GLME_CLOCO
ID GLME_CLOCO Reviewed; 483 AA.
AC P80077;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 113.
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};
OS Clostridium cochlearium.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1494;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=7880251; DOI=10.1111/j.1432-1033.1994.tb20083.x;
RA Zelder O., Beatrix B., Leutbecher U., Buckel W.;
RT "Characterization of the coenzyme-B12-dependent glutamate mutase from
RT Clostridium cochlearium produced in Escherichia coli.";
RL Eur. J. Biochem. 226:577-585(1994).
RN [2]
RP PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=1315276; DOI=10.1111/j.1432-1033.1992.tb16840.x;
RA Leutbecher U., Boecher R., Linder D., Buckel W.;
RT "Glutamate mutase from Clostridium cochlearium. Purification, cobamide
RT content and stereospecific inhibitors.";
RL Eur. J. Biochem. 205:759-765(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 17787 / DSM 1285 / NCIB 10633;
RX PubMed=10467146; DOI=10.1016/s0969-2126(99)80116-6;
RA Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W.,
RA Kratky C.;
RT "Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme
RT B12-dependent enzyme provides new mechanistic insights.";
RL Structure 7:891-902(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS
RP AND SUBSTRATE, COFACTOR, AND SUBUNIT.
RX PubMed=11592143;
RX DOI=10.1002/1521-3773(20010917)40:18<3377::aid-anie3377>3.0.co;2-8;
RA Gruber K., Reitzer R., Kratky C.;
RT "Radical shuttling in a protein: ribose pseudorotation controls alkyl-
RT radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase.";
RL Angew. Chem. Int. Ed. Engl. 40:3377-3380(2001).
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:1315276,
CC ECO:0000269|PubMed:7880251}.
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:1315276, ECO:0000269|PubMed:7880251};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01923,
CC ECO:0000269|PubMed:10467146, ECO:0000269|PubMed:11592143,
CC ECO:0000269|PubMed:1315276, ECO:0000269|PubMed:7880251};
CC -!- ACTIVITY REGULATION: Competitively inhibited by (2S,4S)-4-
CC fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and
CC (S)-3-methylitaconate. {ECO:0000269|PubMed:1315276,
CC ECO:0000269|PubMed:7880251}.
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, ECO:0000269|PubMed:10467146,
CC ECO:0000269|PubMed:11592143, ECO:0000269|PubMed:1315276,
CC ECO:0000269|PubMed:7880251}.
CC -!- INTERACTION:
CC P80077; P80078: glmS; NbExp=2; IntAct=EBI-1028142, EBI-1028147;
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01923}.
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DR EMBL; X80997; CAA56923.1; -; Genomic_DNA.
DR PIR; I40662; I40662.
DR PDB; 1CB7; X-ray; 2.00 A; B/D=1-483.
DR PDB; 1CCW; X-ray; 1.60 A; B/D=1-483.
DR PDB; 1I9C; X-ray; 1.90 A; B/D=1-483.
DR PDB; 6H9E; X-ray; 1.82 A; B/D=1-483.
DR PDB; 6H9F; X-ray; 2.10 A; B/D=1-483.
DR PDBsum; 1CB7; -.
DR PDBsum; 1CCW; -.
DR PDBsum; 1I9C; -.
DR PDBsum; 6H9E; -.
DR PDBsum; 6H9F; -.
DR AlphaFoldDB; P80077; -.
DR SMR; P80077; -.
DR IntAct; P80077; 1.
DR STRING; 1494.SAMN05216497_1185; -.
DR BioCyc; MetaCyc:MON-1101; -.
DR SABIO-RK; P80077; -.
DR UniPathway; UPA00561; UER00617.
DR EvolutionaryTrace; P80077; -.
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 3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Isomerase.
FT CHAIN 1..483
FT /note="Glutamate mutase epsilon subunit"
FT /id="PRO_0000087511"
FT BINDING 66
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 68
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 100
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 123
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 149..150
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 171
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 177
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 180
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 181
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 297
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 326
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 330
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT BINDING 334
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1CCW"
FT TURN 174..181
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 187..206
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1CCW"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 258..278
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 301..318
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1CCW"
FT TURN 328..332
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 337..353
FT /evidence="ECO:0007829|PDB:1CCW"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 363..386
FT /evidence="ECO:0007829|PDB:1CCW"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 391..400
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 440..457
FT /evidence="ECO:0007829|PDB:1CCW"
FT HELIX 463..472
FT /evidence="ECO:0007829|PDB:1CCW"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:1CCW"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:1CCW"
SQ SEQUENCE 483 AA; 53574 MW; 0789965B945B3F5C CRC64;
MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE KLVLAKKKGI
TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR QNRYDECENG IKESEKAGRS
LLNGFPGVNY GVKGCRKVLE AVNLPLQARH GTPDSRLLAE IIHAGGWTSN EGGGISYNVP
YAKNVTIEKS LLDWQYCDRL VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA
AEQGVKNITV GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD
ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA LNMLEGQRMP
MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE TGVMDIPFGP SKYNAGKMMP
VRDNLGCVRY LEFGNVPFTE EIKNYNRERL QERAKFEGRD VSFQMVIDDI FAVGKGRLIG
RPE
