Reviewed, UniProtKB/Swiss-Prot P77467 (PAAG_ECOLI)

Names and origin

Protein names

Recommended name:
    Probable enoyl-CoA hydratase paaG
    EC=4.2.1.17

Gene names

Name:	paaG
Synonyms:	ydbT
Ordered Locus Names:	b1394, JW1389

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could possibly oxidizes fatty acids using specific components By similarity.
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
Pathway	Aromatic compound metabolism; phenylacetic acid degradation.
Induction	Activated by cAMP receptor protein (CRP) and integration host factor (IHF). Inhibited by paaX.
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sdhA	P0AC41	1	EBI-1118484,EBI-371263

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 262	262	Probable enoyl-CoA hydratase paaG
Natural variations
	Natural variant	121	1	G → C in strain: W.

Sequences

	Sequence		Length	Mass (Da)
	P77467-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: DD7B95B30D88660C	FASTA	262	28,405
	10 20 30 40 50 60 MMEFILSHVE KGVMTLTLNR PERLNSFNDE MHAQLAECLK QVERDDTIRC LLLTGAGRGF 70 80 90 100 110 120 CAGQDLNDRN VDPTGPAPDL GMSVERFYNP LVRRLAKLPK PVICAVNGVA AGAGATLALG 130 140 150 160 170 180 GDIVIAARSA KFVMAFSKLG LIPDCGGTWL LPRVAGRARA MGLALLGNQL SAEQAHEWGM 190 200 210 220 230 240 IWQVVDDETL ADTAQQLARH LATQPTFGLG LIKQAINSAE TNTLDTQLDL ERDYQRLAGR 250 260 SADYREGVSA FLAKRSPQFT GK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., Diaz E. J. Biol. Chem. 273:25974-25986(1998) [PubMed: 9748275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: W / ATCC 11105 / DSM 1900.
[2]	"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: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli." Ferrandez A., Garcia J.L., Diaz E. J. Biol. Chem. 275:12214-12222(2000) [PubMed: 10766858] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X97452 Genomic DNA. Translation: CAA66096.1. U00096 Genomic DNA. Translation: AAC74476.1. AP009048 Genomic DNA. Translation: BAA15000.1.
PIR	E64890.
RefSeq	AP_002021.1. NP_415912.1.
3D structure databases
HSSP	HSSP built from PDB template 1MJ3 based on UniProtKB P14604.
ModBase	Search...
Protein-protein interaction databases
IntAct	P77467.
Genome annotation databases
GeneID	946263.
GenomeReviews	Gene locus b1394 in contig U00096_GR. Gene locus JW1389 in contig AP009048_GR.
KEGG	ecj:JW1389. eco:b1394.
Organism-specific databases
EchoBASE	EB3504.
EcoGene	EG13741. paaG.
CMR	Search...
Phylogenomic databases
HOGENOM	P77467.
Enzyme and pathway databases
BioCyc	EcoCyc:G6715-MON. MetaCyc:G6715-MON.
Family and domain databases
InterPro	IPR001753. Crotonase_core. IPR011968. PaaB1. [Graphical view]
Pfam	PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02280. PaaB1. 1 hit.
PROSITE	PS00166. ENOYL_COA_HYDRATASE. False negative. [Graphical view]
ProDom	P77467. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

PAAG_ECOLI

Accession

Primary (citable) accession number: P77467
Secondary accession number(s): O53015

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	September 2, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)