ID A0A1E7R1D9_9GAMM Unreviewed; 286 AA.
AC A0A1E7R1D9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ECO:0000313|EMBL:KAA8733343.1};
GN ORFNames=BJI46_05225 {ECO:0000313|EMBL:OEY93142.1}, F4V57_08335
GN {ECO:0000313|EMBL:KAA8733343.1};
OS Acinetobacter qingfengensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1262585 {ECO:0000313|EMBL:OEY93142.1, ECO:0000313|Proteomes:UP000185895};
RN [1] {ECO:0000313|EMBL:OEY93142.1, ECO:0000313|Proteomes:UP000185895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4671 {ECO:0000313|EMBL:OEY93142.1,
RC ECO:0000313|Proteomes:UP000185895};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8733343.1, ECO:0000313|Proteomes:UP000323633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 69710T {ECO:0000313|EMBL:KAA8733343.1,
RC ECO:0000313|Proteomes:UP000323633};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) 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:OEY93142.1}.
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DR EMBL; VXKN01000005; KAA8733343.1; -; Genomic_DNA.
DR EMBL; MKKK01000056; OEY93142.1; -; Genomic_DNA.
DR RefSeq; WP_070070712.1; NZ_VXKN01000005.1.
DR AlphaFoldDB; A0A1E7R1D9; -.
DR STRING; 1262585.BJI46_05225; -.
DR OrthoDB; 9801055at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000185895; Unassembled WGS sequence.
DR Proteomes; UP000323633; 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:UP000185895}.
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT ACT_SITE 201
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 24..25
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 56..57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 88..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT BINDING 202..203
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ SEQUENCE 286 AA; 31223 MW; 5E75229FF8F2AE07 CRC64;
MTAFSQHNLA MPTPDINAPI GIFDSGIGGL SVALEVLKYL PNERILFYAD TANVPYGSRG
DAEIQQLTAQ AIEWLYQQGC KIAIVACNTA SAFSLDYLRE HYGEKFPIIG LVPAVKPAVI
QSITKVIAVL ATPATFRGKL IRDVIDHFAV PAGIKVLPVT CLDLVPLIEQ GKAMSAECLL
ILQQLLQPVM DAGADYLVLG CTHYPFLRPA IEQLYQDRLI MVDSGLAVAR QSGRILAKQN
LLTSTMMLGP RLICVFSGNN SQAMRPILQK MIGVRNDWKL IDLSNS
//
