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Reviewed, UniProtKB/Swiss-Prot Q48GW3 (FADB_PSE14)

Last modified November 25, 2008. Version 29. 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

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: PSPPH_3210
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

Catalytic activity

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

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. 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.

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 – 721721Fatty acid oxidation complex subunit alpha HAMAP MF_01621
PRO_0000109280

Regions

Region1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Region312 – 7214103-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48GW3-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: C66C6B34D3EFFC89

FASTA72177,630
        10         20         30         40         50         60 
MIYEGKAITV KALESGIVEL NFDLKGESVN KFNRLTLNEL RQAVDAIKAD ASVKGVIVSS 

        70         80         90        100        110        120 
GKDVFIVGAD ITEFVDNFKL PEAELVAGNL QANRIFSDFE DLGVPTVVAI NGIALGGGLE 

       130        140        150        160        170        180 
MCLAADYRVI SSSARIGLPE VKLGLYPGFG GTVRLPRIIG ADNAIEWIAS GKESSAEDAL 

       190        200        210        220        230        240 
KVGAVDAVVA PEKLQAAALD LIQRAISGEF DYKAKRQPKL DKLKLNAIEQ MMAFETAKGF 

       250        260        270        280        290        300 
VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEIEAAGFVK MAKTSAAQSL IGLFLNDQEL 

       310        320        330        340        350        360 
KKKAKGYDAV AKDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL 

       370        380        390        400        410        420 
LGGRLEKGRL TAAKMAEALN AIRPTLSYGD FGNVDLVVEA VVENPKVKQA VLAEVEANVG 

       430        440        450        460        470        480 
EHTILASNTS TISISLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SEEAVATTVA 

       490        500        510        520        530        540 
YARKMGKNPI VVNDCPGFLV NRVLFPYFGG FARLVSAGVD FVRIDKVMEK FGWPMGPAYL 

       550        560        570        580        590        600 
MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS VVDALYEAKR LGQKNGKGFY AYETDKKGKP 

       610        620        630        640        650        660 
KKVNDPAVLD VLKPIVYEQR EVSDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLIY 

       670        680        690        700        710        720 
GIGFPPFRGG ALRYIDSIGV AEFVALADQY AELGALYQPT AKLREMASKG QSFFGQASSE 


E 

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References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed: 16159782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000058 Genomic DNA. Translation: AAZ34330.1.
RefSeqYP_275370.1.

3D structure databases

SMRQ48GW3. Positions 1-715.
ModBaseSearch...

Genome annotation databases

GeneID3556880.
GenomeReviewsGene locus PSPPH_3210 in contig CP000058_GR.
KEGGpsp:PSPPH_3210.
NMPDRfig|264730.3.peg.3186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ48GW3.

Family and domain databases

HAMAPMF_01621.
[Tree]
InterProIPR006180. 3-OHacyl-CoA_DHase_CS.
IPR006176. 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108. 3HC_DHase_C.
IPR001753. Crotonase_core.
IPR013328. DHase_multihelical.
IPR012799. FadB.
IPR016040. NAD(P)-bd.
[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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_PSE14
AccessionPrimary (citable) accession number: Q48GW3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 13, 2005
Last modified: November 25, 2008
This is version 29 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)

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