YBFF_ECOLI
ID YBFF_ECOLI Reviewed; 254 AA.
AC P75736;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Esterase YbfF;
DE EC=3.1.-.-;
GN Name=ybfF; OrderedLocusNames=b0686, JW0673;
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;
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP FUNCTION.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
CC -!- FUNCTION: Displays esterase activity toward palmitoyl-CoA, malonyl-CoA
CC and pNP-butyrate. {ECO:0000269|PubMed:15808744}.
CC -!- SIMILARITY: Belongs to the DmpD/TodF/XylF esterase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC73780.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35335.1; -; Genomic_DNA.
DR PIR; E64803; E64803.
DR RefSeq; NP_415212.1; NC_000913.3.
DR RefSeq; WP_000773288.1; NZ_SSZK01000045.1.
DR PDB; 3BF7; X-ray; 1.10 A; A/B=1-254.
DR PDB; 3BF8; X-ray; 1.68 A; A/B=1-254.
DR PDBsum; 3BF7; -.
DR PDBsum; 3BF8; -.
DR AlphaFoldDB; P75736; -.
DR SMR; P75736; -.
DR BioGRID; 4261906; 7.
DR IntAct; P75736; 4.
DR STRING; 511145.b0686; -.
DR ESTHER; ecoli-ybff; ABHD11-Acetyl_transferase.
DR jPOST; P75736; -.
DR PaxDb; P75736; -.
DR PRIDE; P75736; -.
DR EnsemblBacteria; AAC73780; AAC73780; b0686.
DR EnsemblBacteria; BAA35335; BAA35335; BAA35335.
DR GeneID; 945288; -.
DR KEGG; ecj:JW0673; -.
DR KEGG; eco:b0686; -.
DR PATRIC; fig|1411691.4.peg.1590; -.
DR EchoBASE; EB1725; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_53_1_6; -.
DR InParanoid; P75736; -.
DR OMA; MMYFARK; -.
DR PhylomeDB; P75736; -.
DR BioCyc; EcoCyc:EG11776-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR EvolutionaryTrace; P75736; -.
DR PRO; PR:P75736; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:EcoCyc.
DR GO; GO:0016790; F:thiolester hydrolase activity; IDA:EcoCyc.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..254
FT /note="Esterase YbfF"
FT /id="PRO_0000207081"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /evidence="ECO:0000250"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:3BF7"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:3BF7"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3BF7"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:3BF7"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3BF7"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:3BF7"
SQ SEQUENCE 254 AA; 28437 MW; 8B2F6E28713D9B8A CRC64;
MKLNIRAQTA QNQHNNSPIV LVHGLFGSLD NLGVLARDLV NDHNIIQVDM RNHGLSPRDP
VMNYPAMAQD LVDTLDAQQI DKATFIGHSM GGKAVMALTA LASDRIDKLV AIDIAPVDYH
VRRHDEIFAA INAVSESDAQ TRQQAAAIMR QHLNEEGVIQ FLLKSFVDGE WRFNVPVLWD
QYPHIVGWEK IPAWDHPALF IPGGNSPYVS EQYRDDLLAQ FPQARAHVIA GAGHWVHAEK
PDAVLRAIRR YLND
