(data stored in ACNUC10821 zone)

SWISSPROT: C8U2X8_ECO10

ID   C8U2X8_ECO10            Unreviewed;       510 AA.
AC   C8U2X8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   RecName: Full=Citrate lyase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE            Short=Citrase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE            EC=2.8.3.10 {ECO:0000256|PIRNR:PIRNR009451};
DE            EC=4.1.3.6 {ECO:0000256|PIRNR:PIRNR009451};
DE   AltName: Full=Citrate (pro-3S)-lyase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE   AltName: Full=Citrate CoA-transferase subunit {ECO:0000256|PIRNR:PIRNR009451};
GN   Name=citF {ECO:0000313|EMBL:BAI29486.1};
GN   OrderedLocusNames=ECO103_0623 {ECO:0000313|EMBL:BAI29486.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29486.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29486.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + citrate = (3S)-citryl-CoA + acetate;
CC         Xref=Rhea:RHEA:19405, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57321; EC=2.8.3.10;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089;
CC         EC=4.1.3.6; Evidence={ECO:0000256|PIRNR:PIRNR009451};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR009451}.
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DR   EMBL; AP010958; BAI29486.1; -; Genomic_DNA.
DR   RefSeq; WP_000192245.1; NC_013353.1.
DR   SMR; C8U2X8; -.
DR   EnsemblBacteria; BAI29486; BAI29486; ECO103_0623.
DR   KEGG; eoh:ECO103_0623; -.
DR   HOGENOM; HOG000117923; -.
DR   KO; K01643; -.
DR   OMA; GHCDVAA; -.
DR   BioCyc; ECOL585395:ECO103_RS03250-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0009346; C:citrate lyase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008814; F:citrate CoA-transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR006472; Citrate_lyase_asu.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR40596; PTHR40596; 1.
DR   Pfam; PF04223; CitF; 1.
DR   PIRSF; PIRSF009451; Citrt_lyas_alpha; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
DR   TIGRFAMs; TIGR01584; citF; 1.
PE   4: Predicted;
DR   PRODOM; C8U2X8.
DR   SWISS-2DPAGE; C8U2X8.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR009451};
KW   Lyase {ECO:0000256|PIRNR:PIRNR009451, ECO:0000313|EMBL:BAI29486.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR009451,
KW   ECO:0000313|EMBL:BAI29486.1}.
FT   COILED       33     53       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   510 AA;  55191 MW;  D787C0AC34DB3D53 CRC64;
     MTQKIEQSQR QERVAAWNRR AECDLAAFQN SPKQTYQAEK ARDRKLCANL EEAIRRSGLQ
     DGMTVSFHHA FRGGDLTVNM VMDVIAKMGF KNLTLASSSL SDCHAPLVEH IRQGVVTRIY
     TSGLRGPLAE EISRGLLAEP VQIHSHGGRV HLVQSGELNI DVAFLGVPSC DEFGNANGYT
     GKACCGSLGY AMVDADNAKQ VVMLTEELLP YPHNPASIEQ DQVDLIVKVD RVGDAAKIGA
     GATRMTTNPR ELLIARSAAD VIVNSGYFKE GFSMQTGTGG ASLAVTRFLE DKMRSRDIRA
     DFALGGITAT MVDLHEKGLI RKLLDVQSFD SHAAQSLARN PNHIEISANQ YANWGSKGAS
     VDRLDVVVLS ALEIDTQFNV NVLTGSDGVL RGASGGHCDT AIASALSIIV APLVRGRIPT
     LVDNVLTCIT PGSSVDILVT DHGIAVNPAR PELAERLQEA GIKVVSIEWL RERARLLTGE
     PQPIEFTDRV VAVVRYRDGS VIDVVHQVKE
//

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