P37766 (YDIF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetate CoA-transferase YdiF
EC=2.8.3.8

Alternative name(s):
Short-chain acyl-CoA:acetate CoA-transferase

Gene names

Name:	ydiF
Ordered Locus Names:	b1694, JW1684

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. May play a role in short-chain fatty acid metabolism in E.coli By similarity.
Catalytic activity	Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.
Subunit structure	Homotetramer; dimer of dimers By similarity.
Miscellaneous	Formation of the covalent enzyme-CoA thioester intermediate proceeds via an unstable anhydride species formed between the carboxylate group of the catalytic glutamate of the enzyme and the carbonyl carbon of the thioester linkage of the substrate By similarity.
Sequence similarities	Belongs to the 3-oxoacid CoA-transferase family.

Ontologies

Keywords
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ketone body catabolic process Inferred from electronic annotation. Source: InterPro protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB short-chain fatty acid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	acetate CoA-transferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Acetate CoA-transferase YdiF		PRO_0000168990
Sites
	Active site	333	1	Acyl-thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37766 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: E07A0D445015030D	FASTA	531	57,562
	10 20 30 40 50 60 MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL ADKYKQTQTP 70 80 90 100 110 120 RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP RISELAEQNK IIAYNYPQGV 130 140 150 160 170 180 LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA 190 200 210 220 230 240 PDIAFIRATT CDSEGYATFE DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV 250 260 270 280 290 300 RIPGYLVDIV VVDPDQTQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR 310 320 330 340 350 360 KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN VNTRAILDMT 370 380 390 400 410 420 SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG GFIDISATSK KIIFCGTLTA 430 440 450 460 470 480 GSLKTEITDG KLNIVQEGRV KKFIRELPEI TFSGKIALER GLDVRYITER AVFTLKEDGL 490 500 510 520 530 HLIEIAPGVD LQKDILDKMD FTPVISPELK LMDERLFIDA AMGFVLPEAA H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase." Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R. Biochem. J. 238:475-483(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[5]	"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Borodovsky M., Rudd K.E., Koonin E.V. Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74764.1. AP009048 Genomic DNA. Translation: BAA15447.2. X04306 Genomic DNA. No translation available.
PIR	F64927.
RefSeq	NP_416209.1. NC_000913.2. YP_489956.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P37766.
SMR	P37766. Positions 4-529.
ModBase	Search...
Protein-protein interaction databases
IntAct	P37766. 1 interaction.
STRING	511145.b1694.
Proteomic databases
PaxDb	P37766.
PRIDE	P37766.
Protocols and materials databases
DNASU	946211.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74764; AAC74764; b1694. BAA15447; BAA15447; BAA15447.
GeneID	12931296. 946211.
KEGG	ecj:Y75_p1669. eco:b1694.
PATRIC	32118694. VBIEscCol129921_1765.
Organism-specific databases
EchoBASE	EB2328.
EcoGene	EG12432. ydiF.
Phylogenomic databases
eggNOG	COG4670.
HOGENOM	HOG000058376.
OMA	ASDLKVM.
ProtClustDB	CLSK880166.
Enzyme and pathway databases
BioCyc	EcoCyc:EG12432-MONOMER. ECOL316407:JW1684-MONOMER.
Gene expression databases
Genevestigator	P37766.
Family and domain databases
InterPro	IPR014388. 3-oxoacid_CoA-transferase. IPR004165. CoA_trans_fam_I. [Graphical view]
PANTHER	PTHR13707. PTHR13707. 1 hit.
Pfam	PF01144. CoA_trans. 1 hit. [Graphical view]
PIRSF	PIRSF000858. SCOT-t. 1 hit.
SMART	SM00882. CoA_trans. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YDIF_ECOLI

Accession

Primary (citable) accession number: P37766
Secondary accession number(s): P76199, P76898

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program