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CILA_ECOLI
ID   CILA_ECOLI              Reviewed;         510 AA.
AC   P75726; P77102; Q9R7T5; Q9R7T6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Citrate lyase alpha chain;
DE            Short=Citrase alpha chain;
DE            EC=4.1.3.6;
DE   AltName: Full=Citrate (pro-3S)-lyase alpha chain;
DE   AltName: Full=Citrate CoA-transferase subunit;
DE            EC=2.8.3.10;
GN   Name=citF; Synonyms=ybdV; OrderedLocusNames=b0615, JW5087;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=K12 / BW25113;
RX   PubMed=19429622; DOI=10.1128/jb.00108-09;
RA   Shimada T., Yamamoto K., Ishihama A.;
RT   "Involvement of the leucine response transcription factor LeuO in
RT   regulation of the genes for sulfa drug efflux.";
RL   J. Bacteriol. 191:4562-4571(2009).
CC   -!- FUNCTION: Represents a citrate:acetyl-ACP transferase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
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   -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Repressed by H-NS. Part of the citCDEFXG operon.
CC       {ECO:0000269|PubMed:19429622}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40815.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U82598; AAB40815.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73716.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35251.2; -; Genomic_DNA.
DR   PIR; E64795; E64795.
DR   RefSeq; NP_415148.1; NC_000913.3.
DR   RefSeq; WP_000192242.1; NZ_LN832404.1.
DR   AlphaFoldDB; P75726; -.
DR   SMR; P75726; -.
DR   BioGRID; 4261998; 7.
DR   ComplexPortal; CPX-4781; Citrate lyase complex.
DR   STRING; 511145.b0615; -.
DR   PaxDb; P75726; -.
DR   PRIDE; P75726; -.
DR   EnsemblBacteria; AAC73716; AAC73716; b0615.
DR   EnsemblBacteria; BAA35251; BAA35251; BAA35251.
DR   GeneID; 945230; -.
DR   KEGG; ecj:JW5087; -.
DR   KEGG; eco:b0615; -.
DR   PATRIC; fig|1411691.4.peg.1653; -.
DR   EchoBASE; EB3311; -.
DR   eggNOG; COG3051; Bacteria.
DR   HOGENOM; CLU_046521_2_0_6; -.
DR   InParanoid; P75726; -.
DR   OMA; GHCDVAA; -.
DR   PhylomeDB; P75726; -.
DR   BioCyc; EcoCyc:CITTRANS-MON; -.
DR   BioCyc; MetaCyc:CITTRANS-MON; -.
DR   PRO; PR:P75726; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009346; C:ATP-independent citrate lyase complex; IPI:ComplexPortal.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008814; F:citrate CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:ComplexPortal.
DR   GO; GO:0006101; P:citrate metabolic process; IDA:ComplexPortal.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Reference proteome; Transferase.
FT   CHAIN           1..510
FT                   /note="Citrate lyase alpha chain"
FT                   /id="PRO_0000089752"
SQ   SEQUENCE   510 AA;  55173 MW;  CA466F1620D8EB92 CRC64;
     MTQKIEQSQR QERVAAWNRR AECDLAAFQN SPKQTYQAEK ARDRKLCANL EEAIRRSGLQ
     DGMTVSFHHA FRGGDLTVNM VMDVIAKMGF KNLTLASSSL SDCHAPLVEH IRQGVVTRIY
     TSGLRGPLAE EISRGLLAEP VQIHSHGGRV HLVQSGELNI DVAFLGVPSC DEFGNANGYT
     GKACCGSLGY AIVDADNAKQ 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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