Reviewed, UniProtKB/Swiss-Prot Q1R466 (FADB_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/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
              EC=4.2.1.17
              EC=5.3.3.8
              EC=5.1.2.3
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35

Gene names

Name:	fadB
Ordered Locus Names:	UTI89_C4431

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	729 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_01621
Catalytic activity	(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621 (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621 (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01621
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01621
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid catabolic process 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 coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: HAMAP 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 – 729	729	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_0000255841
Regions
	Nucleotide binding	400 – 402	3	NAD By similarity
	Nucleotide binding	427 – 429	3	NAD By similarity
	Region	1 – 189	189	Enoyl-CoA hydratase/isomerase By similarity
	Region	311 – 729	419	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Binding site	296	1	Substrate By similarity
	Binding site	324	1	NAD; via amide nitrogen By similarity
	Binding site	343	1	NAD By similarity
	Binding site	407	1	NAD By similarity
	Binding site	453	1	NAD By similarity
	Binding site	500	1	Substrate By similarity
	Binding site	660	1	Substrate By similarity
	Site	119	1	Important for catalytic activity By similarity
	Site	139	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R466-1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 7189317A309D7190	FASTA	729	79,531
	10 20 30 40 50 60 MLYKGDTLYL DWLEDGIAEL VFDTPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN 70 80 90 100 110 120 KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC 130 140 150 160 170 180 VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK 190 200 210 220 230 240 IGLVDGVVKA EKLVEGAIAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAA MSFTIAKGMV 250 260 270 280 290 300 AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 310 320 330 340 350 360 GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT LGMTEAAKLL 370 380 390 400 410 420 NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP 430 440 450 460 470 480 DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 490 500 510 520 530 540 ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGAGF RKIDKVMEKQ FGWPMGPAYL 550 560 570 580 590 600 LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP 610 620 630 640 650 660 KKEEDVVVDD LLAKVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY 670 680 690 700 710 720 GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA RPVGDLKTA

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: ABE09848.1. Different initiation.
RefSeq	YP_543379.2.
3D structure databases
SMR	Q1R466. Positions 1-714.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1R466.
Genome annotation databases
GeneID	3993837.
GenomeReviews	Gene locus UTI89_C4431 in contig CP000243_GR.
KEGG	eci:UTI89_C4431.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HBG691737.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C4431-MONOMER.
Family and domain databases
HAMAP	MF_01621. FadB. [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. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012799. FadB. 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. 1 hit.
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02437. FadB. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_ECOUT

Accession

Primary (citable) accession number: Q1R466

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	February 9, 2010
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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