ID GLME_CLOTT Reviewed; 485 AA. AC Q05509; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 13-SEP-2023, entry version 97. 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}; Synonyms=mutE; OS Clostridium tetanomorphum. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1553; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1; RX PubMed=8428631; DOI=10.1016/0014-5793(93)81488-l; RA Holloway D.E., Marsh E.N.G.; RT "Cloning and sequencing of glutamate mutase component E from Clostridium RT tetanomorphum. Organization of the mut genes."; RL FEBS Lett. 317:44-48(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1; RX PubMed=8454064; DOI=10.1016/0014-5793(93)80042-s; RA Brecht M., Kellermann J., Plueckthun A.; RT "Cloning and sequencing of glutamate mutase component E from Clostridium RT tetanomorphum."; RL FEBS Lett. 319:84-89(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-485. RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1; RX PubMed=1420191; DOI=10.1021/bi00159a015; RA Goda S.K., Minton N.P., Botting N.P., Gani D.; RT "Cloning, sequencing, and expression in Escherichia coli of the Clostridium RT tetanomorphum gene encoding beta-methylaspartase and characterization of RT the recombinant protein."; RL Biochemistry 31:10747-10756(1992). RN [4] RP PROTEIN SEQUENCE OF 1-20. RC STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1; RX PubMed=1397267; DOI=10.1016/0014-5793(92)81321-c; RA Marsh E.N.G., Holloway D.E.; RT "Cloning and sequencing of glutamate mutase component S from Clostridium RT tetanomorphum. Homologies with other cobalamin-dependent enzymes."; RL FEBS Lett. 310:167-170(1992). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND RP SUBUNIT. RX PubMed=8051138; DOI=10.1016/s0021-9258(17)32009-4; RA Holloway D.E., Marsh E.N.; RT "Adenosylcobalamin-dependent glutamate mutase from Clostridium RT tetanomorphum. Overexpression in Escherichia coli, purification, and RT characterization of the recombinant enzyme."; RL J. Biol. Chem. 269:20425-20430(1994). 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, ECO:0000269|PubMed:8051138}. 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 ECO:0000269|PubMed:8051138}; CC -!- COFACTOR: CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01923, CC ECO:0000269|PubMed:8051138}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=18 uM for adenosylcobalamin {ECO:0000269|PubMed:8051138}; CC KM=1.09 mM for L-glutamate {ECO:0000269|PubMed:8051138}; CC Vmax=22.8 umol/min/mg enzyme {ECO:0000269|PubMed:8051138}; CC Note=kcat is 20.6 sec(-1) for mutase activity with L-glutamate.; 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 monomer CC (Probable). {ECO:0000305|PubMed:8051138}. CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family. CC {ECO:0000255|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; X70499; CAA49910.1; -; Genomic_DNA. DR EMBL; X70695; CAA50026.1; -; Genomic_DNA. DR EMBL; S48141; AAB24069.1; -; Genomic_DNA. DR PIR; S32433; S32433. DR AlphaFoldDB; Q05509; -. DR SMR; Q05509; -. DR BRENDA; 5.4.99.1; 1527. DR SABIO-RK; Q05509; -. DR UniPathway; UPA00561; UER00617. 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 1: Evidence at protein level; KW Cobalamin; Cobalt; Direct protein sequencing; Isomerase. FT CHAIN 1..485 FT /note="Glutamate mutase epsilon subunit" FT /id="PRO_0000087512" 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" FT CONFLICT 8 FT /note="W -> L (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="E -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 17 FT /note="R -> A (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 19 FT /note="E -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 485 AA; 53741 MW; 131792A392CACCC0 CRC64; MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD KLVRAKEAGI TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR QNRYEECEIG IKESEKAGRS LLNGFPGVNH GVKGCRKVLE SVNLPLQARH GTPDSRLLAE IIHAGGWTSN EGGGISYNIP YAKSVPIDKC LKDWQYCDRL VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA LNMLEGQRMP MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE ELKNYNRERL AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK //