ID   MURI_CAMJE              Reviewed;         250 AA.
AC   Q9PM24; Q0P7X6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=Cj1652c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RG   Center for structural genomics of infectious diseases (CSGID);
RT   "Crystal structure of glutamate racemase from Campylobacter jejuni subsp.
RT   jejuni.";
RL   Submitted (NOV-2011) to the PDB data bank.
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}.
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; AL111168; CAL35749.1; -; Genomic_DNA.
DR   PIR; B81262; B81262.
DR   RefSeq; WP_002851499.1; NC_002163.1.
DR   RefSeq; YP_002345021.1; NC_002163.1.
DR   PDB; 3UHF; X-ray; 1.83 A; A/B=1-250.
DR   PDB; 3UHO; X-ray; 2.20 A; A/B=1-250.
DR   PDB; 3UHP; X-ray; 2.79 A; A/B=1-250.
DR   PDBsum; 3UHF; -.
DR   PDBsum; 3UHO; -.
DR   PDBsum; 3UHP; -.
DR   AlphaFoldDB; Q9PM24; -.
DR   SMR; Q9PM24; -.
DR   IntAct; Q9PM24; 18.
DR   STRING; 192222.Cj1652c; -.
DR   PaxDb; Q9PM24; -.
DR   PRIDE; Q9PM24; -.
DR   EnsemblBacteria; CAL35749; CAL35749; Cj1652c.
DR   GeneID; 905925; -.
DR   KEGG; cje:Cj1652c; -.
DR   PATRIC; fig|192222.6.peg.1628; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_0_2_7; -.
DR   OMA; LDFFKPH; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000799; 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   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   1: Evidence at protein level;
KW   3D-structure; Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..250
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095462"
FT   ACT_SITE        70
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   ACT_SITE        180
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   BINDING         7..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT                   ECO:0000269|Ref.2, ECO:0007744|PDB:3UHF,
FT                   ECO:0007744|PDB:3UHO"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT                   ECO:0000269|Ref.2, ECO:0007744|PDB:3UHF,
FT                   ECO:0007744|PDB:3UHO"
FT   BINDING         71..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT                   ECO:0000269|Ref.2, ECO:0007744|PDB:3UHF,
FT                   ECO:0007744|PDB:3UHO"
FT   BINDING         181..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT                   ECO:0000269|Ref.2, ECO:0007744|PDB:3UHF,
FT                   ECO:0007744|PDB:3UHO"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           13..21
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           44..58
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:3UHP"
FT   HELIX           93..104
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          111..115
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           117..122
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           124..130
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           145..150
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           157..167
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:3UHP"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           187..194
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           203..214
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:3UHF"
FT   HELIX           234..244
FT                   /evidence="ECO:0007829|PDB:3UHF"
SQ   SEQUENCE   250 AA;  28084 MW;  6F0CE3981E24DE5F CRC64;
     MKIGVFDSGV GGLSVLKSLY EARLFDEIIY YGDTARVPYG VKDKDTIIKF CLEALDFFEQ
     FQIDMLIIAC NTASAYALDA LRAKAHFPVY GVIDAGVEAT IKALHDKNKE ILVIATKATI
     KSEEYQKRLL SQGYTNINAL ATGLFVPMVE EGIFEGDFLQ SAMEYYFKNI TTPDALILAC
     THFPLLGRSL SKYFGDKTKL IHSGDAIVEF LKERENIDLK NHKAKLHFYA SSDVESLKNT
     AKIWLNLLRK