Reviewed, UniProtKB/Swiss-Prot Q0TFA6 (FADJ_ECOL5)

Names and origin

Protein names

Recommended name:
    Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase
              EC=4.2.1.17
              EC=5.1.2.3
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35

Gene names

Name:	fadJ
Ordered Locus Names:	ECP_2379

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity.
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01617 (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01617 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01617
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01617
Subunit structure	Heterotetramer of two alpha chains (fadJ) and two beta chains (fadI) By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 3-hydroxybutyryl-CoA epimerase activity Inferred from electronic annotation. Source: HAMAP NAD or NADH binding Inferred from electronic annotation. Source: InterPro enoyl-CoA hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 714	714	Fatty acid oxidation complex subunit alpha HAMAP MF_01617		PRO_0000273983
Regions
	Region	1 – 190	190	Enoyl-CoA hydratase By similarity
	Region	306 – 714	409	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Active site	118	1	By similarity
	Active site	140	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0TFA6-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: F1A53A6CAF6CEE26	FASTA	714	77,144
	10 20 30 40 50 60 MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA 70 80 90 100 110 120 KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA 130 140 150 160 170 180 LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAV 190 200 210 220 230 240 KLGLVDDVVP HSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT 250 260 270 280 290 300 QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDPG 310 320 330 340 350 360 SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPQGINHALK YSWDQLEGKV 370 380 390 400 410 420 RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL ELKQQMVAEV EQNCATHTIF 430 440 450 460 470 480 ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHASTSAQTI ATTVKLAKKQ 490 500 510 520 530 540 GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERIEHID TALVKFGFPV GPIQLLDEVG 550 560 570 580 590 600 IDTGTKIMPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 610 620 630 640 650 660 IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VCCLDEQVIR SVRDGDIGAV FGIGFPPFLG 670 680 690 700 710 GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCNRFVEMSE RGESFWKTTA TDLQ

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000247 Genomic DNA. Translation: ABG70373.1.
RefSeq	YP_670274.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4188711.
GenomeReviews	Gene locus ECP_2379 in contig CP000247_GR.
KEGG	ecp:ECP_2379.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0TFA6.
OMA	Q0TFA6. AYAMTIP.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_2379-MON.
Family and domain databases
HAMAP	MF_01617. [Tree]
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012802. FadJ. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 2 hits.
Pfam	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02440. FadJ. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADJ_ECOL5

Accession

Primary (citable) accession number: Q0TFA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 26 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)