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Database: UniProt
Entry: A0A323VV45_9ACTN
LinkDB: A0A323VV45_9ACTN
Original site: A0A323VV45_9ACTN 
ID   A0A323VV45_9ACTN        Unreviewed;       269 AA.
AC   A0A323VV45;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=DMO24_03730 {ECO:0000313|EMBL:PZA22698.1}, FHX36_001854
GN   {ECO:0000313|EMBL:MBB3676119.1};
OS   Modestobacter versicolor.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=429133 {ECO:0000313|EMBL:PZA22698.1, ECO:0000313|Proteomes:UP000247602};
RN   [1] {ECO:0000313|EMBL:PZA22698.1, ECO:0000313|Proteomes:UP000247602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP153-2 {ECO:0000313|EMBL:PZA22698.1,
RC   ECO:0000313|Proteomes:UP000247602};
RA   Gundlapally S.R.;
RT   "Draft genome sequence of Modestobacter versicolor CP153-2.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB3676119.1, ECO:0000313|Proteomes:UP000580718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16678 {ECO:0000313|EMBL:MBB3676119.1,
RC   ECO:0000313|Proteomes:UP000580718};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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:PZA22698.1}.
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DR   EMBL; JACIBU010000001; MBB3676119.1; -; Genomic_DNA.
DR   EMBL; QKNV01000022; PZA22698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A323VV45; -.
DR   OrthoDB; 9801055at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000247602; Unassembled WGS sequence.
DR   Proteomes; UP000580718; 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:UP000247602}.
FT   ACT_SITE        75
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        185
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         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   269 AA;  28026 MW;  99BD736262E1B337 CRC64;
     MTTADAPIGI FDSGVGGLTV ARAVLDQLPT ESIRYVGDTA HSPYGPKPIA EVRRHSLAVM
     DDLVAAGVKM LVIACNSASA ACLGDARERY DVPVVEVVLP AVRRATAATR NGRVGVIGTQ
     ATITSGAYED AFAAAPQLTV TSAACPSFVD FVERGITSGR QLVGLAQSYL DPLLAADVDT
     VVLGCTHYPL LTGVLSLVLG DEVTLVSSAE ETAKDVYRVL TRTDLLRDPE GPPPVHAFLA
     TGDPEPFARL GRRFLGPEVD AVSRTGAAA
//
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