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Q5QXH7 (FADB_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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:IL0011
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length718 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 – 718718Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109271

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 188188Enoyl-CoA hydratase/isomerase By similarity
Region310 – 7184093-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2951Substrate 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 site6581Substrate By similarity
Site1181Important for catalytic activity By similarity
Site1381Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QXH7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: A870D2CA91816281

FASTA71877,268
        10         20         30         40         50         60 
MIYQGESIRV DFIEPGFAEL QFDAKGSVNK FDQATLEEFS EALTKLQNTD DLRGVIVTSS 

        70         80         90        100        110        120 
KSTFIVGADI TEFLTLFSDQ EKTRSWVAKA SRVFDQLEDL PVPTVGAVTG FALGGGCEAL 

       130        140        150        160        170        180 
LACDYRVADT TATIGLPEVK LGLIPGFGGT MRLPRVIGPD NALEWITTGK NNKALDALKV 

       190        200        210        220        230        240 
GAVDAVVEPE NLTKAALNLA KAAAAGQQDW KAKRQPKLEP LKANDTELMM TLVTAKGMIA 

       250        260        270        280        290        300 
AKAGKHYPAP HKALEAIENG AREHREGALT AENNAFFDLT QTEACQAQVG IFLADQAVKG 

       310        320        330        340        350        360 
KSKKYAKAAT KEIKTAGVLG AGIMGGGIAY QSALKGVPAV MKDIKQDALD LGMKEAGKIL 

       370        380        390        400        410        420 
KKGVERGKVN NEKMIKILSS ITPTLLNDAV KDVDIVVEAV VENPKVKGSV LAEIEGVIGD 

       430        440        450        460        470        480 
DAILTSNTST ISITELAKNL KRPEKFCGMH FFNPVHKMPL VEIIRGEKTS DDTVNAVVAY 

       490        500        510        520        530        540 
ALKLGKTPIV VNDCPGFLVN RVLFPYLAGF AGMVDEGVDF VGIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
SDVVGIDTAD HCTVVMEAGF PTRMKRDESS AIAKLAAAER YGQKNGKGFY VYGTDKKGKP 

       610        620        630        640        650        660 
TKEADPATYE LLGCEQGKKL DADEVIARCM IPMVNEVVRC LEEDIVGSAA EADMALLYGL 

       670        680        690        700        710 
GFPPFRGGPF RYLETLGMDN FIQLADKYAH LGEIYQVTDG MREMAKAGKS YFDTTSAK 

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References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV80855.1.
RefSeqYP_154404.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXH7.
SMRQ5QXH7. Positions 1-712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV80855; AAV80855; IL0011.
GeneID3173765.
KEGGilo:IL0011.
PATRIC22138027. VBIIdiLoi21852_0011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycILOI283942:GI0U-11-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. 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.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_IDILO
AccessionPrimary (citable) accession number: Q5QXH7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 74 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