GMSS_CLOTT
ID GMSS_CLOTT Reviewed; 137 AA.
AC Q05488;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=mutS;
OS Clostridium tetanomorphum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1553;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-33.
RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
RX PubMed=1397267; DOI=10.1016/0014-5793(92)81321-c;
RA Marsh E.N.G., Holloway D.E.;
RT "Cloning and sequencing of glutamate mutase component S from Clostridium
RT tetanomorphum. Homologies with other cobalamin-dependent enzymes.";
RL FEBS Lett. 310:167-170(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-24.
RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
RX PubMed=8454064; DOI=10.1016/0014-5793(93)80042-s;
RA Brecht M., Kellermann J., Plueckthun A.;
RT "Cloning and sequencing of glutamate mutase component E from Clostridium
RT tetanomorphum.";
RL FEBS Lett. 319:84-89(1993).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=8051138; DOI=10.1016/s0021-9258(17)32009-4;
RA Holloway D.E., Marsh E.N.;
RT "Adenosylcobalamin-dependent glutamate mutase from Clostridium
RT tetanomorphum. Overexpression in Escherichia coli, purification, and
RT characterization of the recombinant enzyme.";
RL J. Biol. Chem. 269:20425-20430(1994).
RN [4]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
RX PubMed=9739092; DOI=10.1016/s0969-2126(98)00103-8;
RA Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B.;
RT "How a protein prepares for B12 binding: structure and dynamics of the B12-
RT binding subunit of glutamate mutase from Clostridium tetanomorphum.";
RL Structure 6:1021-1033(1998).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=11828501;
RX DOI=10.1002/1439-7633(20010903)2:9<643::aid-cbic643>3.0.co;2-j;
RA Hoffmann B., Tollinger M., Konrat R., Huhta M., Marsh E.N., Krautler B.;
RT "A protein pre-organized to trap the nucleotide moiety of coenzyme B(12):
RT refined solution structure of the B(12)-binding subunit of glutamate mutase
RT from Clostridium tetanomorphum.";
RL ChemBioChem 2:643-655(2001).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=11397096; DOI=10.1006/jmbi.2001.4696;
RA Tollinger M., Eichmuller C., Konrat R., Huhta M.S., Marsh E.N.,
RA Krautler B.;
RT "The B(12)-binding subunit of glutamate mutase from Clostridium
RT tetanomorphum traps the nucleotide moiety of coenzyme B(12).";
RL J. Mol. Biol. 309:777-791(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:8051138}.
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:8051138};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00526,
CC ECO:0000269|PubMed:8051138};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for adenosylcobalamin {ECO:0000269|PubMed:8051138};
CC KM=1.09 mM for L-glutamate {ECO:0000269|PubMed:8051138};
CC Vmax=22.8 umol/min/mg enzyme {ECO:0000269|PubMed:8051138};
CC Note=kcat is 20.6 sec(-1) for mutase activity with L-glutamate.;
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:8051138}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00526}.
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DR EMBL; X70499; CAA49908.1; -; Genomic_DNA.
DR EMBL; X68570; CAA48567.1; -; Genomic_DNA.
DR PIR; S29502; S29502.
DR PDB; 1BE1; NMR; -; A=1-137.
DR PDB; 1FMF; NMR; -; A=1-137.
DR PDB; 1ID8; NMR; -; A=1-137.
DR PDBsum; 1BE1; -.
DR PDBsum; 1FMF; -.
DR PDBsum; 1ID8; -.
DR AlphaFoldDB; Q05488; -.
DR BMRB; Q05488; -.
DR SMR; Q05488; -.
DR DrugBank; DB02576; F-Loop of Vitamin B12.
DR BRENDA; 5.4.99.1; 1527.
DR SABIO-RK; Q05488; -.
DR UniPathway; UPA00561; UER00617.
DR EvolutionaryTrace; Q05488; -.
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_0000216445"
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 /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 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"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1BE1"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1ID8"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1FMF"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1BE1"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1BE1"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1BE1"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1BE1"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1BE1"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1BE1"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1BE1"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1BE1"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1BE1"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:1BE1"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1BE1"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:1BE1"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1BE1"
SQ SEQUENCE 137 AA; 14748 MW; E71FE55BA8CE3DB3 CRC64;
MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA IETKADLICV
SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN WPDVEQRFKA MGFDRVYPPG
TSPETTIADM KEVLGVE
