ID   MURI_PHEZH              Reviewed;         283 AA.
AC   B4RCD6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN   Name=murI {ECO:0000255|HAMAP-Rule:MF_00258};
GN   OrderedLocusNames=PHZ_c0121;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Caulobacterales; Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR   EMBL; CP000747; ACG76535.1; -; Genomic_DNA.
DR   RefSeq; WP_012520683.1; NC_011144.1.
DR   AlphaFoldDB; B4RCD6; -.
DR   SMR; B4RCD6; -.
DR   STRING; 450851.PHZ_c0121; -.
DR   KEGG; pzu:PHZ_c0121; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_0_3_5; -.
DR   OrthoDB; 9801055at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001868; Chromosome.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR004391; Glu_race.
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.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..283
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000114056"
FT   ACT_SITE        70
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        206
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         7..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         71..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         207..208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   283 AA;  31045 MW;  68622AD5329B617E CRC64;
     MAIGVFDSGV GGLTVHHRLV ERFPDADFVY LADQANAPYG GRPGEEIVEL TKAGCIRLFE
     AGCDLVVLAC NTAASVALRR LQQTWLPGYR RETGRALNVL GIVVPTIEAA TGLPWEHEAE
     RRGEKVEKLD ILGVFSTPAT ARSRVYEIEI DKRRQDVAVF SEPCPELARM IEAGAPREEL
     KAVIEGHVQA LRTRIGRAPD RAILGCTHYE IVADLFREAL PPGTPLIRQP EATADALARY
     LDRHPEFDPG RSGLRRFLTT GEPGAQNSLV ETFWGGPLSF EPA
//