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B0VE45 (FADB_ACIBY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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:ABAYE3470
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length717 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 – 717717Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_1000186030

Regions

Nucleotide binding402 – 4043NAD By similarity
Nucleotide binding429 – 4313NAD By similarity
Region1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Region313 – 7174053-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4521For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2981Substrate By similarity
Binding site3261NAD; via amide nitrogen By similarity
Binding site3451NAD By similarity
Binding site4091NAD By similarity
Binding site4551NAD By similarity
Binding site5021Substrate By similarity
Site1201Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VE45 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: C8F7CAC439DE6C1B

FASTA71777,874
        10         20         30         40         50         60 
MIHAGNAITV QMLADGIAEF RFDLQGESVN KFNRATIEDF KAAIAAVKAN NDIKGLVVTS 

        70         80         90        100        110        120 
GKSTFIVGAD ITEFGQNFAQ GEKAIVDWLM PVHEIFNSFE DLDLPKVAAI NGMALGGGFE 

       130        140        150        160        170        180 
MCLVCDYRVM SEAAQVGLPE IKLGIYPGFG GSVRLSRLIG IDNAVEWMAM ATPKKPAAAL 

       190        200        210        220        230        240 
KDGAVDAVVA ADKLLDAATD LVKQAISGRL NWKAKRQEKL EAVKLNPLEQ MMAFNTAKGA 

       250        260        270        280        290        300 
VLAKANPAQY PAPKLLLDSL QAGASLARDE ALKAEAEGFA KAAVTPQAEA LIGLFINDQV 

       310        320        330        340        350        360 
VKKASKQHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ LALGMKEANN 

       370        380        390        400        410        420 
LLTKQVERKK MKPVQMGETL ARIRPTLSYE EFKEVDIVIE AVTENPKVKE IVLAETEKNV 

       430        440        450        460        470        480 
RENTIIASNT STISITRLAK ALQRPENFVG MHFFNPVHMM PLVEVIRGEK TSEEAIATTV 

       490        500        510        520        530        540 
VLAQKMGKTP IVVNDCPGFL VNRVLFPYFG AFDLLVKDGA DFQQIDNVMS KFGWPMGPAY 

       550        560        570        580        590        600 
LIDVVGIDTG VHGAEVMAEG FPDRMKPDYK GAIEAMYEAK RLGQKNDVGF YKYELDKKGK 

       610        620        630        640        650        660 
KAKTVDPTAY EVIAPFVTGE KREFDNQEII DRMMLALCNE TVRCLEDNIV ATASEADMAM 

       670        680        690        700        710 
IMGIGFPPFR GGPCRYIDQT GVAEYVALCD KYAHLGKAYE APQMLRDMAA NNKKFYG 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AYE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU459141 Genomic DNA. Translation: CAM88259.1.
RefSeqYP_001715228.1. NC_010410.1.

3D structure databases

ProteinModelPortalB0VE45.
SMRB0VE45. Positions 1-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509173.ABAYE3470.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM88259; CAM88259; ABAYE3470.
GeneID6002533.
KEGGaby:ABAYE3470.
PATRIC20730070. VBIAciBau69881_3327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycABAU509173:GJXF-3349-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.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 1 hit.
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_ACIBY
AccessionPrimary (citable) accession number: B0VE45
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 49 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