(data stored in SCRATCH zone)

SWISSPROT: Q8X695_ECO57

ID   Q8X695_ECO57            Unreviewed;       296 AA.
AC   Q8X695; Q7AH67;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 112.
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:AAG54680.1};
GN   OrderedLocusNames=ECs0385 {ECO:0000313|EMBL:BAB33808.1}, Z0427
GN   {ECO:0000313|EMBL:AAG54680.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB33808.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33808.1};
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., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2] {ECO:0000313|EMBL:AAG54680.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54680.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G.III., Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
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: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate =
CC       pyruvate + succinate. {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; AE005174; AAG54680.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33808.1; -; Genomic_DNA.
DR   PIR; A90677; A90677.
DR   PIR; D85527; D85527.
DR   RefSeq; NP_308412.1; NC_002695.1.
DR   RefSeq; WP_000052201.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; Q8X695; -.
DR   STRING; 155864.Z0427; -.
DR   EnsemblBacteria; AAG54680; AAG54680; Z0427.
DR   EnsemblBacteria; BAB33808; BAB33808; BAB33808.
DR   GeneID; 914487; -.
DR   KEGG; ece:Z0427; -.
DR   KEGG; ecs:ECs0385; -.
DR   PATRIC; fig|386585.9.peg.480; -.
DR   eggNOG; ENOG4105CR4; Bacteria.
DR   eggNOG; COG2513; LUCA.
DR   HOGENOM; HOG000220041; -.
DR   KO; K03417; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01939; PrpB; 1.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR012695; PrpB.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02317; prpB; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X695.
DR   SWISS-2DPAGE; Q8X695.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01939,
KW   ECO:0000256|RuleBase:RU361121};
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;  32145 MW;  05EECAE3F85B62EC 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 HYEEKLDDLF VRSQAK
//

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