Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1KCZ3 (FADB_SHEWM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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:Swoo_0021
OrganismShewanella woodyi (strain ATCC 51908 / MS32) [Complete proteome] [HAMAP]
Taxonomic identifier392500 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length716 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 – 716716Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_1000186055

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7164063-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2961Substrate By similarity
Binding site3241NAD; via amide nitrogen By similarity
Binding site3431NAD By similarity
Binding site4071NAD By similarity
Binding site4531NAD By similarity
Binding site5001Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B1KCZ3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 1338DB146E80536A

FASTA71676,934
        10         20         30         40         50         60 
MIYQSPTIQV ELLEDNIARL CFNAAGSVNK LDRETIDSLN AALDAIKQDT NIQGLVLTSG 

        70         80         90        100        110        120 
KGAFIVGADI TEFLGLFAQE ESVLLPWIAE ANVVFNKIED LPFPTISAIN GFALGGGFET 

       130        140        150        160        170        180 
VLATDFRIAD TTAKLGLPET KLGLIPGFGG TVRLPRLIGA DNALEWITTG KDHKPEAALK 

       190        200        210        220        230        240 
VGAIDAVVAP ENLEASAIAM LKEALSEKLD WQARRAKKQA PLNLPKLEAM MSFATAKGMV 

       250        260        270        280        290        300 
FKVAGKHYPA PMTAISVIEQ AARSERADAL MVEHQAFIKL AKTDVAQALI GIFLNDQLVK 

       310        320        330        340        350        360 
GKAKKAGKLA KNVDSAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD LGLGEASKLL 

       370        380        390        400        410        420 
AAQIKRGRST PEKMAKVLNN ITATLDYAPV KDVDVVVEAV VEHPKVKSMV LAEVEQNVSD 

       430        440        450        460        470        480 
DAIITSNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEVIRGENSS EETIASVVAY 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLADGADF AAIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTGH HAQAVMAEGF PDRMGKDGKD AIDIMFDSER FGQKNNKGFY AYSVDRRGKP 

       610        620        630        640        650        660 
KKDLDPTSYE LLGAEFGDLK AFESDEIIAR TMIPMIIETV RCLEEGIIAT PAEADMGLVF 

       670        680        690        700        710 
GLGFPPFRGG VFRYIDTMGV ANFVALADKY AHLGGLYQVT DAMRELAANN GSYYQA 

« Hide

References

[1]"Complete sequence of Shewanella woodyi ATCC 51908."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51908 / MS32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000961 Genomic DNA. Translation: ACA84322.1.
RefSeqYP_001758417.1. NC_010506.1.

3D structure databases

ProteinModelPortalB1KCZ3.
SMRB1KCZ3. Positions 1-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING392500.Swoo_0021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA84322; ACA84322; Swoo_0021.
GeneID6114238.
KEGGswd:Swoo_0021.
PATRIC23602221. VBISheWoo126588_0021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMANPIVVND.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycSWOO392500:GI2C-21-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 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.
IPR029045. ClpP/crotonase-like_dom.
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.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_SHEWM
AccessionPrimary (citable) accession number: B1KCZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: June 11, 2014
This is version 52 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