ID J7U8U7_MORMO Unreviewed; 481 AA.
AC J7U8U7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=MU9_1022 {ECO:0000313|EMBL:AGG30068.1};
OS Morganella morganii subsp. morganii KT.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Morganella.
OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG30068.1, ECO:0000313|Proteomes:UP000011834};
RN [1] {ECO:0000313|EMBL:AGG30068.1, ECO:0000313|Proteomes:UP000011834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT {ECO:0000313|EMBL:AGG30068.1,
RC ECO:0000313|Proteomes:UP000011834};
RX PubMed=23282187;
RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT "Whole-genome sequencing and identification of Morganella morganii KT
RT pathogenicity-related genes.";
RL BMC Genomics 13:S4-S4(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004345; AGG30068.1; -; Genomic_DNA.
DR RefSeq; WP_004236125.1; NC_020418.1.
DR AlphaFoldDB; J7U8U7; -.
DR GeneID; 69680028; -.
DR KEGG; mmk:MU9_1022; -.
DR eggNOG; COG4865; Bacteria.
DR HOGENOM; CLU_029922_0_0_6; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000011834; 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 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:UP000011834}.
FT BINDING 67
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 69
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 99
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 122
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 148..149
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 170
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 176
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 179
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 180
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 296
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 325
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 329
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 333
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
SQ SEQUENCE 481 AA; 53084 MW; 582653A94DE0A0CE CRC64;
MELKNKKIAI DDFMAERKDV LKTWVTGKDV ENFEDGVKYQ ATISEDKNFA KKLFEADRDG
ITLSQPRAGV ALIEEHIELL KKLQKECDLL PTTIDAYTRL NRYEEAAVGI QKSVEAGTSK
LNGLPVVNHG VAACRHITES LDKPLQIRHG TPDARLLCEI SMASGFTSYE GGGISYNIPY
AKRVTLEKSI RDWQYCDRVI GLYEENGIRI NREPFGPLTG TLIPPFISHT VAIIEGLVAL
EQGVKSITVG YGQVGNLVQD IAAIRSLREL SHEYFRAYGY EDYELSTVFH QWMGGFPEDE
SRAAAVISWG AAVAGMSGAT KVITKSPHEA FGIPTAEANC QGLRASNQML NMVRDQKFPP
CKDVDLEVEL IKREVRAVMK KVLELGNGDI AVGTVRAFEA GVLDIPFAPA MCNSGKMMPI
RDNNGAIRVF DAGAVPLPDD VLSMHHDFVA ERAREEGREA SFQMIIDDIN AVSHSKLVGR
P
//
