ID A5CZJ7_PELTS Unreviewed; 141 AA.
AC A5CZJ7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=Sbm {ECO:0000313|EMBL:BAF60600.1};
GN Synonyms=glmS {ECO:0000256|HAMAP-Rule:MF_00526};
GN OrderedLocusNames=PTH_2419 {ECO:0000313|EMBL:BAF60600.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF60600.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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}.
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DR EMBL; AP009389; BAF60600.1; -; Genomic_DNA.
DR AlphaFoldDB; A5CZJ7; -.
DR STRING; 370438.PTH_2419; -.
DR KEGG; pth:PTH_2419; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_136705_0_0_9; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000006556; 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:0008168; F:methyltransferase activity; IEA:UniProt.
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 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 PANTHER; PTHR45833; METHIONINE SYNTHASE; 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};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00526};
KW Reference proteome {ECO:0000313|Proteomes:UP000006556}.
FT DOMAIN 4..138
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT BINDING 17
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 62..64
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00526"
SQ SEQUENCE 141 AA; 15514 MW; 63DC60153A402C77 CRC64;
MKDKITVITG TVGVDAHVIG TKIVSRILGE QGFNVVALGA QTPPEEFIKV AQETDADAIF
MSSLYGMAEL DLQGFKEKCI EAGLNDVLLY IGGILGVMKH DWKEDEEKFK RLGFDRVYPP
EADVMAAIED LKQDLRAKGK L
//
