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Protein
Submitted name:

Beta-hydroxyacyl-ACP dehydratase

Gene

fabZ

Organism
Plasmodium falciparum
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-hydroxyacyl-ACP dehydrataseImported
Submitted name:
Fatty acid synthesis proteinImported
Gene namesi
Name:fabZImported
OrganismiPlasmodium falciparumImported
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 230212Sequence analysisPRO_5005942462Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5833.PF13_0128.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6BX-ray2.09A/B/C/D/E/F81-230[»]
1ZHGX-ray2.40A/B91-229[»]
2OKHX-ray3.00A/B94-229[»]
2OKIX-ray2.70A/B94-229[»]
3AZ8X-ray3.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
3AZ9X-ray2.75A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
3AZAX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
3AZBX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
SMRiQ965D7. Positions 84-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 221126FabAInterPro annotationAdd
BLAST

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG410IF9K. Eukaryota.
COG0764. LUCA.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00406. FabZ.
InterProiIPR013114. FabA_FabZ.
IPR010084. FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamiPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR01750. fabZ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q965D7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFLIIHIAV IVLPFVLMID VKRENSFFLR HSPKRLYKKA DYNNMYDKII
60 70 80 90 100
KKQQNRIYDV SSQINQDNIN GQNISFNLTF PNYDTSIDIE DIKKILPHRY
110 120 130 140 150
PFLLVDKVIY MQPNKTIIGL KQVSTNEPFF NGHFPQKQIM PGVLQIEALA
160 170 180 190 200
QLAGILCLKS DDSQKNNLFL FAGVDGVRWK KPVLPGDTLT MQANLISFKS
210 220 230
SLGIAKLSGV GYVNGKVVIN ISEMTFALSK
Length:230
Mass (Da):26,211
Last modified:December 1, 2001 - v1
Checksum:i7DE16234AA981623
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237572 mRNA. Translation: AAK83685.1.
AY118082 Genomic DNA. Translation: AAM75408.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237572 mRNA. Translation: AAK83685.1.
AY118082 Genomic DNA. Translation: AAM75408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6BX-ray2.09A/B/C/D/E/F81-230[»]
1ZHGX-ray2.40A/B91-229[»]
2OKHX-ray3.00A/B94-229[»]
2OKIX-ray2.70A/B94-229[»]
3AZ8X-ray3.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
3AZ9X-ray2.75A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
3AZAX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
3AZBX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X81-230[»]
SMRiQ965D7. Positions 84-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5833.PF13_0128.

Chemistry

ChEMBLiCHEMBL4512.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IF9K. Eukaryota.
COG0764. LUCA.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00406. FabZ.
InterProiIPR013114. FabA_FabZ.
IPR010084. FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamiPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR01750. fabZ. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A Type II Fatty Acid Synthase in the Apicoplast of Plasmodium falciparum."
    Waller R.F., Ralph S.A., Reed M.B., Su V., Proietto C.E., Foth B.J., Besra G.S., Douglas J.D., Minnikin D.E., Roos D.S., Cowman A.F., McFadden G.I.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Identification, characterization, and inhibition of Plasmodium falciparum beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ)."
    Sharma S.K., Kapoor M., Ramya T.N., Kumar S., Kumar G., Modak R., Sharma S., Surolia N., Surolia A.
    J. Biol. Chem. 278:45661-45671(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The crystal structure of PfFabZ, the unique beta-hydroxyacyl-ACP dehydratase involved in fatty acid biosynthesis of Plasmodium falciparum."
    Kostrewa D., Winkler F.K., Folkers G., Scapozza L., Perozzo R.
    Protein Sci. 14:1570-1580(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 81-230.
  4. "Crystal structure of dimeric FabZ of Plasmodium falciparum reveals conformational switching to active hexamers by peptide flips."
    Swarnamukhi P.L., Sharma S.K., Bajaj P., Surolia N., Surolia A., Suguna K.
    FEBS Lett. 580:2653-2660(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 91-229.
  5. "Packing and loop-structure variations in non-isomorphous crystals of FabZ from Plasmodium falciparum."
    Swarnamukhi P.L., Sharma S.K., Padala P., Surolia N., Surolia A., Suguna K.
    Acta Crystallogr. D 63:458-464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 94-229.
  6. "Structural basis for the functional and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Plasmodium falciparum."
    Maity K., Venkata B.S., Kapoor N., Surolia N., Surolia A., Suguna K.
    J. Struct. Biol. 176:238-249(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 81-230.

Entry informationi

Entry nameiQ965D7_PLAFA
AccessioniPrimary (citable) accession number: Q965D7
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: April 13, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.