(data stored in SCRATCH zone)

SWISSPROT: C8U225_ECO10

ID   C8U225_ECO10            Unreviewed;       296 AA.
AC   C8U225;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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:BAI29183.1};
GN   OrderedLocusNames=ECO103_0314 {ECO:0000313|EMBL:BAI29183.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29183.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29183.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI29183.1; -; Genomic_DNA.
DR   RefSeq; WP_000052205.1; NC_013353.1.
DR   EnsemblBacteria; BAI29183; BAI29183; ECO103_0314.
DR   KEGG; eoh:ECO103_0314; -.
DR   HOGENOM; HOG000220041; -.
DR   KO; K03417; -.
DR   OMA; SMVLYPL; -.
DR   BioCyc; ECOL585395:ECO103_RS01645-MONOMER; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000959; 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; C8U225.
DR   SWISS-2DPAGE; C8U225.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121,
KW   ECO:0000313|EMBL:BAI29183.1};
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   296 AA;  32136 MW;  2201DAE3F84472F3 CRC64;
     MSLHSPGKAF RAALTKENPL QIVGTINANH ALLAQRAGYQ AIYLSGGGVA AGSLGLPDLG
     ISTLDDVLTD IRRITDVCSL PLLVDADIGF GSSAFNVART VKSMIKAGAA GLHIEDQVGA
     KRCGHRPNKA IVSKEEMVDR IRAAVDAKTD PDFVIMARTD ALAVEGLDAA IERAQAYVEA
     GAEMLFPEAI TELAMYRQFA DAVQVPILAN ITEFGATPLF TTDELRSAHV AMALYPLSAF
     RAMNRAAEHV YNVLRQEGTQ KSVIDTMQTR NELYESINYY QYEEKLDDLF ARSQVK
//

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