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Reviewed, UniProtKB/Swiss-Prot Q9HZJ2 (FADB_PSEAE)

Last modified February 9, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
              EC=4.2.1.17
              EC=5.3.3.8
              EC=5.1.2.3
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35
Gene names
Name: fadB
Ordered Locus Names: PA3014
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length715 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity. HAMAP MF_01621

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01621

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01621

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 715715Fatty acid oxidation complex subunit alpha HAMAP MF_01621
PRO_0000109274

Regions

Nucleotide binding401 – 4033NAD By similarity
Nucleotide binding428 – 4303NAD By similarity
Region1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Region312 – 7154043-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Binding site2971Substrate 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 site6601Substrate By similarity
Site1201Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9HZJ2-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 7ED8573BE8F31101

FASTA71576,954
        10         20         30         40         50         60 
MIYQGKAITV KPLEGGIVEL NFDLKGESVN KFNRLTLSEL RAAVDAIKAD ASVKGVIVTS 

        70         80         90        100        110        120 
GKDVFIVGAD ITEFVDNFQL PDEELMAGNL EANKIFSDFE DLDVPTVAAI NGIALGGGLE 

       130        140        150        160        170        180 
MCLAADFRVM SATAKVGLPE VKLGIYPGFG GTVRLPRLIG CDNAVEWIAS GKENKAEDAL 

       190        200        210        220        230        240 
KVGAVDAVVA PEQLQAAALD LAKRAVAGEL DHKARRQPKL EKLKLNAIEQ MMAFETAKGF 

       250        260        270        280        290        300 
VAGQAGPNYP APVEAIKSIQ KAANFGRDKA LEVEAAGFVK LAKTSVAQSL IGLFLNDQEL 

       310        320        330        340        350        360 
KKKAKKYDEV AKDVKLAAVL GAGIMGGGIA YQSALKGTPI LMKDIREEGI QMGLNEAAKL 

       370        380        390        400        410        420 
LGKRVEKGRL TPAKMAEALN GIRPTMSYGD FGNVDIVVEA VVENPKVKQA VLAEVEGAVK 

       430        440        450        460        470        480 
EDAIIASNTS TISISLLAQA LKRPENFCGM HFFNPVHMMP LVEVIRGEKT GETAIATTVA 

       490        500        510        520        530        540 
YAKKMGKSPI VVNDCPGFLV NRVLFPYFGG FAKLLSFGVD FVRIDKVMEK FGWPMGPAYL 

       550        560        570        580        590        600 
SDVVGIDTGH HGRDVMAEGF PDRMAVEGKT AVDVMYEANR LGQKNGKGFY AYETDKRGKP 

       610        620        630        640        650        660 
KKVTDPQAYE VLKPIVVEQR EVTDEDIVNF MMIPLCLETV RCLEDGIVET AAEADMGLIY 

       670        680        690        700        710 
GIGFPPFRGG ALRYIDSIGV AEFVALADKY AELGALYHPT AKLREMAKNG QKFFG

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004091 Genomic DNA. Translation: AAG06402.1.
PIRG83269.
RefSeqNP_251704.1.

3D structure databases

SMRQ9HZJ2. Positions 1-715.
ModBaseSearch...

Genome annotation databases

GeneID878680.
GenomeReviewsGene locus PA3014 in contig AE004091_GR.
KEGGpae:PA3014.

Organism-specific databases

PseudoCAPPA3014.
CMRSearch...

Phylogenomic databases

HOGENOMHBG691737.
OMAASRFGQK.

Enzyme and pathway databases

BioCycPAER208964:PA3014-MONOMER.
BRENDA1.1.1.35. 354.
4.2.1.17. 354.
5.1.2.3. 354.
5.3.3.8. 354.

Family and domain databases

HAMAPMF_01621. FadB.
[Tree]
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.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFADB_PSEAE
AccessionPrimary (citable) accession number: Q9HZJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents