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P32771 (FADH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 123. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-(hydroxymethyl)glutathione dehydrogenase
EC=1.1.1.284
Alternative name(s):
Alcohol dehydrogenase SFA
EC=1.1.1.1
Glutathione-dependent formaldehyde dehydrogenase
Short name=FALDH
Short name=FDH
Short name=FLD
Short name=GSH-FDH
EC=1.1.1.-
Gene names
Name:SFA1
Synonyms:SFA
Ordered Locus Names:YDL168W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde.

Catalytic activity

S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Induction

By formaldehyde, ethanol and methyl methanesulphonate.

Miscellaneous

Requires GSH for oxidation of formaldehyde or of methylglyoxal, while oxidation of long-chain alcohols is independent of GSH and enzyme activity improves with chain length.

Present with 8370 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386S-(hydroxymethyl)glutathione dehydrogenase
PRO_0000160785

Sites

Metal binding491Zinc 1; catalytic By similarity
Metal binding711Zinc 1; catalytic By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1151Zinc 2 By similarity
Metal binding1791Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P32771 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: A495AFD7B47E4B11

FASTA38641,042
        10         20         30         40         50         60 
MSAATVGKPI KCIAAVAYDA KKPLSVEEIT VDAPKAHEVR IKIEYTAVCH TDAYTLSGSD 

        70         80         90        100        110        120 
PEGLFPCVLG HEGAGIVESV GDDVITVKPG DHVIALYTAE CGKCKFCTSG KTNLCGAVRA 

       130        140        150        160        170        180 
TQGKGVMPDG TTRFHNAKGE DIYHFMGCST FSEYTVVADV SVVAIDPKAP LDAACLLGCG 

       190        200        210        220        230        240 
VTTGFGAALK TANVQKGDTV AVFGCGTVGL SVIQGAKLRG ASKIIAIDIN NKKKQYCSQF 

       250        260        270        280        290        300 
GATDFVNPKE DLAKDQTIVE KLIEMTDGGL DFTFDCTGNT KIMRDALEAC HKGWGQSIII 

       310        320        330        340        350        360 
GVAAAGEEIS TRPFQLVTGR VWKGSAFGGI KGRSEMGGLI KDYQKGALKV EEFITHRRPF 

       370        380 
KEINQAFEDL HNGDCLRTVL KSDEIK

« Hide

References

« Hide 'large scale' references
[1]"Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its protein product."
Wehner E.P., Rao E., Brendel M.
Mol. Gen. Genet. 237:351-358(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38626 / AH22 / NRRL Y-12843.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X68020 Genomic DNA. Translation: CAA48161.1.
Z67750 Genomic DNA. Translation: CAA91578.1.
Z74216 Genomic DNA. Translation: CAA98742.1.
BK006938 Genomic DNA. Translation: DAA11693.1.
PIRS31140.
RefSeqNP_010113.1. NM_001180228.1.

3D structure databases

ProteinModelPortalP32771.
SMRP32771. Positions 10-381.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5366N.
IntActP32771. 2 interactions.
MINTMINT-539686.
STRING4932.YDL168W.

Proteomic databases

PaxDbP32771.
PeptideAtlasP32771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL168W; YDL168W; YDL168W.
GeneID851386.
KEGGsce:YDL168W.

Organism-specific databases

CYGDYDL168w.
SGDS000002327. SFA1.

Phylogenomic databases

eggNOGCOG1062.
GeneTreeENSGT00430000030800.
HOGENOMHOG000294674.
KOK00121.
OMASVESIPK.
OrthoDBEOG4HX88P.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11840.

Gene expression databases

GenevestigatorP32771.
GermOnlineYDL168W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 2 hits.
TIGRFAMsTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968534.

Entry information

Entry nameFADH_YEAST
AccessionPrimary (citable) accession number: P32771
Secondary accession number(s): D6VRI3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 3, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome IV

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents