ID   MURI_SERP5              Reviewed;         287 AA.
AC   A8GL72;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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}; OrderedLocusNames=Spro_4769;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV43862.1; -; Genomic_DNA.
DR   RefSeq; WP_012147443.1; NC_009832.1.
DR   AlphaFoldDB; A8GL72; -.
DR   SMR; A8GL72; -.
DR   STRING; 399741.Spro_4769; -.
DR   EnsemblBacteria; ABV43862; ABV43862; Spro_4769.
DR   KEGG; spe:Spro_4769; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_2_0_6; -.
DR   OMA; MPWGPRT; -.
DR   OrthoDB; 1718671at2; -.
DR   UniPathway; UPA00219; -.
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   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; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..287
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000059075"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        208
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         32..33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         97..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         209..210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   287 AA;  31399 MW;  A6E0760EFFF36CFB CRC64;
     MATLLQEENT TSLEAIPSNT TAKTRPTVLV FDSGVGGLSV YQEVRQLLPD LHYIYAFDNV
     AFPYGEKSEE FIVERVLEIV SAVQQRHPLA IVIIACNTAS TVSLPALRER FTFPVVGVVP
     AIKPAARLTA NGVVGLLATR GTVQRTYTHE LIARFATDCK IELLGSSELV ELAEAKLHGE
     AVPLPTLKKI LHPWLSMREP PDTVVLGCTH FPLLAEELMQ VLPEGTRLID SGAAIARRTA
     WLISTQENLV STQEDNLAYC MALNEDTDAL LPVLQGYGFK SLKKLPV