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GLME_FUSNN
ID   GLME_FUSNN              Reviewed;         485 AA.
AC   Q8RHY5;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Glutamate mutase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01923};
DE            EC=5.4.99.1 {ECO:0000255|HAMAP-Rule:MF_01923};
DE   AltName: Full=Glutamate mutase E chain {ECO:0000255|HAMAP-Rule:MF_01923};
DE   AltName: Full=Glutamate mutase large subunit {ECO:0000255|HAMAP-Rule:MF_01923};
DE   AltName: Full=Methylaspartate mutase {ECO:0000255|HAMAP-Rule:MF_01923};
GN   Name=glmE {ECO:0000255|HAMAP-Rule:MF_01923}; OrderedLocusNames=FN1855;
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_01923}.
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_01923};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01923};
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_01923}.
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_01923}.
CC   -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01923}.
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DR   EMBL; AE009951; AAL93954.1; -; Genomic_DNA.
DR   RefSeq; NP_602655.1; NC_003454.1.
DR   AlphaFoldDB; Q8RHY5; -.
DR   SMR; Q8RHY5; -.
DR   STRING; 190304.FN1855; -.
DR   EnsemblBacteria; AAL93954; AAL93954; FN1855.
DR   KEGG; fnu:FN1855; -.
DR   PATRIC; fig|190304.8.peg.331; -.
DR   eggNOG; COG4865; Bacteria.
DR   HOGENOM; CLU_029922_0_0_0; -.
DR   InParanoid; Q8RHY5; -.
DR   OMA; VIVKTPH; -.
DR   BioCyc; FNUC190304:G1FZS-352-MON; -.
DR   UniPathway; UPA00561; UER00617.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0031419; F:cobalamin 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; cd00245; Glm_e; 1.
DR   Gene3D; 3.90.970.10; -; 1.
DR   HAMAP; MF_01923; Me_Asp_mutase_E; 1.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006396; Glu_mut_E.
DR   InterPro; IPR014714; Glu_mut_E_C_dom_sf.
DR   Pfam; PF06368; Met_asp_mut_E; 1.
DR   PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
DR   TIGRFAMs; TIGR01503; MthylAspMut_E; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Isomerase; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Glutamate mutase epsilon subunit"
FT                   /id="PRO_0000429444"
FT   BINDING         100
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         123
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         149..150
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         171
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         180
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         297
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         326
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         330
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
SQ   SEQUENCE   485 AA;  55431 MW;  A6468786AB850104 CRC64;
     MPITFKKIDK EDFLEIRKNF LENYKNLDDF DLNTAIRFHK SLPDHKNFQK KIEQSVQDNK
     IMTQAHSKET LLEDLIKNLN TFYRVGQADF LSIIIDSHTR ENHYDNAKVI LEDSIKSNKS
     LLNGFPLINY GTKLARKIIN DVEVPLQIKH GSPDARLLVE VALLSGFSAF DGGGISHNIP
     FSKSISLKDS LENWKYVDRL VGIYEENGIK INREIFSPLT ATLVPPAISN SIQILETLLA
     VEQGVKNISI GVAQYGNITQ DIASLLALKE HIQFYLDTFS FKDINISTVF NQWIGGFPEE
     ELKAYSLISY STTIALFSKT NRIFVKNIDE YAKNSLGNTM INSLLLTKTI LDIGNNQKIN
     NYEEIIFEKE QIKKETAQII AKIFSRCDGD LRKAIIEAFE YGVLDVPFAP SKYNLGKMMP
     ARDSEGMIRY LDIGNLPFCP LIEEFHNKKI KERSMKENRE INFQMTIDDI FAMSQGKLIN
     KKSRE
 
 
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