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Protein

Fatty aldehyde dehydrogenase HFD1

Gene

HFD1

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 oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid.1 Publication

Catalytic activityi

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei236 – 2361PROSITE-ProRule annotation
Active sitei273 – 2731PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2196NADSequence Analysis

GO - Molecular functioni

  1. 3-chloroallyl aldehyde dehydrogenase activity Source: SGD
  2. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC
  3. aldehyde dehydrogenase [NAD(P)+] activity Source: InterPro
  4. carboxylate reductase activity Source: SGD

GO - Biological processi

  1. aldehyde catabolic process Source: SGD
  2. cellular aldehyde metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciYEAST:G3O-32806-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty aldehyde dehydrogenase HFD1 (EC:1.2.1.3)
Gene namesi
Name:HFD1
Ordered Locus Names:YMR110C
ORF Names:YM9718.09C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR110c.
EuPathDBiFungiDB:YMR110C.
SGDiS000004716. HFD1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei134 – 15219HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endosome membrane Source: UniProtKB-SubCell
  2. integral component of mitochondrial outer membrane Source: SGD
  3. lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 532532Fatty aldehyde dehydrogenase HFD1PRO_0000056597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04458.
PaxDbiQ04458.
PeptideAtlasiQ04458.
PRIDEiQ04458.

Expressioni

Gene expression databases

GenevestigatoriQ04458.

Interactioni

Protein-protein interaction databases

BioGridi35286. 33 interactions.
DIPiDIP-4437N.
IntActiQ04458. 8 interactions.
MINTiMINT-570953.
STRINGi4932.YMR110C.

Structurei

3D structure databases

SMRiQ04458. Positions 15-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00390000002825.
HOGENOMiHOG000271515.
InParanoidiQ04458.
KOiK00128.
OMAiPEKPPFN.
OrthoDBiEOG7SFJ6D.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNDGSKILN YTPVSKIDEI VEISRNFFFE KQLKLSHENN PRKKDLEFRQ
60 70 80 90 100
LQLKKLYYAV KDHEEELIDA MYKDFHRNKI ESVLNETTKL MNDILHLIEI
110 120 130 140 150
LPKLIKPRRV SDSSPPFMFG KTIVEKISRG SVLIIAPFNF PLLLAFAPLA
160 170 180 190 200
AALAAGNTIV LKPSELTPHT AVVMENLLTT AGFPDGLIQV VQGAIDETTR
210 220 230 240 250
LLDCGKFDLI FYTGSPRVGS IVAEKAAKSL TPCVLELGGK SPTFITENFK
260 270 280 290 300
ASNIKIALKR IFFGAFGNSG QICVSPDYLL VHKSIYPKVI KECESVLNEF
310 320 330 340 350
YPSFDEQTDF TRMIHEPAYK KAVASINSTN GSKIVPSKIS INSDTEDLCL
360 370 380 390 400
VPPTIVYNIG WDDPLMKQEN FAPVLPIIEY EDLDETINKI IEEHDTPLVQ
410 420 430 440 450
YIFSDSQTEI NRILTRLRSG DCVVGDTVIH VGITDAPFGG IGTSGYGNYG
460 470 480 490 500
GYYGFNTFSH ERTIFKQPYW NDFTLFMRYP PNSAQKEKLV RFAMERKPWF
510 520 530
DRNGNNKWGL RQYFSLSAAV ILISTIYAHC SS
Length:532
Mass (Da):59,979
Last modified:November 1, 1997 - v1
Checksum:i6CAF4BFCF963AF88
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49702 Genomic DNA. Translation: CAA89746.1.
BK006946 Genomic DNA. Translation: DAA10007.1.
PIRiS54571.
RefSeqiNP_013828.1. NM_001182610.1.

Genome annotation databases

EnsemblFungiiYMR110C; YMR110C; YMR110C.
GeneIDi855137.
KEGGisce:YMR110C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49702 Genomic DNA. Translation: CAA89746.1.
BK006946 Genomic DNA. Translation: DAA10007.1.
PIRiS54571.
RefSeqiNP_013828.1. NM_001182610.1.

3D structure databases

SMRiQ04458. Positions 15-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35286. 33 interactions.
DIPiDIP-4437N.
IntActiQ04458. 8 interactions.
MINTiMINT-570953.
STRINGi4932.YMR110C.

Proteomic databases

MaxQBiQ04458.
PaxDbiQ04458.
PeptideAtlasiQ04458.
PRIDEiQ04458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR110C; YMR110C; YMR110C.
GeneIDi855137.
KEGGisce:YMR110C.

Organism-specific databases

CYGDiYMR110c.
EuPathDBiFungiDB:YMR110C.
SGDiS000004716. HFD1.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00390000002825.
HOGENOMiHOG000271515.
InParanoidiQ04458.
KOiK00128.
OMAiPEKPPFN.
OrthoDBiEOG7SFJ6D.

Enzyme and pathway databases

BioCyciYEAST:G3O-32806-MONOMER.

Miscellaneous databases

NextBioi978519.
PROiQ04458.

Gene expression databases

GenevestigatoriQ04458.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  6. "Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae."
    Burri L., Vascotto K., Gentle I.E., Chan N.C., Beilharz T., Stapleton D.I., Ramage L., Lithgow T.
    FEBS J. 273:1507-1515(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
    Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
    Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway."
    Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., Ohno Y., Zoeller R.A., Kihara A.
    Mol. Cell 46:461-471(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHFD1_YEAST
AccessioniPrimary (citable) accession number: Q04458
Secondary accession number(s): D6VZT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2930 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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