GLME_DESHY
ID GLME_DESHY Reviewed; 484 AA.
AC Q24SG9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=DSY3234;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85023.1; -; Genomic_DNA.
DR RefSeq; WP_011460941.1; NC_007907.1.
DR AlphaFoldDB; Q24SG9; -.
DR SMR; Q24SG9; -.
DR STRING; 138119.DSY3234; -.
DR EnsemblBacteria; BAE85023; BAE85023; DSY3234.
DR KEGG; dsy:DSY3234; -.
DR eggNOG; COG4865; Bacteria.
DR HOGENOM; CLU_029922_0_0_9; -.
DR OMA; VIVKTPH; -.
DR OrthoDB; 809497at2; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000001946; 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 Gene3D; 3.90.970.10; -; 1.
DR HAMAP; MF_01923; Me_Asp_mutase_E; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006396; Glu_mut_E.
DR InterPro; IPR014714; Glu_mut_E_C_dom_sf.
DR Pfam; PF06368; Met_asp_mut_E; 1.
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..484
FT /note="Glutamate mutase epsilon subunit"
FT /id="PRO_0000429442"
FT BINDING 66
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 68
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 100
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 123
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 149..150
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 171
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 177
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 180
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 181
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 297
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 326
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 330
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 334
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
SQ SEQUENCE 484 AA; 53409 MW; D46D2DB6E991AD91 CRC64;
MDLTNRMMEP EEFARQRQEV LNQWATGRDV DFEEAVAYHK NLPRSKNFSY KLAEGKARGI
TFAQPRAGVA LLNEHLELLR FLEEEGEADF LPTTIDSYTR QNRYAEAQTG IDESRLVGRS
MLNGFPAVNH GVSACRRLIE HPKVPVQVRH GTPDARLLAE ITLAGGFTAY EGGGISYNIP
YAKDVSIEKS IKYWQYVDRL VGMYEEKGVS INREPFGPLT GTLVPPSVSH GVAVIEGILA
VAQGVRSLTL GYGQCGNLLQ DVAAIRTLPL LAAEYLSKLG YTDFDITTVF HQWMGGFPQD
EAKAYGVISW GAAAAALGKA TKVIVKSPHE ALGIPTKEAN AAGIRTTKQI LNMLKDQSLP
MTEELALEEK MIREETRAIL DRTLDLGEGD MAVGAVRAFQ AGVIDVPFAP SRYNGGRILP
ARDSQGAVRV LDFGNLPFSE EIKEFHRERI ARRGRDEGRE PSFQMVIDDI YAIGKGMLVG
RPRS
