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Q9F0Y7 (FADB_ENTCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. 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
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadB
OrganismEnterobacter cloacae
Taxonomic identifier550 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109266

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7294193-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2961Substrate By similarity
Binding site3241NAD; via amide nitrogen By similarity
Binding site3431NAD By similarity
Binding site4071NAD By similarity
Binding site4531NAD By similarity
Binding site5001Substrate By similarity
Binding site6601Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9F0Y7 [UniParc].

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

FASTA72979,759
        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

ProteinModelPortalQ9F0Y7.
SMRQ9F0Y7. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01621. FadB.
InterProIPR006180. 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]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_ENTCL
AccessionPrimary (citable) accession number: Q9F0Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways