P36007 (SRY1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Threo-3-hydroxyaspartate ammonia-lyase
EC=4.3.1.16

Alternative name(s):
L-threo-3-hydroxyaspartate dehydratase

Gene names

Name:	SRY1
Ordered Locus Names:	YKL218C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exhibits dehydratase activity specific for L-threo-3-hydroxyaspartate. Ref.4
Catalytic activity	Threo-3-hydroxy-L-aspartate = oxaloacetate + NH3.
Cofactor	Pyridoxal phosphate By similarity. Ref.4
Sequence similarities	Belongs to the serine/threonine dehydratase family.
Biophysicochemical properties	Kinetic parameters: KM=3.9 mM for L-threo-3-hydroxyaspartate Ref.4 Vmax=110 µmol/min/mg enzyme toward L-threo-3-hydroxyaspartate

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular modified amino acid catabolic process Inferred from direct assay Ref.4. Source: SGD
Molecular function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threo-3-hydroxyaspartate ammonia-lyase activity Inferred from mutant phenotype Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 326	326	Threo-3-hydroxyaspartate ammonia-lyase		PRO_0000185589
Amino acid modifications
	Modified residue	53	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	217	1	Phosphoserine Ref.5
	Modified residue	219	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P36007 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 21CF7FEFC8AB4431	FASTA	326	34,899
	10 20 30 40 50 60 MIVPTYGDVL DASNRIKEYV NKTPVLTSRM LNDRLGAQIY FKGENFQRVG AFKFRGAMNA 70 80 90 100 110 120 VSKLSDEKRS KGVIAFSSGN HAQAIALSAK LLNVPATIVM PEDAPALKVA ATAGYGAHII 130 140 150 160 170 180 RYNRYTEDRE QIGRQLAAEH GFALIPPYDH PDVIAGQGTS AKELLEEVGQ LDALFVPLGG 190 200 210 220 230 240 GGLLSGSALA ARSLSPGCKI FGVEPEAGND GQQSFRSGSI VHINTPKTIA DGAQTQHLGE 250 260 270 280 290 300 YTFAIIRENV DDILTVSDQE LVKCMHFLAE RMKVVVEPTA CLGFAGALLK KEELVGKKVG 310 320 IILSGGNVDM KRYATLISGK EDGPTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein." Tzermia M., Horaitis O., Alexandraki D. Yeast 10:663-679(1994) [PubMed: 7941750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity." Wada M., Nakamori S., Takagi H. FEMS Microbiol. Lett. 225:189-193(2003) [PubMed: 12951240] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[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-217 AND SER-219, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75951 Genomic DNA. Translation: CAA53555.1. Z28218 Genomic DNA. Translation: CAA82063.1. BK006944 Genomic DNA. Translation: DAA08951.1.
PIR	S38061.
RefSeq	NP_012704.1. NM_001179783.1.
3D structure databases
ProteinModelPortal	P36007.
SMR	P36007. Positions 1-318.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6523N.
IntAct	P36007. 2 interactions.
STRING	P36007.
Proteomic databases
PeptideAtlas	P36007.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL218C; YKL218C; YKL218C.
GeneID	853662.
KEGG	sce:YKL218C.
NMPDR	fig|4932.3.peg.3682.
Organism-specific databases
CYGD	YKL218c.
SGD	S000001701. SRY1.
Phylogenomic databases
eggNOG	fuNOG07508.
GeneTree	EFGT00050000001007.
HOGENOM	HBG714501.
OMA	IVEPTGC.
OrthoDB	EOG4V1B91.
Gene expression databases
ArrayExpress	P36007.
Genevestigator	P36007.
GermOnline	YKL218C. 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]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974590.

Entry information

Entry name

SRY1_YEAST

Accession

Primary (citable) accession number: P36007
Secondary accession number(s): D6VWY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program