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   13-SEP-2023, entry version 117.
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; Bacillota; 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   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   Gene3D; 3.40.50.280; Cobalamin-binding domain; 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   NCBIfam; TIGR01501; MthylAspMutase; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 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
//