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Q489W3 (FADB_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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:CPS_0393
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length722 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 – 722722Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109265

Regions

Nucleotide binding401 – 4033NAD By similarity
Nucleotide binding428 – 4303NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7224123-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4511For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2961Substrate By similarity
Binding site3251NAD; via amide nitrogen By similarity
Binding site3441NAD By similarity
Binding site4081NAD By similarity
Binding site4541NAD By similarity
Binding site5011Substrate By similarity
Binding site6611Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q489W3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: A174E51D6CB6A318

FASTA72277,146
        10         20         30         40         50         60 
MIYQGKSLSA QLLEDGIVEF KFDAQGSVNK FDQATFEEYI AVVAAINNCS EAKGVIVTSG 

        70         80         90        100        110        120 
KSTFIVGADI TEFLVSFSQP EDALASWAKK ASDVFDSFED IQLPTIAAIN GIALGGGCEM 

       130        140        150        160        170        180 
TLACDYRVAA TTASIGLPEV KLGLMPGFGG TVRLPRLIGF DNAATWMSTG KAFKPAAALA 

       190        200        210        220        230        240 
QGAIDAVVEP ENLQAAAISM LKLAIDGKLD WRAKRQPKLE ALKLSPTELI MSSTTCKGMI 

       250        260        270        280        290        300 
AAKAGKHYPA PMVMINTLIA SANLDRTGAM AAENTGFAKL AKTDAATAQI GLFMADQVIK 

       310        320        330        340        350        360 
GKAKKASKLA TKAVNKAAVL GAGIMGGGIA YQSAYKGTPI IMKDINDQAL DLGLTTATGI 

       370        380        390        400        410        420 
LTKQVERGRM NAKKMAGVLN NITPSLSYDS VKDVDIVVEA VVENPKVKGM VLAEVEGVIG 

       430        440        450        460        470        480 
EDAILTSNTS TISIDLLAQS VKRPQNFCGM HFFNPVNKMP LVEVIRGKDT SDETVAAVVA 

       490        500        510        520        530        540 
YAAKMGKSPI VVNDCPGFYV NRVLFPYFAG FSQLVLEGAD FTAIDKVMEK QFGWPMGPAY 

       550        560        570        580        590        600 
LLDVVGVDTA DHCTGVMSSG FPTRMKKIDN DPVSTLYANE RLGQKNGKGF YDHIKDKRGR 

       610        620        630        640        650        660 
PMKVPAPVAY ELLGQHCADK KDFSSEEIIA RMMIPMVNEV VRCLEEGVVD TAAEADMGLI 

       670        680        690        700        710        720 
YGVGFPPFRG GAIRYLETLG LDNFIAMADK YTDLGEIYHV TDGLREMAKS GKSYFTTDVK 


LA 

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References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ26244.1.
RefSeqYP_267151.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ489W3.
SMRQ489W3. Positions 1-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167879.CPS_0393.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ26244; AAZ26244; CPS_0393.
GeneID3520494.
KEGGcps:CPS_0393.
PATRIC21464151. VBIColPsy94388_0340.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCPSY167879:GI48-393-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_COLP3
AccessionPrimary (citable) accession number: Q489W3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 65 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