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Database: UniProt
Entry: A0A0P7HPK0_9MICC
LinkDB: A0A0P7HPK0_9MICC
Original site: A0A0P7HPK0_9MICC 
ID   A0A0P7HPK0_9MICC        Unreviewed;       314 AA.
AC   A0A0P7HPK0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=AO716_04470 {ECO:0000313|EMBL:KPN22359.1};
OS   Arthrobacter sp. Edens01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN22359.1, ECO:0000313|Proteomes:UP000054460};
RN   [1] {ECO:0000313|EMBL:KPN22359.1, ECO:0000313|Proteomes:UP000054460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edens01 {ECO:0000313|EMBL:KPN22359.1,
RC   ECO:0000313|Proteomes:UP000054460};
RA   Couger M.B.;
RT   "Draft Genome of Arthrobacter sp. strain Edens01.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPN22359.1}.
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DR   EMBL; LKIU01000002; KPN22359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7HPK0; -.
DR   STRING; 1732020.AO716_04470; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000054460; 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; IPR018187; Asp/Glu_racemase_AS_1.
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; PS00923; ASP_GLU_RACEMASE_1; 1.
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:UP000054460}.
FT   ACT_SITE        80
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        194
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         17..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         49..50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         195..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   314 AA;  32688 MW;  45AE7734A985DAE8 CRC64;
     MKDDLPKTTD APIGIFDSGV GGLTVARAVI DQLPNESILY VGDTAHGPYG PLPIADVRAY
     ALGVMDELVD AGVKLLVIAC NSASAAVLRD ARERYTGRYG IPVIEVIQPA VRRAVAATRS
     GRIGVIGTAA TVSSRAYDDT FAAAPHLTVS SVACPAFVEY VEAGVTAGPE LLEAAEEYLA
     PLKDDGVDTL VLGCTHYPLL TGVISYVMGE NVTLVSSAEE TAKDVYKALL THGLQRGAGV
     PPRHRFVATG DAESFELLAR RFLGPEVVRV EHADSVAARY PTGVLARITP EMIAAARAQA
     GLPAAGAALG NGAR
//
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