Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 to 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

Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 14911 Publication
Active sitei156 – 15611 Publication

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydratase activity Source: SGD
  • enoyl-CoA hydratase activity Source: SGD

GO - Biological processi

  • fatty acid elongation Source: SGD
  • sphingolipid biosynthetic process Source: SGD
  • vacuolar transport Source: SGD
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:MONOMER-17327.
YEAST:G3O-31552-MONOMER.
YEAST:MONOMER3O-85.
ReactomeiREACT_308531. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

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
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

CYGDiYJL097w.
EuPathDBiFungiDB:YJL097W.
SGDiS000003633. PHS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 2918HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 4718LumenalSequence AnalysisAdd
BLAST
Transmembranei48 – 6619HelicalSequence AnalysisAdd
BLAST
Topological domaini67 – 7610CytoplasmicSequence Analysis
Transmembranei77 – 9418HelicalSequence AnalysisAdd
BLAST
Topological domaini95 – 995LumenalSequence Analysis
Transmembranei100 – 11718HelicalSequence AnalysisAdd
BLAST
Topological domaini118 – 14225CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei143 – 16018HelicalSequence AnalysisAdd
BLAST
Topological domaini161 – 17818LumenalSequence AnalysisAdd
BLAST
Transmembranei179 – 19618HelicalSequence AnalysisAdd
BLAST
Topological domaini197 – 21721CytoplasmicSequence AnalysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491Y → A: No catalytic activity. 1 Publication
Mutagenesisi156 – 1561E → A: No catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1PRO_0000203047Add
BLAST

Proteomic databases

PaxDbiP40857.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP40857.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi214 – 2174Endoplasmic reticulum retention signal

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5198.
GeneTreeiENSGT00530000062962.
HOGENOMiHOG000190538.
InParanoidiP40857.
KOiK10703.
OMAiRRKVMRS.
OrthoDBiEOG7NKKXC.

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 interactions.
DIPiDIP-2104N.
IntActiP40857. 31 interactions.
MINTiMINT-534987.

Proteomic databases

PaxDbiP40857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYJL097w.
EuPathDBiFungiDB:YJL097W.
SGDiS000003633. PHS1.

Phylogenomic databases

eggNOGiCOG5198.
GeneTreeiENSGT00530000062962.
HOGENOMiHOG000190538.
InParanoidiP40857.
KOiK10703.
OMAiRRKVMRS.
OrthoDBiEOG7NKKXC.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:MONOMER-17327.
YEAST:G3O-31552-MONOMER.
YEAST:MONOMER3O-85.
ReactomeiREACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi973747.
PROiP40857.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and function analysis of a 9.74 kb fragment of Saccharomyces cerevisiae chromosome X including the BCK1 gene."
    Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S., Zimmermann F.K.
    Yeast 10:1481-1488(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  7. "A molecular caliper mechanism for determining very long-chain fatty acid length."
    Denic V., Weissman J.S.
    Cell 130:663-677(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  8. "Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation."
    Kihara A., Sakuraba H., Ikeda M., Denpoh A., Igarashi Y.
    J. Biol. Chem. 283:11199-11209(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TYR-149 AND GLU-156, ACTIVE SITE, CATALYTIC ACTIVITY, PATHWAY.

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: July 22, 2015
This is version 112 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

External Data

Dasty 3

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 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.