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A5GFY8 (SERA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-3-phosphoglycerate dehydrogenase

Short name=3-PGDH
EC=1.1.1.95
Gene names
Name:PHGDH
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH.

2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH.

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Serine biosynthesis
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-serine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

phosphoglycerate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 533532D-3-phosphoglycerate dehydrogenase
PRO_0000318300

Regions

Nucleotide binding155 – 1562NAD By similarity
Nucleotide binding234 – 2363NAD By similarity
Nucleotide binding283 – 2864NAD By similarity

Sites

Active site2361 By similarity
Active site2651 By similarity
Active site2831Proton donor By similarity
Binding site781NAD By similarity
Binding site1751NAD By similarity
Binding site2071NAD; via carbonyl oxygen By similarity
Binding site2601NAD By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3711Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GFY8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 2D80F1809E1579BE

FASTA53356,810
        10         20         30         40         50         60 
MAFANLRKVL ISDSLDPCCR EILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT 

        70         80         90        100        110        120 
SDVINAAKKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMILCLARQ 

       130        140        150        160        170        180 
IPQATASMKD GKWERKKFMG TELNGKVLGI LGLGRIGREV ATRMQSFGMK TIGYDPIIAP 

       190        200        210        220        230        240 
EVSASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFALCKKGVR VVNCARGGIV 

       250        260        270        280        290        300 
DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHEKVIS CPHLGASTRE AQSRCGEEIA 

       310        320        330        340        350        360 
IQFVDMVKGR SLAGVVNAQA LTSAFSPHTK PWIGLAEALG ALMQAWAGSP KGTIQVVTQG 

       370        380        390        400        410        420 
TSLKNSGTCL SPAVIVGLLK EASHRADVNL VNAKLLEKEA GLHVTTSHNP AAPEEQGGAE 

       430        440        450        460        470        480 
CFLTVALAGA PYQAVGLVQG TAPMLHALNG AVFRPEVPLR RGLPLLLFRA QPSNPTMLPT 

       490        500        510        520        530 
MIGLLAEARV QLLSYQTSVV SDGETWHVMA ISSLLPSLEP WKQHVTEAFQ FHF 

« Hide

References

[1]Porcine genome sequencing project
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Duroc.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR956647 Genomic DNA. Translation: CAN13230.1.
RefSeqNP_001116634.1. NM_001123162.1.
UniGeneSsc.21431.

3D structure databases

ProteinModelPortalA5GFY8.
SMRA5GFY8. Positions 6-307.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5GFY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000007358; ENSSSCP00000007163; ENSSSCG00000006717.
GeneID100144529.
KEGGssc:100144529.

Organism-specific databases

CTD26227.

Phylogenomic databases

GeneTreeENSGT00530000063021.
HOVERGENHBG054241.
OMATGVFDGY.
OrthoDBEOG4Q2DF9.

Family and domain databases

InterProIPR006236. D-3-Phosphoglycerate_DH.
IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KOK00058.
PANTHERPTHR10996:SF20. D3PG_Deh. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR01327. PGDH. 1 hit.
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERA_PIG
AccessionPrimary (citable) accession number: A5GFY8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 12, 2007
Last modified: November 16, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families