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Q9SCX9 (GPDA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 1, chloroplastic
EC=1.1.1.8
Gene names
Name:DHAPRD
Ordered Locus Names:At5g40610
ORF Names:MNF13.16
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in glycerolipid metabolism By similarity.

Catalytic activity

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Subcellular location

Plastid › chloroplast Ref.1.

Tissue specificity

Expressed in young seedlings, flowers and siliques. Expressed at low levels in roots. Ref.1

Sequence similarities

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=12.8 µM for glycerone phosphate Ref.1

Vmax=3.2 µmol/sec/mg enzyme toward glycerone phosphate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Chloroplast Potential
Chain33 – 400368Glycerol-3-phosphate dehydrogenase [NAD(+)] 1, chloroplastic
PRO_0000287871

Regions

Nucleotide binding61 – 666NAD By similarity
Region321 – 3222Substrate binding By similarity

Sites

Active site2571Proton acceptor By similarity
Binding site921NAD By similarity
Binding site1491NAD By similarity
Binding site1721NAD; via amide nitrogen By similarity
Binding site1721Substrate By similarity
Binding site2051NAD; via amide nitrogen By similarity
Binding site3211NAD By similarity
Binding site3501NAD; via amide nitrogen By similarity
Binding site3521NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SCX9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9A37BC876E8663CC

FASTA40043,791
        10         20         30         40         50         60 
MRFRSFFFSS SIFSLSHSRS PSLSSSRFSS LSAAMSPALE KSRQGNGGCN DDSKSKVTVV 

        70         80         90        100        110        120 
GSGNWGSVAA KLIASNALKL PSFHDEVRMW VFEEVLPNGE KLNDVINKTN ENVKYLPGIK 

       130        140        150        160        170        180 
LGRNVVADPD LENAVKDANM LVFVTPHQFM DGICKKLDGK ITGDVEAISL VKGMEVKKEG 

       190        200        210        220        230        240 
PCMISSLISK QLGINCCVLM GANIANEIAV EKFSEATVGY RGSREIADTW VQLFSTPYFM 

       250        260        270        280        290        300 
VTPVHDVEGV ELCGTLKNVV AIAAGFVDGL EMGNNTKAAI MRIGLREMKA LSKLLFPSVK 

       310        320        330        340        350        360 
DSTFFESCGV ADVITTCLGG RNRRVAEAFA KSRGKRSFDE LEAEMLQGQK LQGVSTAREV 

       370        380        390        400 
YEVLKHCGWL EMFPLFSTVH QICTGRLQPE AIVQYRENKL

« Hide

References

« Hide 'large scale' references
[1]"Molecular and biochemical characterizations of a plastidic glycerol-3-phosphate dehydrogenase from Arabidopsis."
Wei Y., Periappuram C., Datla R., Selvaraj G., Zou J.
Plant Physiol. Biochem. 39:841-848(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ242602 mRNA. Translation: CAB64726.1.
AB009052 Genomic DNA. Translation: BAB08532.1.
CP002688 Genomic DNA. Translation: AED94573.1.
BT000967 mRNA. Translation: AAN41367.1.
AY080863 mRNA. Translation: AAL87336.1.
IPIIPI00538973.
RefSeqNP_198877.1. NM_123425.4.
UniGeneAt.695.

3D structure databases

HSSPHSSP built from PDB template 1X0X based on UniProtKB Q8N1B0.
ProteinModelPortalQ9SCX9.
SMRQ9SCX9. Positions 56-383.
ModBaseSearch...

Proteomic databases

PaxDbQ9SCX9.
PRIDEQ9SCX9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G40610.1; AT5G40610.1; AT5G40610.
GeneID834060.
KEGGath:AT5G40610.

Organism-specific databases

TAIRAt5g40610.

Phylogenomic databases

eggNOGCOG0240.
HOGENOMHOG000246855.
InParanoidQ9SCX9.
KOK00006.
OMAKPVQEML.
PhylomeDBQ9SCX9.
ProtClustDBCLSN2686185.

Enzyme and pathway databases

UniPathwayUPA00940.

Gene expression databases

GenevestigatorQ9SCX9.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11728. PTHR11728. 1 hit.
PfamPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSPR00077. GPDHDRGNASE.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR03376. glycerol3P_DH. 1 hit.
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPDA1_ARATH
AccessionPrimary (citable) accession number: Q9SCX9
Secondary accession number(s): Q8RXI6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents