GMSS_DESHY
ID GMSS_DESHY Reviewed; 136 AA.
AC Q24SG7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glutamate mutase sigma subunit {ECO:0000255|HAMAP-Rule:MF_00526};
DE EC=5.4.99.1 {ECO:0000255|HAMAP-Rule:MF_00526};
DE AltName: Full=Glutamate mutase S chain {ECO:0000255|HAMAP-Rule:MF_00526};
DE AltName: Full=Glutamate mutase small subunit {ECO:0000255|HAMAP-Rule:MF_00526};
DE AltName: Full=Methylaspartate mutase {ECO:0000255|HAMAP-Rule:MF_00526};
GN Name=glmS {ECO:0000255|HAMAP-Rule:MF_00526}; Synonyms=mamA;
GN OrderedLocusNames=DSY3236;
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_00526}.
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_00526};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00526};
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_00526}.
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_00526}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00526}.
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DR EMBL; AP008230; BAE85025.1; -; Genomic_DNA.
DR RefSeq; WP_005816944.1; NC_007907.1.
DR AlphaFoldDB; Q24SG7; -.
DR SMR; Q24SG7; -.
DR STRING; 138119.DSY3236; -.
DR EnsemblBacteria; BAE85025; BAE85025; DSY3236.
DR KEGG; dsy:DSY3236; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_136705_0_0_9; -.
DR OMA; GHGEMDC; -.
DR OrthoDB; 1335734at2; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000001946; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; cd02072; Glm_B12_BD; 1.
DR HAMAP; MF_00526; Me_Asp_mutase_S; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006394; GlmS.
DR Pfam; PF02310; B12-binding; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR01501; MthylAspMutase; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..136
FT /note="Glutamate mutase sigma subunit"
FT /id="PRO_0000264142"
FT DOMAIN 3..136
FT /note="B12-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 13..17
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 16
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 61..63
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 93..97
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
SQ SEQUENCE 136 AA; 14748 MW; 051735403943D06C CRC64;
MEGKTLVLGV IGADVHAVGN RILDYAFTQA GFKVINIGVL ASQEEFIRAA IETAASVIMV
SSLYGHGELD CRGLREKCQE SGIGDILLYV GGNLVVGKQE FSEVEKRFLA MGFNRVYPPG
TMPEAAIEDL RKDLEL
