ID M0CG24_9EURY Unreviewed; 148 AA.
AC M0CG24;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=C476_07222 {ECO:0000313|EMBL:ELZ22201.1};
OS Natrinema limicola JCM 13563.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ22201.1, ECO:0000313|Proteomes:UP000011615};
RN [1] {ECO:0000313|EMBL:ELZ22201.1, ECO:0000313|Proteomes:UP000011615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ22201.1,
RC ECO:0000313|Proteomes:UP000011615};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 methylamine corrinoid protein family.
CC {ECO:0000256|ARBA:ARBA00010854}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC {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:ELZ22201.1}.
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DR EMBL; AOIT01000029; ELZ22201.1; -; Genomic_DNA.
DR RefSeq; WP_008011369.1; NZ_AOIT01000029.1.
DR AlphaFoldDB; M0CG24; -.
DR STRING; 1230457.C476_07222; -.
DR PATRIC; fig|1230457.4.peg.1447; -.
DR eggNOG; arCOG01710; Archaea.
DR OrthoDB; 225699at2157; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000011615; 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|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00526};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00526, ECO:0000313|EMBL:ELZ22201.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00526};
KW Reference proteome {ECO:0000313|Proteomes:UP000011615}.
FT DOMAIN 2..135
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT BINDING 12..16
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00526"
FT BINDING 15
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 60..62
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 148 AA; 16005 MW; 9640B3DC5D9B045A CRC64;
MTKTVILGVI GSDAHVVGIT ILEQALEAAG FDVVNLGVQT SQEEFVEAAS ANDAEAVLVS
SLYGHAKQDC EGFHQRIADA DLDVTTYIGG NLAVGQDDFE ETRKFFRELG FDRVFDSETD
PEDAIEALRA DLDMRSSESE QESQTVSA
//
