Reviewed, UniProtKB/Swiss-Prot Q1R972 (FADJ_ECOUT)

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:	UTI89_C2625

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
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. HAMAP MF_01617
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. HAMAP MF_01617
Subcellular location	Cytoplasm By similarity HAMAP MF_01617.
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_0000273982
Regions
	Region	1 – 190	190	Enoyl-CoA hydratase By similarity
	Region	306 – 714	409	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Site	118	1	Important for catalytic activity By similarity
	Site	140	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R972-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: D05212AF62C80111	FASTA	714	77,148
	10 20 30 40 50 60 MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQIRENK 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 ASTDVKKDPG 310 320 330 340 350 360 SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPRGINHALK 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 AALVKFGFPV GPIQLLDEVG 550 560 570 580 590 600 IDTGTKIMPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 610 620 630 640 650 660 IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV FGIGFPPFLG 670 680 690 700 710 GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCDRLVEMSE RGESFWKTTA TDLQ

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000243 Genomic DNA. Translation: ABE08092.1.
RefSeq	YP_541623.1.
3D structure databases
SMR	Q1R972. Positions 5-706.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1R972.
Genome annotation databases
GeneID	3991795.
GenomeReviews	Gene locus UTI89_C2625 in contig CP000243_GR.
KEGG	eci:UTI89_C2625.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HBG691737.
OMA	HATTSDE.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C2625-MONOMER.
Family and domain databases
HAMAP	MF_01617. FadJ. [Tree]
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR001753. Crotonase_core. IPR013328. DH_multihelical. 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. 2 hits. 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_ECOUT

Accession

Primary (citable) accession number: Q1R972

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	May 16, 2006
Last modified:	February 9, 2010
This is version 34 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)