MURI_OCEIH
ID MURI_OCEIH Reviewed; 274 AA.
AC Q8EPJ4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=OB2108;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC biosynthesis. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00258};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; BA000028; BAC14064.1; -; Genomic_DNA.
DR RefSeq; WP_011066503.1; NC_004193.1.
DR AlphaFoldDB; Q8EPJ4; -.
DR SMR; Q8EPJ4; -.
DR STRING; 221109.22777793; -.
DR EnsemblBacteria; BAC14064; BAC14064; BAC14064.
DR KEGG; oih:OB2108; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; MPWGPRT; -.
DR OrthoDB; 1718671at2; -.
DR PhylomeDB; Q8EPJ4; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000822; Chromosome.
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 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 PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; SSF53681; 2.
DR TIGRFAMs; TIGR00067; glut_race; 1.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..274
FT /note="Glutamate racemase"
FT /id="PRO_0000095494"
FT ACT_SITE 72
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 9..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 274 AA; 30159 MW; 82F4290E0E834074 CRC64;
MDKSIGVIDS GVGGLTVVHE LMRQLPKEQL IYLGDTARCP YGPRSKEEVR QFTWEMVDFL
LTKNIKMLVV ACNTATAFTL KDLKEQLDIP VIGVIQPGAR AAIKSTTNNQ VGVIGTEGTI
SSGAYSQALE KIKSDIQVSG LACPPFVPMV ERGVLSGPEA KAVVSEALRP FSNNKEMDTL
ILGCTHYPLL KSTIQEVMGE EVTVISSSEE TARETSTLLD VHQIMNRSDL VPLHQFYTTG
DLEIFIEIAK TIFQESHFQM LTIKQANIST NKVW