GMSS_CLOCO
ID GMSS_CLOCO Reviewed; 137 AA.
AC P80078; Q60144;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 112.
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};
OS Clostridium cochlearium.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1494;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=7880251; DOI=10.1111/j.1432-1033.1994.tb20083.x;
RA Zelder O., Beatrix B., Leutbecher U., Buckel W.;
RT "Characterization of the coenzyme-B12-dependent glutamate mutase from
RT Clostridium cochlearium produced in Escherichia coli.";
RL Eur. J. Biochem. 226:577-585(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=8013871; DOI=10.1111/j.1574-6968.1994.tb06797.x;
RA Zelder O., Beatrix B., Buckel W.;
RT "Cloning, sequencing and expression in Escherichia coli of the gene
RT encoding component S of the coenzyme B12-dependent glutamate mutase from
RT Clostridium cochlearium.";
RL FEMS Microbiol. Lett. 118:15-21(1994).
RN [3]
RP PROTEIN SEQUENCE OF 1-23, FUNCTION, ACTIVITY REGULATION, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=1315276; DOI=10.1111/j.1432-1033.1992.tb16840.x;
RA Leutbecher U., Boecher R., Linder D., Buckel W.;
RT "Glutamate mutase from Clostridium cochlearium. Purification, cobamide
RT content and stereospecific inhibitors.";
RL Eur. J. Biochem. 205:759-765(1992).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=10429202; DOI=10.1046/j.1432-1327.1999.00482.x;
RA Hoffmann B., Konrat R., Bothe H., Buckel W., Krautler B.;
RT "Structure and dynamics of the B12-binding subunit of glutamate mutase from
RT Clostridium cochlearium.";
RL Eur. J. Biochem. 263:178-188(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=10467146; DOI=10.1016/s0969-2126(99)80116-6;
RA Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W.,
RA Kratky C.;
RT "Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme
RT B12-dependent enzyme provides new mechanistic insights.";
RL Structure 7:891-902(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS
RP AND SUBSTRATE, COFACTOR, AND SUBUNIT.
RX PubMed=11592143;
RX DOI=10.1002/1521-3773(20010917)40:18<3377::aid-anie3377>3.0.co;2-8;
RA Gruber K., Reitzer R., Kratky C.;
RT "Radical shuttling in a protein: ribose pseudorotation controls alkyl-
RT radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase.";
RL Angew. Chem. Int. Ed. Engl. 40:3377-3380(2001).
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, ECO:0000269|PubMed:1315276,
CC ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871}.
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 ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00526,
CC ECO:0000269|PubMed:10467146, ECO:0000269|PubMed:11592143,
CC ECO:0000269|PubMed:1315276, ECO:0000269|PubMed:7880251,
CC ECO:0000269|PubMed:8013871};
CC -!- ACTIVITY REGULATION: Competitively inhibited by (2S,4S)-4-
CC fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and
CC (S)-3-methylitaconate. {ECO:0000269|PubMed:1315276,
CC ECO:0000269|PubMed:7880251}.
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, ECO:0000269|PubMed:10467146,
CC ECO:0000269|PubMed:11592143, ECO:0000269|PubMed:1315276,
CC ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871}.
CC -!- INTERACTION:
CC P80078; P80077: glmE; NbExp=2; IntAct=EBI-1028147, EBI-1028142;
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00526}.
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DR EMBL; X80997; CAA56921.1; -; Genomic_DNA.
DR EMBL; X75890; CAA53484.1; -; Genomic_DNA.
DR PIR; I40658; I40658.
DR PDB; 1B1A; NMR; -; A=1-137.
DR PDB; 1CB7; X-ray; 2.00 A; A/C=1-137.
DR PDB; 1CCW; X-ray; 1.60 A; A/C=1-137.
DR PDB; 1I9C; X-ray; 1.90 A; A/C=1-137.
DR PDB; 6H9E; X-ray; 1.82 A; A/C=1-137.
DR PDB; 6H9F; X-ray; 2.10 A; A/C=1-137.
DR PDBsum; 1B1A; -.
DR PDBsum; 1CB7; -.
DR PDBsum; 1CCW; -.
DR PDBsum; 1I9C; -.
DR PDBsum; 6H9E; -.
DR PDBsum; 6H9F; -.
DR AlphaFoldDB; P80078; -.
DR SMR; P80078; -.
DR IntAct; P80078; 1.
DR STRING; 1494.SAMN05216497_1183; -.
DR PRIDE; P80078; -.
DR BRENDA; 5.4.99.1; 1471.
DR SABIO-RK; P80078; -.
DR UniPathway; UPA00561; UER00617.
DR EvolutionaryTrace; P80078; -.
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; 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; TIGR01501; MthylAspMutase; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Isomerase;
KW Metal-binding.
FT CHAIN 1..137
FT /note="Glutamate mutase sigma subunit"
FT /id="PRO_0000216443"
FT DOMAIN 3..137
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 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 BINDING 61..63
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 93..97
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:1CCW"
SQ SEQUENCE 137 AA; 14812 MW; D9C5BF8DE5D1E878 CRC64;
MEKKTIVLGV IGSDCHAVGN KILDHAFTNA GFNVVNIGVL SPQEVFIKAA IETKADAILL
SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH WPDVEKRFKD MGYDRVYAPG
TPPEVGIADL KKDLNIE
