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Database: UniProt
Entry: K2KYH7_9GAMM
LinkDB: K2KYH7_9GAMM
Original site: K2KYH7_9GAMM 
ID   K2KYH7_9GAMM            Unreviewed;       257 AA.
AC   K2KYH7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=A10D4_00880 {ECO:0000313|EMBL:EKE87604.1};
OS   Idiomarina xiamenensis 10-D-4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE87604.1, ECO:0000313|Proteomes:UP000014115};
RN   [1] {ECO:0000313|EMBL:EKE87604.1, ECO:0000313|Proteomes:UP000014115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-D-4 {ECO:0000313|EMBL:EKE87604.1,
RC   ECO:0000313|Proteomes:UP000014115};
RX   PubMed=23209204; DOI=10.1128/JB.01855-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL   J. Bacteriol. 194:6938-6938(2012).
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:EKE87604.1}.
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DR   EMBL; AMRG01000001; EKE87604.1; -; Genomic_DNA.
DR   RefSeq; WP_008487116.1; NZ_AMRG01000001.1.
DR   AlphaFoldDB; K2KYH7; -.
DR   STRING; 740709.A10D4_00880; -.
DR   PATRIC; fig|740709.3.peg.176; -.
DR   eggNOG; COG0796; Bacteria.
DR   OrthoDB; 9801055at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000014115; 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:UP000014115}.
FT   ACT_SITE        70
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        183
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         7..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         71..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         184..185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   257 AA;  28104 MW;  E098379EBF0744E4 CRC64;
     MKVGVFDSGV GGLTVAKSLY ESRLFSDIVY YGDTARVPYG SKDQNTVLRY ALEAIEFFNG
     VDVDFVVVAC NTVSVVALAQ MQQYSNKPVY GVIEPGVLAL QQRQLDKNDD RILVIATKAT
     INSGEYQRRI EALGYGQVIA RATPLFVPLV EEQCYQGPIL DAVLQHYFAD LSAHAITTVV
     LGCTHYPLIA QAIAAYFNGA LTIHSGEAMV AWLQQQLQLN AHFDKTRVTI YASENVAAVK
     RVAAQWGLPL QSDAPAK
//
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