Reviewed, UniProtKB/Swiss-Prot Q08985 (SAM4_YEAST)

Names and origin

Protein names

Recommended name:
    Homocysteine S-methyltransferase 2
    EC=2.1.1.10
Alternative name(s):
    S-methylmethionine:homocysteine methyltransferase 2
      Short name=SMM:Hcy S-methyltransferase 2
    S-adenosylmethionine metabolism protein 4

Gene names

Name:	SAM4
Ordered Locus Names:	YPL273W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.2
Catalytic activity	S-adenosyl-L-methionine + L-homocysteine = S-adenosyl-L-homocysteine + L-methionine.
Cofactor	Zinc Potential.
Subcellular location	Cytoplasm. Nucleus. Ref.3
Induction	Up-regulated in response to high extracellular methionine. Ref.2
Miscellaneous	Present with 60300 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Contains 1 Hcy-binding domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	S-adenosylhomocysteine metabolic process Inferred from direct assay. Source: SGD homocysteine metabolic process Inferred from direct assay. Source: SGD methionine biosynthetic process from S-adenosylmethionine Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Ref.3 Inferred from direct assay. Source: SGD nucleus Ref.3 Inferred from direct assay. Source: SGD
Molecular function	homocysteine S-methyltransferase activity Ref.2 Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 325	325	Homocysteine S-methyltransferase 2		PRO_0000114619
Regions
	Domain	6 – 321	316	Hcy-binding
Sites
	Metal binding	239	1	Zinc Potential
	Metal binding	306	1	Zinc Potential
	Metal binding	307	1	Zinc Potential
Amino acid modifications
	Modified residue	99	1	Phosphoserine Ref.5
	Modified residue	138	1	Phosphothreonine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q08985-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 54658C7B92A610F0	FASTA	325	36,669
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[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: 14562095] [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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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
EMBLGenBankDDBJ	Z73629 Genomic DNA. Translation: CAA98009.1.
PIR	S65306.
RefSeq	NP_015050.1.
3D structure databases
ModBase	Search...
Proteomic databases
PeptideAtlas	Q08985.
PRIDE	Q08985.
Genome annotation databases
Ensembl	YPL273W. Saccharomyces cerevisiae. [Contig view]
GeneID	855855.
GenomeReviews	Gene locus YPL273W in contig U00094_GR.
KEGG	sce:YPL273W.
NMPDR	fig|4932.3.peg.6174.
Organism-specific databases
CYGD	YPL273w.
SGD	S000006194. SAM4.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q08985.
OMA	Q08985. DESSANR.
Enzyme and pathway databases
BRENDA	2.1.1.10. 250.
Gene expression databases
GermOnline	YPL273W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003726. S_MeTrfase. [Graphical view]
Gene3D	G3DSA:3.20.20.330. S_methyl_trans. 1 hit.
Pfam	PF02574. S-methyl_trans. 1 hit. [Graphical view]
PROSITE	PS50970. HCY. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	980460.

Entry information

Entry name

SAM4_YEAST

Accession

Primary (citable) accession number: Q08985

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)