Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q08985 (SAM4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Homocysteine S-methyltransferase 2
EC=2.1.1.10
Alternative name(s):
S-adenosylmethionine metabolism protein 4
S-methylmethionine:homocysteine methyltransferase 2
Short name=SMM:Hcy S-methyltransferase 2
Gene names
Name:SAM4
Ordered Locus Names:YPL273W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S-methylmethionine (SMM) to methionine. Ref.3

Catalytic activity

S-methyl-L-methionine + L-homocysteine = 2 L-methionine.

Cofactor

Zinc Potential.

Subcellular location

Cytoplasm. Nucleus Ref.4.

Induction

Up-regulated in response to high extracellular methionine. Ref.3

Miscellaneous

Present with 60300 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Contains 1 Hcy-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Homocysteine S-methyltransferase 2
PRO_0000114619

Regions

Domain6 – 321316Hcy-binding

Sites

Metal binding2391Zinc Potential
Metal binding3061Zinc Potential
Metal binding3071Zinc Potential

Amino acid modifications

Modified residue991Phosphoserine Ref.6
Modified residue1381Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q08985 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 54658C7B92A610F0

FASTA32536,669
        10         20         30         40         50         60 
MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK 

        70         80         90        100        110        120 
IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK 

       130        140        150        160        170        180 
YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE 

       190        200        210        220        230        240 
LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV 

       250        260        270        280        290        300 
SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA 

       310        320 
RIIGGCCRTS PKDIQEISAA VKKYT

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Reverse methionine biosynthesis from S-adenosylmethionine in eukaryotic cells."
Thomas D., Becker A., Surdin-Kerjan Y.
J. Biol. Chem. 275:40718-40724(2000) [PubMed: 11013242] [Abstract]
Cited for: FUNCTION, INDUCTION.
[4]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND THR-138, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z73629 Genomic DNA. Translation: CAA98009.1.
BK006949 Genomic DNA. Translation: DAA11163.1.
PIRS65306.
RefSeqNP_015050.1. NM_001184087.1.

3D structure databases

ProteinModelPortalQ08985.
SMRQ08985. Positions 6-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ08985.

Proteomic databases

PeptideAtlasQ08985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL273W; YPL273W; YPL273W.
GeneID855855.
KEGGsce:YPL273W.
NMPDRfig|4932.3.peg.6174.

Organism-specific databases

CYGDYPL273w.
SGDS000006194. SAM4.

Phylogenomic databases

eggNOGfuNOG08285.
GeneTreeEFGT00050000004751.
HOGENOMHBG204042.
OMARTYARDI.
OrthoDBEOG4MSH79.

Gene expression databases

ArrayExpressQ08985.
GenevestigatorQ08985.
GermOnlineYPL273W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR003726. S_MeTrfase.
[Graphical view]
Gene3DG3DSA:3.20.20.330. S_methyl_trans. 1 hit.
KOK00547.
PfamPF02574. S-methyl_trans. 1 hit.
[Graphical view]
SUPFAMSSF82282. S_methyl_trans. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980460.

Entry information

Entry nameSAM4_YEAST
AccessionPrimary (citable) accession number: Q08985
Secondary accession number(s): D6W397
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 77 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

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