[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; Nature 387:78-81(1997).
[2]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-22 AND SER-29, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

Comments

CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD⁺ = 3-phosphonooxypyruvate + NADH.
CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD⁺ = 2-oxoglutarate + NADH.
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glyceric acid: step 1/3 .
INTERACTION:
Self; NbExp=1; IntAct=EBI-16961, EBI-16961;
O13567:-; NbExp=1; IntAct=EBI-16961, EBI-38884;
O13569:-; NbExp=1; IntAct=EBI-16961, EBI-37420;
P38226:-; NbExp=1; IntAct=EBI-16961, EBI-21429;
Q99318:-; NbExp=1; IntAct=EBI-16961, EBI-34201;
P39714:BDH1; NbExp=1; IntAct=EBI-16961, EBI-3501;
P33313:CNS1; NbExp=1; IntAct=EBI-16961, EBI-4806;
P41910:MAF1; NbExp=1; IntAct=EBI-16961, EBI-10375;
P15424:MSS116; NbExp=1; IntAct=EBI-16961, EBI-11308;
Q12143:NSL1; NbExp=1; IntAct=EBI-16961, EBI-33666;
P49686:NUP42; NbExp=1; IntAct=EBI-16961, EBI-12310;
P40510:SER33; NbExp=1; IntAct=EBI-16961, EBI-16821;
P32771:SFA1; NbExp=1; IntAct=EBI-16961, EBI-6770;
Q12116:TMS1; NbExp=1; IntAct=EBI-16961, EBI-19306;
Q99337:TY1B-NL2; NbExp=1; IntAct=EBI-16961, EBI-34960;
MISCELLANEOUS: Present with 7670 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
SIMILARITY: Contains 1 ACT domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U18839; AAB64636.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S50584; S50584.

RefSeq

NP_011004.1; -.

3D structure databases

HSSP

P08328; 1PSD. [HSSP ENTRY / PDB]

ModBase

P40054.

Protein-protein interaction databases

DIP

DIP:5336N; -.

IntAct

P40054; -.

Organism-specific databases

YER081w; -.

S000000883; SER3.

Gene expression databases

GermOnline

YER081W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0016597;	Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0004617;	Molecular function: phosphoglycerate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0006564;	Biological process: L-serine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002912; ACT_bd.
IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
PF01842; ACT; 1.
Pfam graphical view of domain structure.

PROSITE

PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.

ProtoNet

P40054.

Proteomic databases

PeptideAtlas

P40054; -.

Genome annotation databases

Ensembl

YER081W; Saccharomyces cerevisiae. [Contig view]

856814; -.

U00092_GR; YER081W.

sce:YER081W; -.

fig|4932.3.peg.2074; -.

Phylogenomic databases

HOGENOM

P40054; -.

Other

LinkHub

P40054; -.

NextBio

983085; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; NAD; Oxidoreductase; Phosphoprotein; Serine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 469`	`469`	`D-3-phosphoglycerate dehydrogenase 1.`	`PRO_0000076018`
`DOMAIN`	`398 468`	`71`	`ACT.`
`ACT_SITE`	`287 287`		`By similarity.`
`ACT_SITE`	`316 316`		`By similarity.`
`ACT_SITE`	`347 347`		`Proton donor (By similarity).`
`MOD_RES`	`20 20`		`Phosphoserine.`
`MOD_RES`	`22 22`		`Phosphoserine.`
`MOD_RES`	`29 29`		`Phosphoserine.`

Sequence information

Length: 469 AA [This is the length of the unprocessed precursor]

Molecular weight: 51193 Da [This is the MW of the unprocessed precursor]

CRC64: E1E69070BF41A87C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSIDINNLQ NTFQQAMNMS GSPGAVCTSP TQSFMNTVPQ RLNAVKHPKI LKPFSTGDMK 

        70         80         90        100        110        120 
ILLLENVNQT AITIFEEQGY QVEFYKSSLP EEELIEKIKD VHAIGIRSKT RLTSNVLQHA 

       130        140        150        160        170        180 
KNLVCIGCFC IGTNQVDLDY ATSRGIAVFN SPFSNSRSVA ELVIAEIISL ARQLGDRSIE 

       190        200        210        220        230        240 
LHTGTWNKVA ARCWEVRGKT LGIIGYGHIG SQLSVLAEAM GLHVLYYDIV TIMALGTARQ 

       250        260        270        280        290        300 
VSTLDELLNK SDFVTLHVPA TPETEKMLSA PQFAAMKDGA YVINASRGTV VDIPSLIQAV 

       310        320        330        340        350        360 
KANKIAGAAL DVYPHEPAKN GEGSFNDELN SWTSELVSLP NIILTPHIGG STEEAQSSIG 

       370        380        390        400        410        420 
IEVATALSKY INEGNSVGSV NFPEVALKSL SYDQENTVRV LYIHQNVPGV LKTVNDILSN 

       430        440        450        460 
HNIEKQFSDS NGEIAYLMAD ISSVDQSDIK DIYEQLNQTS AKISIRLLY

P40054 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools