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Q87TN9 (FADB_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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:VP0030
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length723 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 – 723723Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109292

Regions

Nucleotide binding401 – 4033NAD By similarity
Nucleotide binding428 – 4303NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7234133-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
Q87TN9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E4B650E43FE9BAA2

FASTA72378,556
        10         20         30         40         50         60 
MIYQADTLQV KEIQDGIAEL SFCSPKSVNK LDLATLESLD KALDALTSHQ GLKGLMLTSD 

        70         80         90        100        110        120 
KDAFIVGADI TEFLGLFAKT DAELDQWLQF ANSIFNKLED LPVPTISVLK GHTLGGGCEC 

       130        140        150        160        170        180 
VLATDMRIGD KTTSIGLPET KLGIMPGFGG CVRLPRVIGA DSAMEIITQG KACRADEALK 

       190        200        210        220        230        240 
IGLLDAVVET DALYESALQT LTSAINEKID WQARRKQKTS PLTLSKLESM MSFTMAKGLV 

       250        260        270        280        290        300 
AQVAGPHYPA PMTAVITIEE GARFARNEAL DIERKYFVKL AKSEEAKALV GLFLNDQYIK 

       310        320        330        340        350        360 
GIAKKAAKSA SKDTERAAVL GAGIMGGGIA YQSALKGVPV LMKDIAQPSL DLGMTEASKL 

       370        380        390        400        410        420 
LNKRLAQGRI DGFKMAGILA SITPSLHYAG IENSDVIVEA VVENPKVKAT VLSEVESHVG 

       430        440        450        460        470        480 
EDTVITSNTS TIPINLLAQS LKRPENFCGM HFFNPVHRMP LVEIIRGEKT SDETINRVVA 

       490        500        510        520        530        540 
YAAKMGKSPI VVNDCPGFFV NRVLFPYFGG FSMLLRDGAD FTKVDKVMER KFGWPMGPAY 

       550        560        570        580        590        600 
LLDVVGIDTA HHAQAVMAEG FPERMGKQGR DAIDALFEAN KYGQKNGNGF YSYTIDKKGK 

       610        620        630        640        650        660 
PKKTFTEDIL PVLADVCADK QEFDEQTIIQ RMMIPMINEV VLCLQEGIIA TPQEADMALV 

       670        680        690        700        710        720 
YGLGFPPFRG GVFRYLDSVG IAEFVEMAKQ HADLGAMYHV PQMLIDMAAK GESFYGAQQQ 


GSI 

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References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC58293.1.
RefSeqNP_796409.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87TN9.
SMRQ87TN9. Positions 1-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP0030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC58293; BAC58293; BAC58293.
GeneID1187486.
KEGGvpa:VP0030.
PATRIC20138288. VBIVibPar50997_0030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMANPIVVND.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11730.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-30-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_VIBPA
AccessionPrimary (citable) accession number: Q87TN9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 79 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