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Reviewed, UniProtKB/Swiss-Prot A5F465 (FADB_VIBC3)

Last modified June 16, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
              EC=4.2.1.17
              EC=5.3.3.8
              EC=5.1.2.3
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35
Gene names
Name: fadB
Ordered Locus Names: VC0395_A2534
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.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity.

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP 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 MF_01621
PRO_1000073635

Regions

Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region312 – 7234123-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

Sequence LengthMass (Da)Tools
A5F465-1 [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 

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References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000627 Genomic DNA. Translation: ABQ19542.1.
RefSeqYP_001218427.1.
YP_002818460.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5136027.
7774288.
GenomeReviewsGene locus VC0395_A2534 in contig CP000627_GR.
KEGGvco:VC0395_A2534.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA5F465. SEDTINR.

Family and domain databases

HAMAPMF_01621.
[Tree]
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR001753. Crotonase_core.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_VIBC3
AccessionPrimary (citable) accession number: A5F465
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: June 16, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents