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Database: UniProt
Entry: M7MXV2_9MICC
LinkDB: M7MXV2_9MICC
Original site: M7MXV2_9MICC 
ID   M7MXV2_9MICC            Unreviewed;       309 AA.
AC   M7MXV2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=racE {ECO:0000313|EMBL:EMQ99770.1};
GN   Synonyms=murI {ECO:0000256|HAMAP-Rule:MF_00258};
GN   ORFNames=ADIAG_00873 {ECO:0000313|EMBL:EMQ99770.1};
OS   Paeniglutamicibacter gangotriensis Lz1y.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paeniglutamicibacter.
OX   NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ99770.1, ECO:0000313|Proteomes:UP000012015};
RN   [1] {ECO:0000313|EMBL:EMQ99770.1, ECO:0000313|Proteomes:UP000012015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lz1y {ECO:0000313|EMBL:EMQ99770.1,
RC   ECO:0000313|Proteomes:UP000012015};
RX   PubMed=23766407;
RA   Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT   from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT   Station Dakshin Gangotri.";
RL   Genome Announc. 1:e00347-e00313(2013).
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:EMQ99770.1}.
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DR   EMBL; AOCK01000002; EMQ99770.1; -; Genomic_DNA.
DR   RefSeq; WP_007270077.1; NZ_AOCK01000002.1.
DR   AlphaFoldDB; M7MXV2; -.
DR   STRING; 1276920.ADIAG_00873; -.
DR   PATRIC; fig|1276920.7.peg.876; -.
DR   eggNOG; COG0796; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000012015; 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:UP000012015}.
FT   ACT_SITE        88
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        202
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         25..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         57..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         203..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   309 AA;  32527 MW;  362238F569F9BA32 CRC64;
     MTSASSSDKR ETERPRANAP LGIFDSGVGG LTVSRSIIDQ LPGESTMYVG DTANSPYGPL
     PIAQVRANAL GVMDELVDAG VKLLVIACNS ASAAVLRDAR ERYTARYGIP VVEVIQPAVR
     RAVAATRNGK IGVIGTQATV GSRAYEDAFA AAPHYSITSV ACPRFVEFVE NGITTGTELM
     ETAEAYLAPL KAAGVDTLVL GCTHYPLLTG VISYVMGEDV TLVSSAEETA KDVYRALMRH
     DLARTAPEAP THQFLATGDA DSFEILARRF LGPEVLAVEQ VDHVAAHYPT GSIAMITPAM
     VALSKASAS
//
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