ID A0A0F2N4U0_9FIRM Unreviewed; 138 AA.
AC A0A0F2N4U0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Glutamate mutase sigma subunit {ECO:0000256|HAMAP-Rule:MF_00526};
DE EC=5.4.99.1 {ECO:0000256|HAMAP-Rule:MF_00526};
DE AltName: Full=Glutamate mutase S chain {ECO:0000256|HAMAP-Rule:MF_00526};
DE AltName: Full=Glutamate mutase small subunit {ECO:0000256|HAMAP-Rule:MF_00526};
DE AltName: Full=Methylaspartate mutase {ECO:0000256|HAMAP-Rule:MF_00526};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00526};
GN ORFNames=VR68_15515 {ECO:0000313|EMBL:KJR96154.1};
OS Peptococcaceae bacterium BRH_c4a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJR96154.1, ECO:0000313|Proteomes:UP000033439};
RN [1] {ECO:0000313|EMBL:KJR96154.1, ECO:0000313|Proteomes:UP000033439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4a {ECO:0000313|EMBL:KJR96154.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to
CC L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00526};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00526}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_00526}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00526}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR96154.1}.
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DR EMBL; LADN01000093; KJR96154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2N4U0; -.
DR STRING; 1629716.VR68_15515; -.
DR PATRIC; fig|1629716.3.peg.1979; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000033439; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Cobalamin {ECO:0000256|HAMAP-Rule:MF_00526};
KW Cobalt {ECO:0000256|HAMAP-Rule:MF_00526};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00526, ECO:0000313|EMBL:KJR96154.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00526}.
FT DOMAIN 1..135
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT BINDING 14
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:0000256|HAMAP-Rule:MF_00526"
FT BINDING 59..61
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00526"
FT BINDING 91..95
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00526"
SQ SEQUENCE 138 AA; 14890 MW; BAD1B0837A6D4EA8 CRC64;
MPTVVTGVIG ADAHIIGNRI IQKVLEKEGF KVVGLGALTP ADDFIKAAIE TSAAAILVSS
LYGHAELDCD GFRNKCEEAG LQNILLYIGG NLAIGKHDFE EVRKNFKAMG FNRIYPPTVD
LGDFVRDLKK DLGLETGE
//
