Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, chloroplastic

Gene

GLY1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.33 µM for glycerone phosphate1 Publication
  1. Vmax=49 µmol/min/mg enzyme toward glycerone phosphate1 Publication

Pathway: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711NADBy similarity
Binding sitei194 – 1941NAD; via amide nitrogenBy similarity
Binding sitei194 – 1941SubstrateBy similarity
Binding sitei228 – 2281NAD; via amide nitrogenBy similarity
Active sitei279 – 2791Proton acceptorBy similarity
Binding sitei343 – 3431NADBy similarity
Binding sitei369 – 3691NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi94 – 996NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • glycerol-3-phosphate catabolic process Source: InterPro
  • glycerolipid biosynthetic process Source: TAIR
  • glycerolipid metabolic process Source: TAIR
  • glycerophospholipid metabolic process Source: UniProtKB-UniPathway
  • phospholipid biosynthetic process Source: UniProtKB-KW
  • systemic acquired resistance Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism, Plant defense

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GLY1
Synonyms:SFD1
Ordered Locus Names:At2g40690
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G40690.

Subcellular locationi

GO - Cellular componenti

  • chloroplast envelope Source: TAIR
  • glycerol-3-phosphate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

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).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1941K → A: Loss of activity. 1 Publication
Mutagenesisi279 – 2791K → A: Loss of activity. 1 Publication
Mutagenesisi332 – 3321D → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545ChloroplastSequence AnalysisAdd
BLAST
Chaini46 – 420375Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, chloroplasticPRO_0000420174Add
BLAST

Proteomic databases

PaxDbiQ949Q0.
PRIDEiQ949Q0.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT2G40690.1.

Structurei

3D structure databases

ProteinModelPortaliQ949Q0.
SMRiQ949Q0. Positions 89-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 3442Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246853.
InParanoidiQ949Q0.
KOiK00006.
OMAiRTFRLYA.
PhylomeDBiQ949Q0.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q949Q0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVQPACL DLHFSGKHPP LLKHNAIIVR CVSSPNVIPE ADSISGPPDI
60 70 80 90 100
INTNRDQRKV VRIAWEKLVR WSRSLRAKAK TDVLERTRKV VVLGGGSFGT
110 120 130 140 150
AMAAHVARRK EGLEVNMLVR DSFVCQSINE NHHNCKYFPE HKLPENVIAT
160 170 180 190 200
TDAKAALLDA DYCLHAVPVQ FSSSFLEGIA DYVDPGLPFI SLSKGLELNT
210 220 230 240 250
LRMMSQIIPI ALKNPRQPFV ALSGPSFALE LMNNLPTAMV VASKDKKLAN
260 270 280 290 300
AVQQLLASSY LRINTSSDVT GVEIAGALKN VLAIAAGIVD GMNLGNNSMA
310 320 330 340 350
ALVSQGCSEI RWLATKMGAK PTTITGLSGT GDIMLTCFVN LSRNRTVGVR
360 370 380 390 400
LGSGETLDDI LTSMNQVAEG VATAGAVIAL AQKYNVKLPV LTAVAKIIDN
410 420
ELTPTKAVLE LMNLPQIEEV
Length:420
Mass (Da):45,092
Last modified:December 1, 2001 - v1
Checksum:i3AACC248276BFC01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002685 Genomic DNA. Translation: AEC09864.1.
AY050968 mRNA. Translation: AAK93645.1.
AY114078 mRNA. Translation: AAM45126.1.
RefSeqiNP_565939.1. NM_129631.2.
UniGeneiAt.26537.

Genome annotation databases

EnsemblPlantsiAT2G40690.1; AT2G40690.1; AT2G40690.
GeneIDi818664.
KEGGiath:AT2G40690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002685 Genomic DNA. Translation: AEC09864.1.
AY050968 mRNA. Translation: AAK93645.1.
AY114078 mRNA. Translation: AAM45126.1.
RefSeqiNP_565939.1. NM_129631.2.
UniGeneiAt.26537.

3D structure databases

ProteinModelPortaliQ949Q0.
SMRiQ949Q0. Positions 89-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT2G40690.1.

Proteomic databases

PaxDbiQ949Q0.
PRIDEiQ949Q0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G40690.1; AT2G40690.1; AT2G40690.
GeneIDi818664.
KEGGiath:AT2G40690.

Organism-specific databases

TAIRiAT2G40690.

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246853.
InParanoidiQ949Q0.
KOiK00006.
OMAiRTFRLYA.
PhylomeDBiQ949Q0.

Enzyme and pathway databases

UniPathwayiUPA00940.

Miscellaneous databases

PROiQ949Q0.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiGPDA2_ARATH
AccessioniPrimary (citable) accession number: Q949Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.