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Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1

Gene

PHS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.2 Publications

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.2 Publications

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1491 Publication1
Active sitei1561 Publication1

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydratase activity Source: SGD
  • 3-hydroxy-behenoyl-CoA dehydratase activity Source: UniProtKB-EC
  • 3-hydroxy-lignoceroyl-CoA dehydratase activity Source: UniProtKB-EC
  • enoyl-CoA hydratase activity Source: SGD

GO - Biological processi

  • fatty acid elongation Source: SGD
  • sphingolipid biosynthetic process Source: SGD
  • vacuolar transport Source: SGD
  • very long-chain fatty acid biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-85.
YEAST:MONOMER3O-85.
ReactomeiR-SCE-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000492.

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1Curated (EC:4.2.1.1342 Publications)
Alternative name(s):
3-hydroxyacyl-CoA dehydratase PHS1
Short name:
HACD
PTPLA homolog involved in sphingolipid biosynthesis protein 1
Gene namesi
Name:PHS1
Ordered Locus Names:YJL097W
ORF Names:J0902
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL097W.
SGDiS000003633. PHS1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 29HelicalSequence analysisAdd BLAST18
Topological domaini30 – 47LumenalSequence analysisAdd BLAST18
Transmembranei48 – 66HelicalSequence analysisAdd BLAST19
Topological domaini67 – 76CytoplasmicSequence analysis10
Transmembranei77 – 94HelicalSequence analysisAdd BLAST18
Topological domaini95 – 99LumenalSequence analysis5
Transmembranei100 – 117HelicalSequence analysisAdd BLAST18
Topological domaini118 – 142CytoplasmicSequence analysisAdd BLAST25
Transmembranei143 – 160HelicalSequence analysisAdd BLAST18
Topological domaini161 – 178LumenalSequence analysisAdd BLAST18
Transmembranei179 – 196HelicalSequence analysisAdd BLAST18
Topological domaini197 – 217CytoplasmicSequence analysisAdd BLAST21

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • integral component of endoplasmic reticulum membrane Source: SGD
  • vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi149Y → A: No catalytic activity. 1 Publication1
Mutagenesisi156E → A: No catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002030471 – 217Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1Add BLAST217

Proteomic databases

PRIDEiP40857.
TopDownProteomicsiP40857.

Interactioni

Protein-protein interaction databases

BioGridi33660. 27 interactors.
DIPiDIP-2104N.
IntActiP40857. 31 interactors.
MINTiMINT-534987.

Structurei

3D structure databases

ProteinModelPortaliP40857.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi214 – 217Endoplasmic reticulum retention signal4

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000062962.
HOGENOMiHOG000190538.
InParanoidiP40857.
KOiK10703.
OMAiCLSWSIT.
OrthoDBiEOG092C4NVA.

Family and domain databases

InterProiIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40857-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKLASPLS FLPLYNLLSA VGWSYLLYLV ISLYPKVGQP AFFYQTKNVA
60 70 80 90 100
TLVQCGAIIE IINSFLGVVR SPLLTTVAQV SSRLLVVLGI FQLLPNTSGV
110 120 130 140 150
QSVVYISLLL AWSITEIVRY LYYFFMLVFK NGAPKILILL RYNLFWILYP
160 170 180 190 200
TGVASELRII YCALNAAESQ YSLLYKRILI AAMLAYIPGF PMLFLHMVAQ
210
RKKVMKSLRS SFGKKLI
Length:217
Mass (Da):24,511
Last modified:February 1, 1995 - v1
Checksum:i5C87BC9563FB83AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77923 Genomic DNA. Translation: CAA54893.1.
Z49372 Genomic DNA. Translation: CAA89391.1.
AY557855 Genomic DNA. Translation: AAS56181.1.
BK006943 Genomic DNA. Translation: DAA08703.1.
PIRiS50296.
RefSeqiNP_012438.1. NM_001181530.1.

Genome annotation databases

EnsemblFungiiYJL097W; YJL097W; YJL097W.
GeneIDi853348.
KEGGisce:YJL097W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77923 Genomic DNA. Translation: CAA54893.1.
Z49372 Genomic DNA. Translation: CAA89391.1.
AY557855 Genomic DNA. Translation: AAS56181.1.
BK006943 Genomic DNA. Translation: DAA08703.1.
PIRiS50296.
RefSeqiNP_012438.1. NM_001181530.1.

3D structure databases

ProteinModelPortaliP40857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33660. 27 interactors.
DIPiDIP-2104N.
IntActiP40857. 31 interactors.
MINTiMINT-534987.

Chemistry databases

SwissLipidsiSLP:000000492.

Proteomic databases

PRIDEiP40857.
TopDownProteomicsiP40857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL097W; YJL097W; YJL097W.
GeneIDi853348.
KEGGisce:YJL097W.

Organism-specific databases

EuPathDBiFungiDB:YJL097W.
SGDiS000003633. PHS1.

Phylogenomic databases

GeneTreeiENSGT00530000062962.
HOGENOMiHOG000190538.
InParanoidiP40857.
KOiK10703.
OMAiCLSWSIT.
OrthoDBiEOG092C4NVA.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:MONOMER3O-85.
YEAST:MONOMER3O-85.
ReactomeiR-SCE-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiP40857.

Family and domain databases

InterProiIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHACD_YEAST
AccessioniPrimary (citable) accession number: P40857
Secondary accession number(s): D6VW87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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.