(data stored in ACNUC7421 zone)

SWISSPROT: B7ULK8_ECO27

ID   B7ULK8_ECO27            Unreviewed;       149 AA.
AC   B7ULK8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Glutamate mutase sigma subunit {ECO:0000256|HAMAP-Rule:MF_00526};
DE            EC=5.4.99.1 {ECO:0000256|HAMAP-Rule:MF_00526};
DE   AltName: Full=Glutamate mutase S chain {ECO:0000256|HAMAP-Rule:MF_00526};
DE   AltName: Full=Glutamate mutase small subunit {ECO:0000256|HAMAP-Rule:MF_00526};
DE   AltName: Full=Methylaspartate mutase {ECO:0000256|HAMAP-Rule:MF_00526};
GN   Name=glmS {ECO:0000256|HAMAP-Rule:MF_00526};
GN   OrderedLocusNames=E2348C_0612 {ECO:0000313|EMBL:CAS08160.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08160.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08160.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-
CC       glutamate to L-threo-3-methylaspartate ((2S,3S)-3-
CC       methylaspartate). {ECO:0000256|HAMAP-Rule:MF_00526}.
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:0000256|HAMAP-Rule:MF_00526};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00526};
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
CC       mesaconate pathway; acetate and pyruvate from L-glutamate: step
CC       1/4. {ECO:0000256|HAMAP-Rule:MF_00526}.
CC   -!- SUBUNIT: Heterotetramer composed of 2 epsilon subunits (GlmE) and
CC       2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a
CC       monomer. {ECO:0000256|HAMAP-Rule:MF_00526}.
CC   -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit
CC       family. {ECO:0000256|HAMAP-Rule:MF_00526}.
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DR   EMBL; FM180568; CAS08160.1; -; Genomic_DNA.
DR   RefSeq; WP_000710397.1; NC_011601.1.
DR   EnsemblBacteria; CAS08160; CAS08160; E2348C_0612.
DR   KEGG; ecg:E2348C_0612; -.
DR   HOGENOM; HOG000011065; -.
DR   KO; K01846; -.
DR   OMA; GHGEMDC; -.
DR   BioCyc; ECOL574521:E2348C_RS03250-MONOMER; -.
DR   UniPathway; UPA00561; UER00617.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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; cd02072; Glm_B12_BD; 1.
DR   HAMAP; MF_00526; Me_Asp_mutase_S; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006394; GlmS.
DR   Pfam; PF02310; B12-binding; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR01501; MthylAspMutase; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7ULK8.
DR   SWISS-2DPAGE; B7ULK8.
KW   Cobalamin {ECO:0000256|HAMAP-Rule:MF_00526};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00526};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00526};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00526}.
FT   DOMAIN        3    140       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   REGION       13     17       Adenosylcobalamin binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00526}.
FT   REGION       61     63       Adenosylcobalamin binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00526}.
FT   REGION       93     97       Adenosylcobalamin binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00526}.
FT   METAL        16     16       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|HAMAP-Rule:MF_00526}.
SQ   SEQUENCE   149 AA;  16372 MW;  8485DAE49C27D899 CRC64;
     MKKATLVIGV IGADCHAVGN KVLDRVFSNH GFRVINLGVM VSQDEYIDAA IETGADAIVV
     SSIYGHGDID CLGMRERCIE RGLGDILLYV GGNLVVGKHD FADVETKFKE MGFDRVFAPS
     HDLEDVCQLM AHDINQRHDV DTRILEEAI
//

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