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Q949Q0 (GPDA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, chloroplastic

EC=1.1.1.8
Alternative name(s):
Protein SUPPRESSOR OF FATTY ACID DESATURASE DEFICIENCY 1
Gene names
Name:GLY1
Synonyms:SFD1
Ordered Locus Names:At2g40690
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required to supply glycerol-3-phosphate in the chloroplast for the synthesis of glycerolipids. Required for activation of systemic acquired resistance (SAR). Provision of glycerol-3-phosphate may be involved in generating lipid signals necessary for mediating defense responses and SAR. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH. Ref.4 Ref.5 Ref.8

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP-Rule MF_00394

Subcellular location

Plastidchloroplast By similarity HAMAP-Rule MF_00394.

Disruption phenotype

No visible phenotype under normal growth conditions, but leaves have decreased levels of hexadecatrienoic fatty acid (16:3) and increased levels of oleic acid (18:1). Ref.4 Ref.5

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.33 µM for glycerone phosphate Ref.8

Vmax=49 µmol/min/mg enzyme toward glycerone phosphate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Chloroplast Potential
Chain46 – 420375Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, chloroplastic HAMAP-Rule MF_00394
PRO_0000420174

Regions

Nucleotide binding94 – 996NAD By similarity
Region343 – 3442Substrate binding By similarity

Sites

Active site2791Proton acceptor By similarity
Binding site1711NAD By similarity
Binding site1941NAD; via amide nitrogen By similarity
Binding site1941Substrate By similarity
Binding site2281NAD; via amide nitrogen By similarity
Binding site3431NAD By similarity
Binding site3691NAD By similarity

Experimental info

Mutagenesis1941K → A: Loss of activity. Ref.8
Mutagenesis2791K → A: Loss of activity. Ref.8
Mutagenesis3321D → A: Loss of activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q949Q0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 3AACC248276BFC01

FASTA42045,092
        10         20         30         40         50         60 
MAASVQPACL DLHFSGKHPP LLKHNAIIVR CVSSPNVIPE ADSISGPPDI INTNRDQRKV 

        70         80         90        100        110        120 
VRIAWEKLVR WSRSLRAKAK TDVLERTRKV VVLGGGSFGT AMAAHVARRK EGLEVNMLVR 

       130        140        150        160        170        180 
DSFVCQSINE NHHNCKYFPE HKLPENVIAT TDAKAALLDA DYCLHAVPVQ FSSSFLEGIA 

       190        200        210        220        230        240 
DYVDPGLPFI SLSKGLELNT LRMMSQIIPI ALKNPRQPFV ALSGPSFALE LMNNLPTAMV 

       250        260        270        280        290        300 
VASKDKKLAN AVQQLLASSY LRINTSSDVT GVEIAGALKN VLAIAAGIVD GMNLGNNSMA 

       310        320        330        340        350        360 
ALVSQGCSEI RWLATKMGAK PTTITGLSGT GDIMLTCFVN LSRNRTVGVR LGSGETLDDI 

       370        380        390        400        410        420 
LTSMNQVAEG VATAGAVIAL AQKYNVKLPV LTAVAKIIDN ELTPTKAVLE LMNLPQIEEV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene SUPPRESSSOR OF FATTY ACID DESATURASE DEFICIENCY1 is required for glycerolipid metabolism and for the activation of systemic acquired resistance."
Nandi A., Welti R., Shah J.
Plant Cell 16:465-477(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
[5]"Oleic acid levels regulated by glycerolipid metabolism modulate defense gene expression in Arabidopsis."
Kachroo A., Venugopal S.C., Lapchyk L., Falcone D., Hildebrand D., Kachroo P.
Proc. Natl. Acad. Sci. U.S.A. 101:5152-5157(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
[6]"Plastidial fatty acid levels regulate resistance gene-dependent defense signaling in Arabidopsis."
Chandra-Shekara A.C., Venugopal S.C., Barman S.R., Kachroo A., Kachroo P.
Proc. Natl. Acad. Sci. U.S.A. 104:7277-7282(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Plastid omega3-fatty acid desaturase-dependent accumulation of a systemic acquired resistance inducing activity in petiole exudates of Arabidopsis thaliana is independent of jasmonic acid."
Chaturvedi R., Krothapalli K., Makandar R., Nandi A., Sparks A.A., Roth M.R., Welti R., Shah J.
Plant J. 54:106-117(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Biochemical and molecular-genetic characterization of SFD1's involvement in lipid metabolism and defense signaling."
Lorenc-Kukula K., Chaturvedi R., Roth M., Welti R., Shah J.
Front. Plant Sci. 3:26-26(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-194; LYS-279 AND ASP-332.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002685 Genomic DNA. Translation: AEC09864.1.
AY050968 mRNA. Translation: AAK93645.1.
AY114078 mRNA. Translation: AAM45126.1.
RefSeqNP_565939.1. NM_129631.2.
UniGeneAt.26537.

3D structure databases

ProteinModelPortalQ949Q0.
SMRQ949Q0. Positions 89-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G40690.1-P.

Proteomic databases

PaxDbQ949Q0.
PRIDEQ949Q0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G40690.1; AT2G40690.1; AT2G40690.
GeneID818664.
KEGGath:AT2G40690.

Organism-specific databases

TAIRAT2G40690.

Phylogenomic databases

eggNOGCOG0240.
HOGENOMHOG000246853.
InParanoidQ949Q0.
OMATLCHAMR.
PhylomeDBQ949Q0.
ProtClustDBCLSN2688847.

Enzyme and pathway databases

UniPathwayUPA00940.

Gene expression databases

GenevestigatorQ949Q0.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_00394. NAD_Glyc3P_dehydrog.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
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. SSF48179. 1 hit.
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ949Q0.

Entry information

Entry nameGPDA2_ARATH
AccessionPrimary (citable) accession number: Q949Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names