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Q4FQC6 (FADB_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. 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:Psyc_1934
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length719 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 – 719719Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109283

Regions

Nucleotide binding402 – 4043NAD By similarity
Nucleotide binding429 – 4313NAD By similarity
Region1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Region313 – 7194073-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
Q4FQC6 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 67B55A992065C896

FASTA71978,225
        10         20         30         40         50         60 
MVYQGNRITV TMLEDGIANM QYNAENESVN KFDTETNKQF AEVVNALEKA DDVKGLIVTS 

        70         80         90        100        110        120 
SKGVFIAGAD ITEFVASFKQ SEEEIKDWVI NINDAFNRFE DLPFPKVAAI NGAALGGGCE 

       130        140        150        160        170        180 
MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG GTVRSTRVIG IDNALELIAT GAPKKALDAL 

       190        200        210        220        230        240 
KLGLVDATVA ADDLQDAAID LVKKCISGEL DWKAKREEKL VAVKLNQLEQ AMAFNSAKGM 

       250        260        270        280        290        300 
IFAKANPKQY PAPALAIAAI EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL 

       310        320        330        340        350        360 
VKKLAKQHSK KAHEINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ LDLGMGEASK 

       370        380        390        400        410        420 
LLGKMVDRGK MTPAKMGETL SRIRPTLNYG DFAETDIVIE AVVENPNVKR AVLKEVEGLV 

       430        440        450        460        470        480 
KDDCILASNT STISITFLAE ALERPENFVG MHFFNPVHRM PLVEVIRGEK SSEEAIATTV 

       490        500        510        520        530        540 
ALASKMGKVP VVVNDCPGFL VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY 

       550        560        570        580        590        600 
LIDVVGLDTG VHGAEVMAEG FPDRMKPDYK GAIELLYENK RLGQKNGVGF YKYEMDKRGK 

       610        620        630        640        650        660 
PKKVADEATY ELLKTTTDSE KQTFDDQAII DRTMLAFCNE TVRCLEDNIV STPSEADMAM 

       670        680        690        700        710 
IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAHLGKAYE APQKIRDMAA AGETFYATA 

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References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ19782.1.
RefSeqYP_265216.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FQC6.
SMRQ4FQC6. Positions 1-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_1934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ19782; AAZ19782; Psyc_1934.
GeneID3515904.
KEGGpar:Psyc_1934.
PATRIC23058763. VBIPsyArc98534_2286.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMAAKGMVMQ.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycPARC259536:GI3A-1979-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.
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.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_PSYA2
AccessionPrimary (citable) accession number: Q4FQC6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 30, 2005
Last modified: June 11, 2014
This is version 72 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