Fatty acid oxidation complex subunit alpha - Escherichia coli (strain K12)

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P21177 (FADB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
EC=4.2.1.17
EC=5.1.2.3
EC=5.3.3.8
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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of a 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.10
Catalytic activity	(S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH. HAMAP-Rule MF_01621 (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O. HAMAP-Rule MF_01621 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP-Rule MF_01621 (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP-Rule MF_01621
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01621
Subunit structure	Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).
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-Rule 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.
Biophysicochemical properties	Kinetic parameters: K_M=53 µM for crotonyl-CoA (for enoyl-CoA hydratase activity) Ref.8 K_M=5.8 µM for 3-cis-tetradecenoyl-CoA (for Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase activity) K_M=69 µM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity) K_M=2.0 µM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial 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 nucleotide binding Inferred from electronic annotation. Source: InterPro
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-Rule MF_01621

PRO_0000109268

Regions

Nucleotide binding

400 – 402

NAD By similarity

Nucleotide binding

427 – 429

NAD By similarity

Region

1 – 189

189

Enoyl-CoA hydratase/isomerase HAMAP-Rule MF_01621

Region

311 – 729

419

3-hydroxyacyl-CoA dehydrogenase HAMAP-Rule MF_01621

Sites

Active site

450

For 3-hydroxyacyl-CoA dehydrogenase activity Ref.8

Binding site

296

Substrate By similarity

Binding site

324

NAD; via amide nitrogen Probable

Binding site

343

NAD By similarity

Binding site

407

NAD By similarity

Binding site

453

NAD By similarity

Binding site

500

Substrate By similarity

Binding site

660

Substrate By similarity

Site

119

Important for catalytic activity By similarity

Site

139

Important for catalytic activity By similarity

Experimental info

Mutagenesis

322

G → A: 10-fold increase in KM for NADH. Ref.8

Mutagenesis

450

H → A or Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity. Ref.8

Sequence conflict

518

A → R in AAA23750. Ref.1

Sequence conflict

664

F → L in CAB40809. Ref.3

Sequence conflict

666

P → A in CAB40809. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P21177 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 6F1055E402F6B129
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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

« Hide

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon." Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M. J. Biol. Chem. 265:10424-10429(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: K12.
[3]	"Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nakahigashi K., Inokuchi H. Nucleic Acids Res. 18:4937-4937(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli." He X.Y., Yang S.Y. Biochemistry 35:9625-9630(1996) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, NAD-BINDING, MUTAGENESIS OF GLY-322 AND HIS-450.
[9]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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	NP_418288.1. NC_000913.2. YP_491598.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P21177.
SMR	P21177. Positions 1-714.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9560N.
IntAct	P21177. 7 interactions.
STRING	511145.b3846.
Proteomic databases
PaxDb	P21177.
PRIDE	P21177.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76849; AAC76849; b3846. BAE77457; BAE77457; BAE77457.
GeneID	12934454. 948336.
KEGG	ecj:Y75_p3334. eco:b3846.
PATRIC	32123189. VBIEscCol129921_3960.
Organism-specific databases
EchoBASE	EB0275.
EcoGene	EG10279. fadB.
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HOG000261344.
KO	K01825.
OMA	NDQFVKG.
ProtClustDB	PRK11730.
Enzyme and pathway databases
BioCyc	EcoCyc:FADB-MONOMER. ECOL316407:JW3822-MONOMER. MetaCyc:FADB-MONOMER.
UniPathway	UPA00659.
Gene expression databases
Genevestigator	P21177.
Family and domain databases
Gene3D	1.10.1040.10. 2 hits. 3.40.50.720. 1 hit.
HAMAP	MF_01621. FadB.
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_superfam. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012799. FadB. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 2 hits.
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:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents