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O33877 (FABA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase

EC=4.2.1.59
Alternative name(s):
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA
Beta-hydroxydecanoyl thioester dehydrase
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
EC=5.3.3.14
Gene names
Name:fabA
Ordered Locus Names:PA1610
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length By similarity. HAMAP-Rule MF_00405

Catalytic activity

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O. HAMAP-Rule MF_00405

(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H2O. HAMAP-Rule MF_00405

Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein]. HAMAP-Rule MF_00405

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_00405

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00405

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00405.

Sequence similarities

Belongs to the thioester dehydratase family. FabA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1711713-hydroxydecanoyl-[acyl-carrier-protein] dehydratase HAMAP-Rule MF_00405
PRO_0000091606

Sites

Active site701 By similarity

Secondary structure

..................... 171
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O33877 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 801E2B9C741A28FC

FASTA17118,748
        10         20         30         40         50         60 
MTKQHAFTRE DLLRCSRGEL FGPGNAQLPA PNMLMIDRIV HISDVGGKYG KGELVAELDI 

        70         80         90        100        110        120 
NPDLWFFACH FEGDPVMPGC LGLDAMWQLV GFYLGWQGNP GRGRALGSGE VKFFGQVLPT 

       130        140        150        160        170 
AKKVTYNIHI KRTINRSLVL AIADGTVSVD GREIYSAEGL RVGLFTSTDS F 

« Hide

References

« Hide 'large scale' references
[1]"Fatty acid biosynthesis in Pseudomonas aeruginosa: cloning and characterization of the fabAB operon encoding beta-hydroxyacyl-acyl carrier protein dehydratase (FabA) and beta-ketoacyl-acyl carrier protein synthase I (FabB)."
Hoang T.T., Schweizer H.P.
J. Bacteriol. 179:5326-5332(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70470 Genomic DNA. Translation: AAC45619.1.
AE004091 Genomic DNA. Translation: AAG04999.1.
PIRD83443.
RefSeqNP_250301.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B0BX-ray1.90A/B1-171[»]
4B0CX-ray2.70A/B/C/D/E1-171[»]
4B0IX-ray2.03A/B/C/D/E1-171[»]
4B0JX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-171[»]
4B8UX-ray2.76A/B/C/D/E1-171[»]
4FQ9X-ray2.02A/B/C/D/E/F/G/H/I/J1-171[»]
ProteinModelPortalO33877.
SMRO33877. Positions 2-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA1610.

Protocols and materials databases

DNASU881984.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID881984.
KEGGpae:PA1610.
PATRIC19837569. VBIPseAer58763_1670.

Organism-specific databases

PseudoCAPPA1610.

Phylogenomic databases

eggNOGCOG0764.
HOGENOMHOG000277828.
KOK01716.
OMAFQGDPVM.
OrthoDBEOG6VB6SH.
ProtClustDBPRK05174.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

HAMAPMF_00405. FabA.
InterProIPR010083. FabA.
IPR013114. FabA_FabZ.
[Graphical view]
PfamPF07977. FabA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01749. fabA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABA_PSEAE
AccessionPrimary (citable) accession number: O33877
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 93 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways