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Database: UniProt
Entry: X2H7E9_9NEIS
LinkDB: X2H7E9_9NEIS
Original site: X2H7E9_9NEIS 
ID   X2H7E9_9NEIS            Unreviewed;       268 AA.
AC   X2H7E9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=SALWKB2_0963 {ECO:0000313|EMBL:AHN28345.1};
OS   Snodgrassella alvi wkB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Snodgrassella.
OX   NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN28345.1, ECO:0000313|Proteomes:UP000019668};
RN   [1] {ECO:0000313|EMBL:AHN28345.1, ECO:0000313|Proteomes:UP000019668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WkB2 {ECO:0000313|EMBL:AHN28345.1};
RX   PubMed=25053814;
RA   Kwong W.K., Engel P., Koch H., Moran N.A.;
RT   "Genomics and host specialization of honey bee and bumble bee gut
RT   symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
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}.
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DR   EMBL; CP007446; AHN28345.1; -; Genomic_DNA.
DR   AlphaFoldDB; X2H7E9; -.
DR   STRING; 1196094.SALWKB2_0963; -.
DR   KEGG; salv:SALWKB2_0963; -.
DR   PATRIC; fig|1196094.4.peg.964; -.
DR   HOGENOM; CLU_052344_0_2_4; -.
DR   OrthoDB; 9801055at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000019668; 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   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}.
FT   ACT_SITE        75
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         12..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         188..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   268 AA;  29441 MW;  BD4597CBD10D4AB6 CRC64;
     MTAIQQPIGV FDSGVGGLTV VRALMERLPN ENIIYFGDTA RVPYGMKSRH TIEVYTEQIV
     SFLLEHDVKA LVVACNTIAA VAREKVRQLA GTMPVLDVIA AGAQAALETT QNNHIGVIAT
     STTVNSNAYA RAIHNQNAQT RVFSQACPLL VPLVEEGWLD HEVTRLTARE YLKPILAEEV
     DTLVLGCTHY PLLKPLIRQE APDLKLVDSA ITTAEATALA LEQHNLINPD HSGAQYRFYV
     SDIPLRFQTI GERFLGRSLE QLEMVSLG
//
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