Fatty acid oxidation complex subunit alpha

Preferred order of sections

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

Organism

Enterobacter cloacae

Taxonomic identifier

550 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity. HAMAP-Rule MF_01621
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) By similarity.
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	Multifunctional enzyme
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_0000109266

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)

Tools

Q9F0Y7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 68EBD8FD10AC7204
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FASTA

729

79,759

        10         20         30         40         50         60 
MLYKGDTLYL NWLEDGIAEL VFDAPGSVNK LDTATVASLG QALDVLEKQP ELKGMLLRSN 

        70         80         90        100        110        120 
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTISAVN GYALGGGCEC 

       130        140        150        160        170        180 
VLATDYRLAT PDLRIGLPET RLGIMPGFGG SVRMPRMLGA DSAMEIIAAG KDVGAEQAQK 

       190        200        210        220        230        240 
IGLVDGVVKP EKLVEGALAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV 

       250        260        270        280        290        300 
MQTAGKHYPA PITAVKTIEA AARLGRDEAL KLENQSFVPL AHTNEARALV GIFLNDQFVK 

       310        320        330        340        350        360 
GKARQLTKNV ETPKHAAVLG AGIMGGGIAY QSAWKGVPVV MKDISEKSLT LGMTEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKLAGVIST IQPVLEYSGF DRVDVVVEAV VENPKVKKAV LAETEDKVRP 

       430        440        450        460        470        480 
ETVLASNTST IPISELASVL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS DETIAKVVAW 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKENSKGKP 

       610        620        630        640        650        660 
KKEEDAVVDG LLADVSQPKR DFTDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG AFRWLDTLGS ARYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPAVEPA 


RPVGELKTA

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References

[1]

"Fatty acid competition as a mechanism by which Enterobacter cloacae suppresses Pythium ultimum sporangium germination and damping-off."
van Dijk K., Nelson E.B.
Appl. Environ. Microbiol. 66:5340-5347(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A-11 / 501R3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF191029 Genomic DNA. Translation: AAG17183.1.
3D structure databases
ProteinModelPortal	Q9F0Y7.
SMR	Q9F0Y7. Positions 1-714.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00659.
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_ENTCL

Accession

Primary (citable) accession number: Q9F0Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents