GMSS_FUSNN
ID GMSS_FUSNN Reviewed; 136 AA.
AC Q8RHY7;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=FN1853;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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}.
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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|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: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}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00526}.
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DR EMBL; AE009951; AAL93952.1; -; Genomic_DNA.
DR RefSeq; NP_602653.1; NC_003454.1.
DR AlphaFoldDB; Q8RHY7; -.
DR SMR; Q8RHY7; -.
DR STRING; 190304.FN1853; -.
DR EnsemblBacteria; AAL93952; AAL93952; FN1853.
DR KEGG; fnu:FN1853; -.
DR PATRIC; fig|190304.8.peg.329; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_136705_0_0_0; -.
DR InParanoid; Q8RHY7; -.
DR OMA; GHGEMDC; -.
DR BioCyc; FNUC190304:G1FZS-350-MON; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000002521; 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: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; IPR006159; Acid_CoA_mut_C.
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; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR01501; MthylAspMutase; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..136
FT /note="Glutamate mutase sigma subunit"
FT /id="PRO_0000216447"
FT DOMAIN 3..136
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 /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 61..63
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
SQ SEQUENCE 136 AA; 15144 MW; 934DB52D9D4B382C CRC64;
MAKKKIVIGV IGSDCHTVGN KIIHNKLEES GFDVVNIGAL SPQIDFINAA LETNSDAIIV
SSIYGYGELD CQGIREKCNE YGLKDILLYI GGNIGSSNEK WENTEKRFKE MGFDRIYKPG
TPIEETIIDL KKDFKI
