Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04458 (HFD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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:
Fatty aldehyde dehydrogenase HFD1

EC=1.2.1.3
Gene names
Name:HFD1
Ordered Locus Names:YMR110C
ORF Names:YM9718.09C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12

Catalytic activity

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

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein Potential. Endosome membrane; Single-pass membrane protein Potential. Cytoplasmic granule membrane; Single-pass membrane protein Potential Ref.3 Ref.5 Ref.6 Ref.7.

Miscellaneous

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

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 532532Fatty aldehyde dehydrogenase HFD1
PRO_0000056597

Regions

Transmembrane134 – 15219Helical; Potential
Nucleotide binding214 – 2196NAD Potential

Sites

Active site2361 By similarity
Active site2731 By similarity

Amino acid modifications

Modified residue1111Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q04458 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 6CAF4BFCF963AF88

FASTA53259,979
        10         20         30         40         50         60 
MSNDGSKILN YTPVSKIDEI VEISRNFFFE KQLKLSHENN PRKKDLEFRQ LQLKKLYYAV 

        70         80         90        100        110        120 
KDHEEELIDA MYKDFHRNKI ESVLNETTKL MNDILHLIEI LPKLIKPRRV SDSSPPFMFG 

       130        140        150        160        170        180 
KTIVEKISRG SVLIIAPFNF PLLLAFAPLA AALAAGNTIV LKPSELTPHT AVVMENLLTT 

       190        200        210        220        230        240 
AGFPDGLIQV VQGAIDETTR LLDCGKFDLI FYTGSPRVGS IVAEKAAKSL TPCVLELGGK 

       250        260        270        280        290        300 
SPTFITENFK ASNIKIALKR IFFGAFGNSG QICVSPDYLL VHKSIYPKVI KECESVLNEF 

       310        320        330        340        350        360 
YPSFDEQTDF TRMIHEPAYK KAVASINSTN GSKIVPSKIS INSDTEDLCL VPPTIVYNIG 

       370        380        390        400        410        420 
WDDPLMKQEN FAPVLPIIEY EDLDETINKI IEEHDTPLVQ YIFSDSQTEI NRILTRLRSG 

       430        440        450        460        470        480 
DCVVGDTVIH VGITDAPFGG IGTSGYGNYG GYYGFNTFSH ERTIFKQPYW NDFTLFMRYP 

       490        500        510        520        530 
PNSAQKEKLV RFAMERKPWF DRNGNNKWGL RQYFSLSAAV ILISTIYAHC SS 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49702 Genomic DNA. Translation: CAA89746.1.
BK006946 Genomic DNA. Translation: DAA10007.1.
PIRS54571.
RefSeqNP_013828.1. NM_001182610.1.

3D structure databases

ProteinModelPortalQ04458.
SMRQ04458. Positions 15-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35286. 32 interactions.
DIPDIP-4437N.
IntActQ04458. 8 interactions.
MINTMINT-570953.
STRING4932.YMR110C.

Proteomic databases

PaxDbQ04458.
PeptideAtlasQ04458.
PRIDEQ04458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR110C; YMR110C; YMR110C.
GeneID855137.
KEGGsce:YMR110C.

Organism-specific databases

CYGDYMR110c.
SGDS000004716. HFD1.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00390000002825.
HOGENOMHOG000271515.
OMAINMANEI.
OrthoDBEOG7SFJ6D.

Enzyme and pathway databases

BioCycYEAST:G3O-32806-MONOMER.

Gene expression databases

GenevestigatorQ04458.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PANTHERPTHR11699:SF15. PTHR11699:SF15. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036492. ALDH. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978519.

Entry information

Entry nameHFD1_YEAST
AccessionPrimary (citable) accession number: Q04458
Secondary accession number(s): D6VZT3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families