GLME_SHIDS
ID GLME_SHIDS Reviewed; 454 AA.
AC Q32IJ5;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glutamate mutase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01923};
DE EC=5.4.99.1 {ECO:0000255|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase E chain {ECO:0000255|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase large subunit {ECO:0000255|HAMAP-Rule:MF_01923};
DE AltName: Full=Methylaspartate mutase {ECO:0000255|HAMAP-Rule:MF_01923};
GN Name=glmE {ECO:0000255|HAMAP-Rule:MF_01923}; OrderedLocusNames=SDY_0674;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to
CC L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
CC {ECO:0000255|HAMAP-Rule:MF_01923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-3-methyl-L-aspartate = L-glutamate;
CC Xref=Rhea:RHEA:12857, ChEBI:CHEBI:29985, ChEBI:CHEBI:58724;
CC EC=5.4.99.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01923};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01923};
CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC pathway; acetate and pyruvate from L-glutamate: step 1/4.
CC {ECO:0000255|HAMAP-Rule:MF_01923}.
CC -!- SUBUNIT: Heterotetramer composed of 2 epsilon subunits (GlmE) and 2
CC sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a
CC monomer. {ECO:0000255|HAMAP-Rule:MF_01923}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01923}.
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DR EMBL; CP000034; ABB60862.1; -; Genomic_DNA.
DR RefSeq; WP_000423331.1; NC_007606.1.
DR RefSeq; YP_402351.1; NC_007606.1.
DR AlphaFoldDB; Q32IJ5; -.
DR SMR; Q32IJ5; -.
DR STRING; 300267.SDY_0674; -.
DR EnsemblBacteria; ABB60862; ABB60862; SDY_0674.
DR KEGG; sdy:SDY_0674; -.
DR PATRIC; fig|300267.13.peg.787; -.
DR HOGENOM; CLU_029922_0_0_6; -.
DR OMA; VIVKTPH; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050097; F:methylaspartate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019670; P:anaerobic glutamate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniPathway.
DR CDD; cd00245; Glm_e; 1.
DR HAMAP; MF_01923; Me_Asp_mutase_E; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006396; Glu_mut_E.
DR Pfam; PF06368; Met_asp_mut_E; 2.
DR PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR TIGRFAMs; TIGR01503; MthylAspMut_E; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Reference proteome.
FT CHAIN 1..454
FT /note="Glutamate mutase epsilon subunit"
FT /id="PRO_0000429445"
FT BINDING 67
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 69
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 99
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 122
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 148..149
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 170
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 176
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 179
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 180
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 296
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 325
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 329
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 333
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
SQ SEQUENCE 454 AA; 50305 MW; 418B335ED7202919 CRC64;
MELRNKKLTH DEFMTERQQV LKTWETGKNV ENFEDGVKYQ QAIPEHKRFS LALLKADKEG
KTLSQPRAGV ALMDEHIELL KTLQEECDLL PSTIDAYTRL NRYEEAAVGI KKSIEAGTSK
LNGLPVVNHG VAACRRLTET LQKPLQIRHG TPDARLLAKI SMASGFTSYE GGGISYNIPY
AKRVTLEKSI RDWQYCDRLM GMYEEHGIRI NREPFGPLTG TLIPPFISHS IAIIEGLLAL
EQSVKSITVG YGQVGSLTQD VAAIQSLREL AHEYFQSYGY TDYELSTVFH QWMGGFPEDE
SKAFAIISWG AAVAGMSGAT KVITKSPHEA WGIPTAAANI QGLKASRQML NMVNEQKFPP
CPAVELEIEL IKSEVRAVLN KVFELGNGDI ARGTVLAFEA GVLEAGAVPL PKDILDLHHD
YVAERARCEG RQPTFQMVVD DINAVSHSKL IGRP
