GLME_CLOTT
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 03-AUG-2022, entry version 93.
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; Firmicutes; 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}.
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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 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 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
