(data stored in SCRATCH zone)

SWISSPROT: B7UJI1_ECO27

ID   B7UJI1_ECO27            Unreviewed;       293 AA.
AC   B7UJI1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
DE            Short=2-MIC {ECO:0000256|HAMAP-Rule:MF_01939};
DE            Short=MICL {ECO:0000256|HAMAP-Rule:MF_01939};
DE            EC=4.1.3.30 {ECO:0000256|HAMAP-Rule:MF_01939};
DE   AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
GN   Name=prpB {ECO:0000256|HAMAP-Rule:MF_01939,
GN   ECO:0000313|EMBL:CAS07839.1};
GN   OrderedLocusNames=E2348C_0291 {ECO:0000313|EMBL:CAS07839.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07839.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07839.1, 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 thermodynamically favored C-C bond
CC       cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and
CC       succinate. {ECO:0000256|RuleBase:RU361121}.
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids
CC       (SCFA) via the 2-methylcitrate cycle (propionate degradation
CC       route). Catalyzes the thermodynamically favored C-C bond cleavage
CC       of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via
CC       an alpha-carboxy-carbanion intermediate. {ECO:0000256|HAMAP-
CC       Rule:MF_01939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC         succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01939,
CC         ECO:0000256|RuleBase:RU361121};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01939};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_01939}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase
CC       superfamily. Methylisocitrate lyase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
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DR   EMBL; FM180568; CAS07839.1; -; Genomic_DNA.
DR   RefSeq; WP_000052189.1; NC_011601.1.
DR   EnsemblBacteria; CAS07839; CAS07839; E2348C_0291.
DR   KEGG; ecg:E2348C_0291; -.
DR   HOGENOM; HOG000220041; -.
DR   KO; K03417; -.
DR   OMA; SMVLYPL; -.
DR   BioCyc; ECOL574521:E2348C_RS01535-MONOMER; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   HAMAP; MF_01939; PrpB; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR012695; PrpB.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02317; prpB; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UJI1.
DR   SWISS-2DPAGE; B7UJI1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121,
KW   ECO:0000313|EMBL:CAS07839.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01939};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}.
FT   REGION       45     47       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01939}.
FT   REGION      123    124       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01939}.
FT   REGION      210    212       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01939}.
FT   METAL        85     85       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   METAL        87     87       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     158    158       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     188    188       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     241    241       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     270    270       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
SQ   SEQUENCE   293 AA;  31698 MW;  3198E573E76024C3 CRC64;
     MSLHSPGKAF RAALTKENPL QIVGTINANH ALLAQRAGYQ AIYLSGGGVA AGSLGLPDLG
     ISTLDDVLTD IRRITDVCSL PLLVDADIGF GSSAFNVART VKSMIKAGAA GLHIEDQVGA
     KRCGHRPNKA IVSKEEMVDR ICAAVDAKTD PDFVIMARTD ALAVEGLDAA IERAEAYVEA
     GAEMLFPEAI TELAMYRQFA DAVQVPILAN ITEFGATPLF TTDELRSAHV AMALYPLSAF
     RAMNRAAEHV YNVLRQEGTQ KSVIDTMQTR NELYESINYY QYEEKLDDLF ARG
//

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