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Protein

6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic

Gene

At1g64190

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

Functioni

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

Catalytic activityi

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

Pathwayi: pentose phosphate pathway

This protein is involved in step 3 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic (At1g24280), Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic (APG1), Glucose-6-phosphate 1-dehydrogenase (At3g27300), Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 2 (ACG12), Glucose-6-phosphate 1-dehydrogenase (G6PD4), Glucose-6-phosphate 1-dehydrogenase (At1g09420), Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic (At5g13110), Glucose-6-phosphate 1-dehydrogenase (At5g35790), Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 1 (ACG9), Glucose-6-phosphate 1-dehydrogenase (At5g40760), Glucose-6-phosphate 1-dehydrogenase 4, chloroplastic (At1g09420)
  2. Probable 6-phosphogluconolactonase 5, chloroplastic (EMB2024), Probable 6-phosphogluconolactonase 2 (At3g49360), Probable 6-phosphogluconolactonase 3 (At5g24420), Probable 6-phosphogluconolactonase 4 (At5g24410), Probable 6-phosphogluconolactonase 1 (At1g13700)
  3. 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic (At1g64190), 6-phosphogluconate dehydrogenase, decarboxylating 2, chloroplastic (At5g41670), 6-phosphogluconate dehydrogenase, decarboxylating 3 (At3g02360)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081NADPBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei195 – 1951Proton donorBy similarity
Binding sitei196 – 1961SubstrateBy similarity
Binding sitei266 – 2661Substrate; via amide nitrogenBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Binding sitei458 – 4581Substrate; shared with dimeric partnerBy similarity
Binding sitei464 – 4641Substrate; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 186NADPBy similarity
Nucleotide bindingi36 – 383NADPBy similarity
Nucleotide bindingi80 – 823NADPBy similarity

GO - Molecular functioni

GO - Biological processi

  • D-gluconate metabolic process Source: UniProtKB-KW
  • pentose-phosphate shunt, oxidative branch Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization, Pentose shunt

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciARA:AT1G64190-MONOMER.
ReactomeiR-ATH-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00115; UER00410.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic (EC:1.1.1.44)
Gene namesi
Ordered Locus Names:At1g64190
ORF Names:F22C12.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G64190.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4874876-phosphogluconate dehydrogenase, decarboxylating 1, chloroplasticPRO_0000421098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SH69.
PRIDEiQ9SH69.

PTM databases

iPTMnetiQ9SH69.

Expressioni

Gene expression databases

GenevisibleiQ9SH69. AT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi27945. 3 interactions.
IntActiQ9SH69. 1 interaction.
STRINGi3702.AT1G64190.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SH69.
SMRiQ9SH69. Positions 5-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1363Substrate bindingBy similarity
Regioni191 – 1922Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2653. Eukaryota.
COG0362. LUCA.
HOGENOMiHOG000255147.
InParanoidiQ9SH69.
KOiK00033.
OMAiHSCVVYD.
PhylomeDBiQ9SH69.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR012284. 6PGD_dom_3.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_Gnd/GntZ.
IPR006115. 6PGDH_NADP-bd.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
PRINTSiPR00076. 6PGDHDRGNASE.
SMARTiSM01350. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9SH69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESAALSRIG LAGLAVMGQN LALNIAEKGF PISVYNRTTS KVDETLDRAA
60 70 80 90 100
VEGNLPVSGQ YSPRDFVLSI QRPRSLIILV KAGAPVDQTI DAFSEYMEPG
110 120 130 140 150
DCIIDGGNEW YQNTERRISE AEQKGLLYLG MGVSGGEEGA RNGPSLMPGG
160 170 180 190 200
SFQAYDNIKD ILEKVAAQVE DGPCVTYIGE GGSGNFVKMV HNGIEYGDMQ
210 220 230 240 250
LISEAYDVLK NVGGLSNEEL AEIFTEWNSG ELESFLVEIT SDIFRVKDEF
260 270 280 290 300
GDGELVDKIL DKTGMKGTGK WTVQQAAELS VAAPTIAASL DCRYLSGLKD
310 320 330 340 350
ERENAAKVLR EAGLKEEIGS ASSGIDKKRL VDDVRQALYA SKICSYAQGM
360 370 380 390 400
NLLRAKSLEK SWNLNFGELA RIWKGGCIIR AVFLDRIKKA YQRNPDLASL
410 420 430 440 450
VVDPEFAKEM VQRQAAWRRV VGLAVSAGIS TPGMCASLAY FDTYRRARLP
460 470 480
ANLVQAQRDL FGAHTYERTD RPGAYHTEWT KLARKNH
Length:487
Mass (Da):53,378
Last modified:May 1, 2000 - v1
Checksum:i2D5F2C25CF2827BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007764 Genomic DNA. Translation: AAF24560.1.
CP002684 Genomic DNA. Translation: AEE34207.1.
BT004568 mRNA. Translation: AAO42814.1.
AK227596 mRNA. Translation: BAE99587.1.
RefSeqiNP_176601.1. NM_105093.3.
UniGeneiAt.43563.
At.70356.

Genome annotation databases

EnsemblPlantsiAT1G64190.1; AT1G64190.1; AT1G64190.
GeneIDi842724.
GrameneiAT1G64190.1; AT1G64190.1; AT1G64190.
KEGGiath:AT1G64190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007764 Genomic DNA. Translation: AAF24560.1.
CP002684 Genomic DNA. Translation: AEE34207.1.
BT004568 mRNA. Translation: AAO42814.1.
AK227596 mRNA. Translation: BAE99587.1.
RefSeqiNP_176601.1. NM_105093.3.
UniGeneiAt.43563.
At.70356.

3D structure databases

ProteinModelPortaliQ9SH69.
SMRiQ9SH69. Positions 5-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27945. 3 interactions.
IntActiQ9SH69. 1 interaction.
STRINGi3702.AT1G64190.1.

PTM databases

iPTMnetiQ9SH69.

Proteomic databases

PaxDbiQ9SH69.
PRIDEiQ9SH69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G64190.1; AT1G64190.1; AT1G64190.
GeneIDi842724.
GrameneiAT1G64190.1; AT1G64190.1; AT1G64190.
KEGGiath:AT1G64190.

Organism-specific databases

TAIRiAT1G64190.

Phylogenomic databases

eggNOGiKOG2653. Eukaryota.
COG0362. LUCA.
HOGENOMiHOG000255147.
InParanoidiQ9SH69.
KOiK00033.
OMAiHSCVVYD.
PhylomeDBiQ9SH69.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.
BioCyciARA:AT1G64190-MONOMER.
ReactomeiR-ATH-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

PROiQ9SH69.

Gene expression databases

GenevisibleiQ9SH69. AT.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR012284. 6PGD_dom_3.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_Gnd/GntZ.
IPR006115. 6PGDH_NADP-bd.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
PRINTSiPR00076. 6PGDHDRGNASE.
SMARTiSM01350. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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.
    , 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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "The oxidative pentose phosphate pathway: structure and organisation."
    Kruger N.J., von Schaewen A.
    Curr. Opin. Plant Biol. 6:236-246(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. Cited for: GENE FAMILY.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry namei6PGD1_ARATH
AccessioniPrimary (citable) accession number: Q9SH69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 117 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

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 one 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.