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   16-JUN-2009, entry version 53.
DE   RecName: Full=Methylaspartate mutase E chain;
DE            EC=5.4.99.1;
DE   AltName: Full=Glutamate mutase subunit epsilon;
GN   Name=mutE;
OS   Clostridium tetanomorphum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 11547;
RX   MEDLINE=93154518; 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
RT   Clostridium 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 / H1;
RX   MEDLINE=93202282; 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
RT   Clostridium tetanomorphum.";
RL   FEBS Lett. 319:84-89(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-485.
RC   STRAIN=ATCC 15920 / DSM 528 / H1;
RX   MEDLINE=93041773; 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
RT   Clostridium tetanomorphum gene encoding beta-methylaspartase and
RT   characterization of the recombinant protein.";
RL   Biochemistry 31:10747-10756(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=NCIMB 11547;
RX   MEDLINE=93011908; 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
RT   Clostridium tetanomorphum. Homologies with other cobalamin-dependent
RT   enzymes.";
RL   FEBS Lett. 310:167-170(1992).
CC   -!- CATALYTIC ACTIVITY: L-threo-3-methylaspartate = L-glutamate.
CC   -!- COFACTOR: Cobalamin.
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
CC       mesaconate pathway; acetate and pyruvate from L-glutamate: step
CC       1/4.
CC   -!- SUBUNIT: Possible heterotetramer, composed of two E chains and two
CC       S chains. E exists as a homodimer and S as a monomer.
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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   HSSP; P80077; 1CCW.
DR   SMR; Q05509; 1-483.
DR   BRENDA; 5.4.99.1; 2080.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050097; F:methylaspartate mutase activity; IEA:EC.
DR   GO; GO:0019670; P:anaerobic glutamate catabolic process; IEA:InterPro.
DR   InterPro; IPR014348; Cbl-dep_enz_cat-sub.
DR   InterPro; IPR006396; Glu_mut_E.
DR   InterPro; IPR014714; Glu_mut_E_C.
DR   Gene3D; G3DSA:3.20.20.240; Cobalamin-dep_enz_cat; 1.
DR   Gene3D; G3DSA:3.90.970.10; Glu_mut_E_C; 1.
DR   Pfam; PF06368; Met_asp_mut_E; 1.
DR   PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR   TIGRFAMs; TIGR01503; MthylAspMut_E; 1.
PE   1: Evidence at protein level;
KW   Cobalamin; Cobalt; Direct protein sequencing; Isomerase.
FT   CHAIN         1    485       Methylaspartate mutase E chain.
FT                                /FTId=PRO_0000087512.
FT   CONFLICT      8      8       W -> L (in Ref. 4; AA sequence).
FT   CONFLICT     12     12       E -> G (in Ref. 4; AA sequence).
FT   CONFLICT     17     17       R -> A (in Ref. 4; AA sequence).
FT   CONFLICT     19     19       E -> G (in Ref. 4; AA sequence).
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
//