Reviewed, UniProtKB/Swiss-Prot P21177 (FADB_ECOLI)

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
Synonyms:	oldB
Ordered Locus Names:	b3846, JW3822

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. Ref.7
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. Ref.7
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA). HAMAP MF_01621
Induction	Repressed by fadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to fadR resulting in its release from the DNA and thus derepression of the transcription. 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_0000109268
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 HAMAP MF_01621
	Region	311 – 729	419	3-hydroxyacyl-CoA dehydrogenase HAMAP MF_01621
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
Experimental info
	Sequence conflict	518	1	A → R in AAA23750. Ref.1
	Sequence conflict	664	1	F → L Ref.2
	Sequence conflict	666	1	P → A Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P21177-1 [UniParc]. Last modified August 1, 1992. Version 2. Checksum: 6F1055E402F6B129	FASTA	729	79,594
	10 20 30 40 50 60 MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK 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 EKLVEGAKAV LRQAINGDLD WKAKRQPKLE PLKLSKIEAT 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 DRVDIVVEAV VENPKVKKAV LAETEQKVRQ 430 440 450 460 470 480 DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 490 500 510 520 530 540 ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL 550 560 570 580 590 600 LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP 610 620 630 640 650 660 KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY 670 680 690 700 710 720 GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA RPVGDLKTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes." Dirusso C.C. J. Bacteriol. 172:6459-6468(1990) [PubMed: 1699931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nakahigashi K., Inokuchi H. Nucleic Acids Res. 18:4937-4937(1990) [PubMed: 2204034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli." Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y. Biochemistry 30:6788-6795(1991) [PubMed: 1712230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed: 1379743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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.
[6]	"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.
[7]	"A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr. Mol. Microbiol. 47:793-805(2003) [PubMed: 12535077] [Abstract] Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M59368 Genomic DNA. Translation: AAA23750.1. X52837 Genomic DNA. Translation: CAB40809.1. M74164 Genomic DNA. Translation: AAA62777.1. M87049 Genomic DNA. Translation: AAA67643.1. U00096 Genomic DNA. Translation: AAC76849.1. AP009048 Genomic DNA. Translation: BAE77457.1.
PIR	A39592.
RefSeq	AP_003956.1. NP_418288.1.
3D structure databases
HSSP	HSSP built from PDB template 3HDH based on UniProtKB P00348.
ModBase	Search...
Protein-protein interaction databases
STRING	P21177.
2-D gel databases
ECO2DBASE	G073.4. 6TH EDITION. G073.5. 6TH EDITION.
Proteomic databases
PRIDE	P21177.
Genome annotation databases
GeneID	948336.
GenomeReviews	Gene locus JW3822 in contig AP009048_GR. Gene locus b3846 in contig U00096_GR.
KEGG	ecj:JW3822. eco:b3846.
Organism-specific databases
EchoBASE	EB0275.
EcoGene	EG10279. fadB.
CMR	Search...
Phylogenomic databases
HOGENOM	P21177.
OMA	ANNGSYY.
Enzyme and pathway databases
BioCyc	EcoCyc:FADB-MON. MetaCyc:FADB-MON.
Gene expression databases
Genevestigator	P21177.
Family and domain databases
HAMAP	MF_01621. [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. 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_ECOLI

Accession

Primary (citable) accession number: P21177
Secondary accession number(s): Q2M8E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	August 1, 1992
Last modified:	November 3, 2009
This is version 95 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)