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Database: UniProt
Entry: E7G4V8_9HELI
LinkDB: E7G4V8_9HELI
Original site: E7G4V8_9HELI 
ID   E7G4V8_9HELI            Unreviewed;       260 AA.
AC   E7G4V8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
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   ECO:0000313|EMBL:EFX41575.1};
GN   ORFNames=HSUHS5_1033 {ECO:0000313|EMBL:EFX41575.1};
OS   Helicobacter suis HS5.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41575.1, ECO:0000313|Proteomes:UP000054093};
RN   [1] {ECO:0000313|EMBL:EFX41575.1, ECO:0000313|Proteomes:UP000054093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS5 {ECO:0000313|EMBL:EFX41575.1,
RC   ECO:0000313|Proteomes:UP000054093};
RX   PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA   Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA   De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT   "Genome sequence of Helicobacter suis supports its role in gastric
RT   pathology.";
RL   Vet. Res. 42:51-51(2011).
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:EFX41575.1}.
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DR   EMBL; ADHO01000219; EFX41575.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7G4V8; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000054093; 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; IPR033134; Asp/Glu_racemase_AS_2.
DR   InterPro; IPR004391; Glu_race.
DR   NCBIfam; TIGR00067; glut_race; 1.
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.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 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:UP000054093}.
FT   ACT_SITE        79
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        189
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         16..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         48..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         80..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   260 AA;  28668 MW;  E034B426788D6974 CRC64;
     MFKAHAGGVL RVGVFDSGVG GLSVLESLLK ARLFEHIIYY GDTARVPYGP KDPATIQKFS
     LEALDFFKPY QIDMLIVACN SVSAWALPQM RNQSKMPIVG VIEAGVLSVL KKTSQEQPIL
     ILGTKATIAS NRYAKELGAH GYKNVQSLAT GLFVPLIEEG VLEGPLLEAC MVHYFKDLKC
     APSVVVLGCT HFPWIVSSLK GYFLERFKTP CEFVHSGEAI VEYLQEKYNL LSRNQESNLE
     LFASGDVSLL KQLAHSLRSK
//
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