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P39954 (SAHH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosylhomocysteinase

Short name=AdoHcyase
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Gene names
Name:SAH1
Ordered Locus Names:YER043C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine By similarity. HAMAP-Rule MF_00563

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP-Rule MF_00563

Cofactor

Binds 1 NAD per subunit.

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. HAMAP-Rule MF_00563

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAF16P435693EBI-16451,EBI-22808

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 449448Adenosylhomocysteinase HAMAP-Rule MF_00563
PRO_0000116937

Regions

Nucleotide binding160 – 1623NAD By similarity
Nucleotide binding223 – 2286NAD By similarity
Nucleotide binding302 – 3043NAD By similarity

Sites

Binding site581Substrate By similarity
Binding site1341Substrate By similarity
Binding site1591Substrate By similarity
Binding site1891Substrate By similarity
Binding site1931Substrate By similarity
Binding site1941NAD By similarity
Binding site2461NAD By similarity
Binding site3491NAD By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue3931Phosphothreonine Ref.4 Ref.5 Ref.6 Ref.7

Sequences

Sequence LengthMass (Da)Tools
P39954 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: D98D9DD329374F5B

FASTA44949,126
        10         20         30         40         50         60 
MSAPAQNYKI ADISLAAFGR KEIELAEHEM PGLMAIRKAY GDVQPLKGAR IAGCLHMTIQ 

        70         80         90        100        110        120 
TAVLIETLVA LGAEVTWSSC NIYSTQDHAA AAIAASGVPV FAWKGETEEE YLWCIEQQLF 

       130        140        150        160        170        180 
AFKDNKKLNL ILDDGGDLTT LVHEKHPEML EDCFGLSEET TTGVHHLYRM VKEGKLKVPA 

       190        200        210        220        230        240 
INVNDSVTKS KFDNLYGCRE SLVDGIKRAT DVMLAGKVAV VAGYGDVGKG CAAALRGMGA 

       250        260        270        280        290        300 
RVLVTEIDPI NALQAAMEGY QVVTMEDASH IGQVFVTTTG CRDIINGEHF INMPEDAIVC 

       310        320        330        340        350        360 
NIGHFDIEID VAWLKANAKE CINIKPQVDR YLLSSGRHVI LLANGRLVNL GCATGHSSFV 

       370        380        390        400        410        420 
MSCSFSNQVL AQIALFKSND KSFREKHIEF QKTGPFEVGV HVLPKILDEA VAKFHLGNLG 

       430        440 
VRLTKLSKVQ SEYLGIPEEG PFKADHYRY 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(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]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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 THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[5]"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 THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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 THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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 THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18796 Genomic DNA. Translation: AAB64578.1.
AY692801 Genomic DNA. Translation: AAT92820.1.
BK006939 Genomic DNA. Translation: DAA07697.1.
PIRS50546.
RefSeqNP_010961.3. NM_001178934.3.

3D structure databases

ProteinModelPortalP39954.
SMRP39954. Positions 8-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36779. 36 interactions.
DIPDIP-5184N.
IntActP39954. 6 interactions.
MINTMINT-538156.
STRING4932.YER043C.

Proteomic databases

PaxDbP39954.
PeptideAtlasP39954.
PRIDEP39954.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER043C; YER043C; YER043C.
GeneID856766.
KEGGsce:YER043C.

Organism-specific databases

CYGDYER043c.
SGDS000000845. SAH1.

Phylogenomic databases

eggNOGCOG0499.
GeneTreeENSGT00390000003626.
HOGENOMHOG000227987.
KOK01251.
OMAEVNPIRA.
OrthoDBEOG7FZ07M.

Enzyme and pathway databases

BioCycYEAST:YER043C-MONOMER.
UniPathwayUPA00314; UER00076.

Gene expression databases

GenevestigatorP39954.

Family and domain databases

HAMAPMF_00563. AdoHcyase.
InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERPTHR23420. PTHR23420. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982947.
PROP39954.

Entry information

Entry nameSAHH_YEAST
AccessionPrimary (citable) accession number: P39954
Secondary accession number(s): D3DLU3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 19, 2014
This is version 121 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 V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways