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A4STF2 (FADB_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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
Ordered Locus Names:ASA_4250
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length715 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 – 715715Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_1000069558

Regions

Nucleotide binding401 – 4033NAD By similarity
Nucleotide binding428 – 4303NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7154053-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4511For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2961Substrate By similarity
Binding site3251NAD; via amide nitrogen By similarity
Binding site3441NAD By similarity
Binding site4081NAD By similarity
Binding site4541NAD By similarity
Binding site5011Substrate By similarity
Binding site6611Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4STF2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 0B02B7D7F59A55EF

FASTA71576,376
        10         20         30         40         50         60 
MIYQGETLSV SYLENGIAEL RFDAPGSVNK LDRATLLSLS EAIAALQQQA DLKGLILTSG 

        70         80         90        100        110        120 
KDAFIVGADI TEFLELFDLP QEDLLGWLKK ANDIFSAIED LPVPTLSAIK GHALGGGCET 

       130        140        150        160        170        180 
ILSTDFRLAD TSAKIGLPET KLGIMPGFGG TVRLPRVIGA DNALEWITTG KDYRADDALK 

       190        200        210        220        230        240 
VGAIDAVVAP DALHSAAVQM MKDAIAGKLN WQSRRAAKKA PLRLSKLEAM MSFSTAAGMV 

       250        260        270        280        290        300 
AAVAGKHYPA PMTAVKTVEA AAGMSRDEAL VVEAQGFIKL AKTDVAKALV GIFLNDQHIK 

       310        320        330        340        350        360 
ALAKKAAKQA AKATRHAAVL GAGIMGGGIA YQSASKGIPA VMKDINEKAL ALGMGEATKL 

       370        380        390        400        410        420 
LNGQLEKGRI DGIKMGQVLS AITPTLSYDN VKHVDLVVEA VVENPKVKAA VLGEVEGIIG 

       430        440        450        460        470        480 
DDAVLASNTS TIPISLLAKG LKRPQNFCGM HFFNPVHRMP LVEIIRGEQT SDETINRVVA 

       490        500        510        520        530        540 
YAAAMGKSPV VVNDCPGFFV NRVLFPYFFG FNKLVADGAD FAAVDKVMEK EFGWPMGPAY 

       550        560        570        580        590        600 
LLDVVGIDTG HHAGDVMAQG FPARMSKEGR TAIDVMYDAS RFGQKNGKGF YAYEQDKKGK 

       610        620        630        640        650        660 
PKKVADVAAY ELLAPIAKPK QDFDKEAIIA GMMIPMINEV VLCLEEGIVA TPAEADIALV 

       670        680        690        700        710 
YGLGFPPFRG GVFRYLDTIG LDRYVAMADQ YADLGPLYRV SDRLREMAAQ GKTFY 

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO92174.1.
RefSeqYP_001143922.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4STF2.
SMRA4STF2. Positions 1-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382245.ASA_4250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO92174; ABO92174; ASA_4250.
GeneID4998357.
KEGGasa:ASA_4250.
PATRIC20794962. VBIAerSal2987_4215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMAAKGMVMQ.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11730.

Enzyme and pathway databases

BioCycASAL382245:GJJN-4236-MONOMER.
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.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_AERS4
AccessionPrimary (citable) accession number: A4STF2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: April 16, 2014
This is version 55 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