomerase activity; 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 {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00258}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00258}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00258}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00258}. FT REGION 7..8 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258" FT REGION 39..40 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258" FT REGION 71..72 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258" FT REGION 181..182 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258" FT ACT_SITE 70 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258" FT ACT_SITE 180 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258" SQ SEQUENCE 247 AA; 27685 MW; 181E24DE52BF12E4 CRC64; MKIGVFDSGV GGLSVLKSLY EARLFDEIIY YGDTARVPYG VKDKDTIIKF CLEALDFFEQ FQIDMLIIAC NTASAYALDA LRAKAHFPVY GVIDAGVEAT IKALHDKNKE ILVIATKATI KSEEYQKRLL SQGYTNINAL ATGLFVPMVE EGIFEGDFLQ SAMEYYFKNI TTPDALILAC THFPLLGRSL SKYFGDKTKL IHSGDAIVEF LKERENIDLK NHKAKLHFYA SSDVKSLKNT AKIWLNL //