Reviewed, UniProtKB/Swiss-Prot P25379 (STDH_YEAST)

Names and origin

Protein names

Recommended name:
    Catabolic L-serine/threonine dehydratase
Including the following 2 domains:
    1- Recommended name:
            L-serine dehydratase
              EC=4.3.1.17
        Alternative name(s):
            L-serine deaminase
    2- Recommended name:
            L-threonine dehydratase
              EC=4.3.1.19
        Alternative name(s):
            L-threonine deaminase

Gene names

Name:	CHA1
Ordered Locus Names:	YCL064C
ORF Names:	YCL64C

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	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-serine = pyruvate + NH3. L-threonine = 2-oxobutanoate + NH3.
Cofactor	Pyridoxal phosphate By similarity.
Subcellular location	Mitochondrion. Ref.4
Miscellaneous	Present with 36600 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the serine/threonine dehydratase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	serine family amino acid catabolic process Ref.1 Inferred from mutant phenotype. Source: SGD threonine catabolic process Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial nucleoid Inferred from direct assay. Source: SGD
Molecular function	L-serine ammonia-lyase activity Ref.1 Inferred from mutant phenotype. Source: SGD L-threonine ammonia-lyase activity Ref.1 Inferred from mutant phenotype. 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 – 360	360	Catabolic L-serine/threonine dehydratase		PRO_0000185598
Amino acid modifications
	Modified residue	37	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	34	1	G → A in AAA35040. Ref.1
	Sequence conflict	268	1	T → P in AAA35040. Ref.1
	Sequence conflict	317 – 318	2	GG → AS in AAA35040. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25379-1 [UniParc]. Last modified March 15, 2004. Version 2. Checksum: FC905FF3D111187D	FASTA	360	39,301
	10 20 30 40 50 60 MSIVYNKTPL LRQFFPGKAS AQFFLKYECL QPSGSFKSRG IGNLIMKSAI RIQKDGKRSP 70 80 90 100 110 120 QVFASSGGNA GFAAATACQR LSLPCTVVVP TATKKRMVDK IRNTGAQVIV SGAYWKEADT 130 140 150 160 170 180 FLKTNVMNKI DSQVIEPIYV HPFDNPDIWE GHSSMIDEIV QDLKSQHISV NKVKGIVCSV 190 200 210 220 230 240 GGGGLYNGII QGLERYGLAD RIPIVGVETN GCHVFNTSLK IGQPVQFKKI TSIATSLGTA 250 260 270 280 290 300 VISNQTFEYA RKYNTRSVVI EDKDVIETCL KYTHQFNMVI EPACGAALHL GYNTKILENA 310 320 330 340 350 360 LGSKLAADDI VIIIACGGSS NTIKDLEEAL DSMRKKDTPV IEVADNFIFP EKNIVNLKSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases." Bornaes C., Petersen J.G., Holmberg S. Genetics 131:531-539(1992) [PubMed: 1628804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 268; 317 AND 318.
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M85194 Genomic DNA. Translation: AAA35040.1. X59720 Genomic DNA. Translation: CAA42403.2.
PIR	DWBYLH. S19395.
RefSeq	NP_001018030.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P25379.
Proteomic databases
PeptideAtlas	P25379.
PRIDE	P25379.
Genome annotation databases
Ensembl	YCL064C; YCL064C; YCL064C; Saccharomyces cerevisiae. [Genome view]
GeneID	850295.
GenomeReviews	Gene locus YCL064C in contig X59720_GR.
KEGG	sce:YCL064C.
NMPDR	fig|4932.3.peg.587.
Organism-specific databases
CYGD	YCL064c.
SGD	S000000569. CHA1.
Phylogenomic databases
HOGENOM	P25379.
OMA	ISHCKSI.
Enzyme and pathway databases
BRENDA	4.3.1.17. 250. 4.3.1.19. 250.
Gene expression databases
ArrayExpress	P25379.
Genevestigator	P25379.
GermOnline	YCL064C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. [Graphical view]
Pfam	PF00291. PALP. 1 hit. [Graphical view]
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	965664.

Entry information

Entry name

STDH_YEAST

Accession

Primary (citable) accession number: P25379

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	March 15, 2004
Last modified:	November 3, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)