ID   GLME_TREDE              Reviewed;         485 AA.
AC   Q73KI2;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=TDE_2236;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12755.1; -; Genomic_DNA.
DR   RefSeq; NP_972836.1; NC_002967.9.
DR   RefSeq; WP_002680091.1; NC_002967.9.
DR   AlphaFoldDB; Q73KI2; -.
DR   SMR; Q73KI2; -.
DR   STRING; 243275.TDE_2236; -.
DR   EnsemblBacteria; AAS12755; AAS12755; TDE_2236.
DR   GeneID; 2741341; -.
DR   KEGG; tde:TDE_2236; -.
DR   PATRIC; fig|243275.7.peg.2112; -.
DR   eggNOG; COG4865; Bacteria.
DR   HOGENOM; CLU_029922_0_0_12; -.
DR   OMA; VIVKTPH; -.
DR   OrthoDB; 809497at2; -.
DR   UniPathway; UPA00561; UER00617.
DR   Proteomes; UP000008212; 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_0000429446"
FT   BINDING         66
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT   BINDING         68
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
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         177
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         181
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
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"
FT   BINDING         334
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
SQ   SEQUENCE   485 AA;  53131 MW;  9B0EADF05A33BFF7 CRC64;
     MRWKNKKIPE GEFMEMREEI LQTWPTGKDV DLKESIDYLK KIPPEKNFAI KLEQADKEGI
     TTAQPRAGVP LLDEHINLLQ FLQDEGGADF LPSTIDAYTR QNRYEEGEAG IEASKKAGRS
     LMNGFPAVNW GVGPCRQVLE AVNLPLQARH GTPDARLLSE IIHAGGYTSN EGGGISYNVP
     YAKAVSIEHS IMCWQYADRL VGFYEENGVH LNREPFGPLT GTLVPPSVAI AVGVIEALLA
     AEQGVKSITV GYGMCGNMTQ DVAAVISLRE ITKDYMKKFG YKDMCITTVF HQWMGGFPAD
     ESRAYGLISL GSTTAALSGA TKVIVKTPHE AFGIPTKEAN AGGIKATKMV LNLLKGQRYP
     DSRVLAQEIE LIKAETKCIM DKVYEIGGGD LVEGTIKAFE AGVIDIPFAP SQYNAGKVMP
     ARDNDGCIRY LMPGNLPFTK DILDFNRGKL EERAKADKRE VDFQMSVDDV YAVSSGVLVG
     RPAKR