ID A0A318AIN3_9MICC Unreviewed; 314 AA.
AC A0A318AIN3;
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=DCC25_01090 {ECO:0000313|EMBL:PXA82004.1};
OS Auritidibacter sp. NML120636.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Auritidibacter.
OX NCBI_TaxID=2170743 {ECO:0000313|EMBL:PXA82004.1, ECO:0000313|Proteomes:UP000247286};
RN [1] {ECO:0000313|EMBL:PXA82004.1, ECO:0000313|Proteomes:UP000247286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML120636 {ECO:0000313|EMBL:PXA82004.1,
RC ECO:0000313|Proteomes:UP000247286};
RA Bernard K., Pacheco A.L., Burdz T., Wiebe D., Beniac D., Booth T.,
RA Goldenberger D., Seth-Smith H., Egli A., Bernier A.-M.;
RT "Auritidibacter winnipegensis sp. nov. recovered from Human Clinical
RT Materials and Emendation of the Genus Auritidibacter (Yassin et al 2011).";
RL Submitted (MAY-2018) 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:PXA82004.1}.
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DR EMBL; QHLO01000001; PXA82004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318AIN3; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000247286; 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:UP000247286}.
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; 33498 MW; 3EF56BFEC5FA14D5 CRC64;
MSTHPEPQPQ APIGIFDSGV GGLTVARSVI DQLPDENIVY VGDTAHSPYG PRPIAQVRQL
ALAIMDELVD AGVKLLVIAC NSASSAVLRD ARERYTAGYG IPVVEVIQPA VRRAVATTRN
GRVGVIGTEA TISSGAYHDM FAAAPQLEIT SVAAPEFVHF VEAGITTGER LISVAERYLA
PLKTAGVDTL VLGCTHYPLL TGVISYVMGA DVSLVTSSEA TAQSVYRALV EYQLENPAGA
TDSAPTLRPD GVPGSQREKY RFMATGNPEQ FQRLARRFLG PEVSSVQEIR TVAEEYPTGT
LRVIDQAVAE HLRA
//
