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A5F465 (FADB_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:VC0395_A2534, VC395_0197
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [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_1000073635

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
A5F465 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 9E512BE6A218C80D

FASTA72378,076
        10         20         30         40         50         60 
MIYQAKTLQV KQLANGIAEL SFCAPASVNK LDLHTLESLD KALDALAADS SVKGLLLSSD 

        70         80         90        100        110        120 
KEAFIVGADI TEFLGLFAKP EAELDEWLQF ANRIFNKLED LPFPTLSALK GHTLGGGCEC 

       130        140        150        160        170        180 
VLATDFRIGD ATTSIGLPET KLGIMPGFGG TVRLPRLIGA DSAMEIITQG KACRAEEALK 

       190        200        210        220        230        240 
VGLLDAIVDS DKLIDSAITT LTQAIEEKLD WQKRRQQKTS ALTLSKLEAM MSFTMAKGMV 

       250        260        270        280        290        300 
AQVAGKHYPA PMTSVVTIEE AARLPRDAAL DIERKHFIKL AKSTEAQALV GIFLNDQYIK 

       310        320        330        340        350        360 
GLAKQSAKAA SQDTQHAAVL GAGIMGGGIA YQSALKGVPV LMKDIAPHSL ELGMTEAAKL 

       370        380        390        400        410        420 
LNKQLERGKI DGFKMAGILA SITPSLHYAG IDQADVIVEA VVENPKVKAA VLSEVEGLVD 

       430        440        450        460        470        480 
AETILTSNTS TIPINLLAKS LKRPQNFCGM HFFNPVHRMP LVEIIRGEHT SEDTINRVVA 

       490        500        510        520        530        540 
YAAKMGKSPI VVNDCPGFFV NRVLFPYFAG FSLLMRDGAN FTEIDKVMER QFGWPMGPAY 

       550        560        570        580        590        600 
LLDVVGIDTA HHAQAVMAEG FPTRMAKSGR EAIDALYEAK KFGQKNGSGF YQYTVDKKGK 

       610        620        630        640        650        660 
PKKAFSDDVL AILAPVCGAP QNFDPQTLIE RTMIPMINEV VLCLEEGIIA SAQEADMALV 

       670        680        690        700        710        720 
YGLGFPPFRG GVFRYLDTIG IANYVAMAEK YADLGALYQV PQLLKNMAQQ GTSFYSAQQA 


SAL 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ19542.1.
CP001235 Genomic DNA. Translation: ACP08224.1.
RefSeqYP_001218427.1. NC_009457.1.
YP_002818460.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F465.
SMRA5F465. Positions 1-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A2534.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ19542; ABQ19542; VC0395_A2534.
ACP08224; ACP08224; VC395_0197.
GeneID5136027.
7774288.
KEGGvco:VC0395_A2534.
vcr:VC395_0197.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMAAKGMVMQ.
ProtClustDBPRK11730.

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.
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_VIBC3
AccessionPrimary (citable) accession number: A5F465
Secondary accession number(s): C3M345
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 53 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