ID H1PN73_9FIRM Unreviewed; 483 AA.
AC H1PN73;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Glutamate mutase epsilon subunit {ECO:0000256|HAMAP-Rule:MF_01923};
DE EC=5.4.99.1 {ECO:0000256|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase E chain {ECO:0000256|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase large subunit {ECO:0000256|HAMAP-Rule:MF_01923};
DE AltName: Full=Methylaspartate mutase {ECO:0000256|HAMAP-Rule:MF_01923};
GN Name=glmE {ECO:0000256|HAMAP-Rule:MF_01923};
GN ORFNames=HMPREF0380_01631 {ECO:0000313|EMBL:EHO82390.1};
OS Eubacterium infirmum F0142.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=883109 {ECO:0000313|EMBL:EHO82390.1, ECO:0000313|Proteomes:UP000004504};
RN [1] {ECO:0000313|EMBL:EHO82390.1, ECO:0000313|Proteomes:UP000004504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0142 {ECO:0000313|EMBL:EHO82390.1,
RC ECO:0000313|Proteomes:UP000004504};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Eubacterium infirmum F0142.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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_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:0000256|HAMAP-Rule:MF_01923};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01923}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01923}.
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DR EMBL; AGWI01000028; EHO82390.1; -; Genomic_DNA.
DR AlphaFoldDB; H1PN73; -.
DR STRING; 883109.HMPREF0380_01631; -.
DR PATRIC; fig|883109.3.peg.1620; -.
DR eggNOG; COG4865; Bacteria.
DR HOGENOM; CLU_029922_0_0_9; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000004504; Unassembled WGS sequence.
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 Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 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 NCBIfam; TIGR01503; MthylAspMut_E; 1.
DR Pfam; PF06368; Met_asp_mut_E; 1.
DR PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|HAMAP-Rule:MF_01923};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_01923};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01923};
KW Reference proteome {ECO:0000313|Proteomes:UP000004504}.
FT BINDING 66
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 68
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 100
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 123
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 149..150
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 171
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 177
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 180
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 181
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 297
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 326
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 330
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 334
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
SQ SEQUENCE 483 AA; 53450 MW; 90D0D02DEDD52CC0 CRC64;
MDLKNKKIPE AEFLALRNEV LAQWPTGKDV DLEEAVNYHK AMPREKVFSE KLISAKEIRN
TLVQPRAGVP VIEDHIKLLN YLEDVGEADL LPTTVDSYTR LNRYEEAENG IEESIRLGRA
MMNGFPPVNH GVSGCRRVIE SVHTPVQVRH GTPDARLLTE ISYAGGFTSY EGGGISYNLP
YCKDVPMNRT IRDWQYVDRL TGLYEEMGVS INREPYGPLT GTLVPPCISH SVAIIEALLA
AEQGVKNITV GYGQCGNIIQ DIAAIRTLEE LTEEYLHKYG YNDVIVTTVL HQWMGGFPAD
ESKAFGVISS GSLIAGLSKA TKVIVKSPHE AIGIPTMEAN GQGLRCTKQV VNMLKDQDFP
EAALKDEKEI IKAETRCIVD KCFELGDGDI AVGTCRATEA GVIDIPFAPC RYNAGLMLPC
RDNNGAVRIL NTGNLPFSQE LKDFHRDKIE ERAKVEARDA SFQMVIDDVY AIGKGRLVGR
PKR
//
