Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q08A39 (FADB_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. 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
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:Sfri_0013
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella ›

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities 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_1000069575

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

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
Binding site6601Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08A39 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 28434AB7ABC1166C

FASTA71676,897
        10         20         30         40         50         60 
MIYQSPTIQV ELLEDNIAKL CFNAQGSVNK FDRETIASLD AALDSIKQNT NIKALLLTSA 

        70         80         90        100        110        120 
KSTFIVGADI TEFLTLFQQD DATLLAWVEQ ANAVFNKLED LPFPTASAIN GFALGGGCET 

       130        140        150        160        170        180 
ILATDLRVAD TNARIGLPET KLGLIPGFGG TVRLPRVIGA DNALEWITTA KDQRPEDALK 

       190        200        210        220        230        240 
VGAIDAVVAP ENLEAAAIQM LHDALNGSLD WQARRTKKQS PLQLPKLEAM MSFATAKGMV 

       250        260        270        280        290        300 
FSVAGKHYPA PMAAVNVVEQ AAGLDRDGAL KVEALAFIKL AKTDVAQALI GIFLNDQFVK 

       310        320        330        340        350        360 
GKAKKAGKLA KDVNQAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALE LGLNEAAKIL 

       370        380        390        400        410        420 
TTQVARGRST PEKMAKVLNN ITPSLDYAAI KNSDIVVEAV VEHPKVKATV LAEVEGYVSE 

       430        440        450        460        470        480 
DAIIASNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEIIRGEHSS EETIATVVAY 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLAEGADF AAVDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGLDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFENKR LGQKNTKGFY AYSVDRRGKP 

       610        620        630        640        650        660 
KKDIDPTSYE LLSAEFGELK AFESDDIIAR CMIPMIIETV RCLEEGIIAS PAEGDMGLVY 

       670        680        690        700        710 
GIGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRALAANN GSYYQA

« Hide

References

[1]"Complete sequence of Shewanella frigidimarina NCIMB 400."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIMB 400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000447 Genomic DNA. Translation: ABI69876.1.
RefSeqYP_748714.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ08A39.
SMRQ08A39. Positions 1-714.
ModBaseSearch...

Protein-protein interaction databases

STRING318167.Sfri_0013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI69876; ABI69876; Sfri_0013.
GeneID4277696.
KEGGsfr:Sfri_0013.
PATRIC23493733. VBISheFri14343_0013.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMANDQFVKG.
ProtClustDBPRK11730.

Enzyme and pathway databases

BioCycSFRI318167:GIXS-13-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. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_SHEFN
AccessionPrimary (citable) accession number: Q08A39
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 31, 2006
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents