GLME_ECO57
ID GLME_ECO57 Reviewed; 481 AA.
AC Q8X987; Q7AGJ4;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN OrderedLocusNames=ECs0762, Z0893;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=10734605; DOI=10.1266/ggs.74.227;
RA Makino K., Yokoyama K., Kubota Y., Yutsudo C.H., Kimura S., Kurokawa K.,
RA Ishii K., Hattori M., Tatsuno I., Abe H., Iida T., Yamamoto K., Ohnishi M.,
RA Hayashi T., Yasunaga T., Honda T., Sasakawa C., Shinagawa H.;
RT "Complete nucleotide sequence of the prophage VT2-Sakai carrying the
RT verotoxin 2 genes of the enterohemorrhagic Escherichia coli O157:H7 derived
RT from the Sakai outbreak.";
RL Genes Genet. Syst. 74:227-239(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11111050; DOI=10.1016/s0378-1119(00)00416-9;
RA Yokoyama K., Makino K., Kubota Y., Watanabe M., Kimura S., Yutsudo C.H.,
RA Kurokawa K., Ishii K., Hattori M., Tatsuno I., Abe H., Yoh M., Iida T.,
RA Ohnishi M., Hayashi T., Yasunaga T., Honda T., Sasakawa C., Shinagawa H.;
RT "Complete nucleotide sequence of the prophage VT1-Sakai carrying the Shiga
RT toxin 1 genes of the enterohemorrhagic Escherichia coli O157:H7 strain
RT derived from the Sakai outbreak.";
RL Gene 258:127-139(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11108008; DOI=10.1016/s0723-2020(00)80059-4;
RA Ohnishi M., Murata T., Nakayama K., Kuhara S., Hattori M., Kurokawa K.,
RA Yasunaga T., Yokoyama K., Makino K., Shinagawa H., Hayashi T.;
RT "Comparative analysis of the whole set of rRNA operons between an
RT enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an Escherichia
RT coli K-12 strain MG1655.";
RL Syst. Appl. Microbiol. 23:315-324(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(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}.
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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|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: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}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01923}.
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DR EMBL; AE005174; AAG55062.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34185.1; -; Genomic_DNA.
DR PIR; B85575; B85575.
DR PIR; B90724; B90724.
DR RefSeq; NP_308789.1; NC_002695.1.
DR RefSeq; WP_000423320.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X987; -.
DR SMR; Q8X987; -.
DR STRING; 155864.EDL933_0807; -.
DR EnsemblBacteria; AAG55062; AAG55062; Z0893.
DR EnsemblBacteria; BAB34185; BAB34185; ECs_0762.
DR GeneID; 917492; -.
DR KEGG; ece:Z0893; -.
DR KEGG; ecs:ECs_0762; -.
DR PATRIC; fig|386585.9.peg.881; -.
DR eggNOG; COG4865; Bacteria.
DR HOGENOM; CLU_029922_0_0_6; -.
DR OMA; VIVKTPH; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 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 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Reference proteome.
FT CHAIN 1..481
FT /note="Glutamate mutase epsilon subunit"
FT /id="PRO_0000429443"
FT BINDING 67
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 69
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 99
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 122
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 148..149
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 170
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 176
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 179
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 180
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 296
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 325
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 329
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 333
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
SQ SEQUENCE 481 AA; 53068 MW; 81CDF76FB64F1D6A CRC64;
MELRNKKLTH DEFMTERQQV LKTWETGKDV ENFEDGVKYQ QTIPEHKRFS LALLKADKEG
KTLSQPRAGV ALMDEHIELL KTLQEECDLL PSTIDAYTRL NRYEEAAVGI KKSIEAGTSK
LNGLPVVNHG VAACRRLTET LQKPLQIRHG TPDARLLAEI SMASGFTSYE GGGISYNIPY
AKRVTLEKSI RDWQYCDRLM GMYEEHGIRI NREPFGPLTG TLIPPFISHS IAIIEGLLAL
EQGVKSITVG YGQVGSLTQD VAAIQSLREL AHEYFQSYGY TDYELSTVFH QWMGGFPEDE
SKAFAIISWG AAVAGMSGAT KVITKSPHEA WGIPTAAANI QGLKASRQML NMVNEQKFPP
CPAVELEIEL IKSEVRAVLN KVFELGNGDI ARGTVLAFEA GVLDVPFAPA ACNAGKILPV
RDNTGAIRVL EAGAVPLPKD ILDLHHDYVA ERARCEGRQP TFQMVVDDIN AVSHSKLIGR
P
