Reviewed, UniProtKB/Swiss-Prot P37303 (GLY1_YEAST)

Names and origin

Protein names

Recommended name:
    Low specificity L-threonine aldolase
      Short name=Low specificity L-TA
      Short name=TA
    EC=4.1.2.5

Gene names

Name:	GLY1
Ordered Locus Names:	YEL046C
ORF Names:	SYGP-ORF34

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	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
Catalytic activity	L-threonine = glycine + acetaldehyde. L-allo-threonine = glycine + acetaldehyde.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; glycine biosynthesis; glycine from L-allo-threonine: step 1/1. Amino-acid degradation; L-threonine degradation via aldolase pathway; acetaldehyde and glycine from L-threonine: step 1/1.
Subunit structure	Homotetramer.
Miscellaneous	Present with 106000 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the threonine aldolase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from direct assay. Source: SGD threonine catabolic process Inferred from direct assay. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	L-allo-threonine aldolase activity Ref.3 Inferred from direct assay. Source: SGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Low specificity L-threonine aldolase		PRO_0000121572
Amino acid modifications
	Modified residue	213	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	367	1	Phosphoserine Ref.9
	Modified residue	369	1	Phosphoserine Ref.9
	Modified residue	370	1	Phosphothreonine Ref.9 Ref.5
	Cross-link	228		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7 Ref.8
Experimental info
	Sequence conflict	253	1	I → M in AAB64996. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P37303-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 43079EB45C502B86	FASTA	387	42,797
	10 20 30 40 50 60 MTEFELPPKY ITAANDLRSD TFTTPTAEMM EAALEASIGD AVYGEDVDTV RLEQTVARMA 70 80 90 100 110 120 GKEAGLFCVS GTLSNQIAIR THLMQPPYSI LCDYRAHVYT HEAAGLAILS QAMVVPVVPS 130 140 150 160 170 180 NGDYLTLEDI KSHYVPDDGD IHGAPTRLIS LENTLHGIVY PLEELVRIKA WCMENGLKLH 190 200 210 220 230 240 CDGARIWNAA AQSGVPLKQY GEIFDSISIC LSKSMGAPIG SVLVGNLKFV KKATHFRKQQ 250 260 270 280 290 300 GGGIRQSGMM ARIALVNINN DWKSQLLYSH SLAHELAEYC EAKGIPLESP ADTNFVFINL 310 320 330 340 350 360 KAARMDPDVL VKKGLKYNVK LMGGRVSFHY QVTRDTLEKV KLAISEAFDY AKEHPFDCNG 370 380 PTQIYRSEST EVDVDGNAIR EIKTYKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine." McNeil J.B., McIntosh E.M., Taylor B.V., Zhang F.-R., Tang S., Bognar A.L. J. Biol. Chem. 269:9155-9165(1994) [PubMed: 8132653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 201238 / W303-1B.
[2]	"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. , 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: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine -- expression of the gene in Escherichia coli and purification and characterization of the enzyme." Liu J.-Q., Nagata S., Dairi T., Misono H., Shimizu S., Yamada H. Eur. J. Biochem. 245:289-293(1997) [PubMed: 9151955] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: a key enzyme in glycine biosynthesis." Monschau N., Stahmann K.-P., Sahm H., McNeil J.B., Bognar A.L. FEMS Microbiol. Lett. 150:55-60(1997) [PubMed: 9163906] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, MASS SPECTROMETRY.
[6]	"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].
[7]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, MASS SPECTROMETRY.
[8]	"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Hitchcock A.L., Auld K., Gygi S.P., Silver P.A. Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, MASS SPECTROMETRY.
[9]	"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-367; SER-369 AND THR-370, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L28739 Genomic DNA. Translation: AAA72430.1. U18779 Genomic DNA. Translation: AAB64996.1.
PIR	S30831.
RefSeq	NP_010868.1.
3D structure databases
SMR	P37303. Positions 16-345.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4287N.
IntAct	P37303. 8 interactions.
STRING	P37303.
Proteomic databases
PeptideAtlas	P37303.
PRIDE	P37303.
Genome annotation databases
Ensembl	YEL046C; YEL046C; YEL046C; Saccharomyces cerevisiae. [Genome view]
GeneID	856665.
KEGG	sce:YEL046C.
Organism-specific databases
CYGD	YEL046c.
SGD	S000000772. GLY1.
Phylogenomic databases
eggNOG	fuNOG04456.
HOGENOM	HBG293912.
OrthoDB	EOG993517.
PhylomeDB	P37303.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12832.
BRENDA	4.1.2.5. 250.
Gene expression databases
ArrayExpress	P37303.
Genevestigator	P37303.
GermOnline	YEL046C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001597. ArAA_b-elim_lyase/Thr_aldolase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF01212. Beta_elim_lyase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLY1_YEAST

Accession

Primary (citable) accession number: P37303
Secondary accession number(s): P32615

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 19, 2010
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)