6PGD2_ORYSJ
ID 6PGD2_ORYSJ Reviewed; 508 AA.
AC Q2R480; A0A0P0Y2I7; Q7Y248;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating 2, chloroplastic;
DE Short=OsG6PGH2;
DE EC=1.1.1.44;
DE Flags: Precursor;
GN Name=G6PGH2; OrderedLocusNames=Os11g0484500, LOC_Os11g29400;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-508, AND INDUCTION.
RC STRAIN=cv. Jiu Caiqing; TISSUE=Leaf;
RX DOI=10.1111/j.1744-7909.2007.00460.x;
RA Hou F.-Y., Huang J., Yu S.-L., Zhang H.-S.;
RT "The 6-phosphogluconate dehydrogenase genes are responsive to abiotic
RT stresses in rice.";
RL J. Integr. Plant Biol. 49:655-663(2007).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC to NADPH. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- INDUCTION: By drought, cold, high salinity and abscisic acid (ABA)
CC treatments. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP33506.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DP000010; ABA93694.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF28275.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT14060.1; -; Genomic_DNA.
DR EMBL; AK071592; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY278362; AAP33506.2; ALT_INIT; mRNA.
DR RefSeq; XP_015616899.1; XM_015761413.1.
DR AlphaFoldDB; Q2R480; -.
DR SMR; Q2R480; -.
DR STRING; 4530.OS11T0484500-01; -.
DR PaxDb; Q2R480; -.
DR PRIDE; Q2R480; -.
DR EnsemblPlants; Os11t0484500-01; Os11t0484500-01; Os11g0484500.
DR GeneID; 4350528; -.
DR Gramene; Os11t0484500-01; Os11t0484500-01; Os11g0484500.
DR KEGG; osa:4350528; -.
DR eggNOG; KOG2653; Eukaryota.
DR HOGENOM; CLU_024540_4_2_1; -.
DR InParanoid; Q2R480; -.
DR OMA; QALYMGK; -.
DR OrthoDB; 847823at2759; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR ExpressionAtlas; Q2R480; baseline and differential.
DR Genevisible; Q2R480; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR PANTHER; PTHR11811; PTHR11811; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..12
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 13..508
FT /note="6-phosphogluconate dehydrogenase, decarboxylating 2,
FT chloroplastic"
FT /id="PRO_0000421102"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 28..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 51..53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 95..97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 206..207
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="N -> K (in Ref. 6; AAP33506)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="E -> K (in Ref. 6; AAP33506)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> T (in Ref. 5; AK071592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 54300 MW; FBF1FAB42278D49B CRC64;
MASPAPAPPA ASSSAAGSAP PPRIGLAGLA TMGQNLALNI AEKGFPISVY NRTAAKVDAT
VSRAEAEGAL PVLGHRDPRG FVLSLSRPRT VVLLVQAGRA VDATIDALVP YLDAGDAIVD
GGNEWYQNTE RRIEEAAARG ILYLGMGVSG GEEGARNGPS LMPGGHIDAY NNIRDILEKA
AAQTEDGACV TFVGPGGAGN FVKMVHNGIE YGDMQLIAEA YDVLRRVGGL SNSEIADVFA
EWNRGELESF LVEITADIFT VADPLDGSGG GGLVDKILDK TGMKGTGKWT VQQAAELAIA
APTIAASLDG RYLSGLKDER VAAAGVLEAE GMPSGLLETI NVDKKMLVDR VRQALYASKI
CSYAQGMNLL RAKSVEKGWN LNLAELARIW KGGCIIRAKF LDRIKKAYDR NPELANLIVD
REFAREMVQR QNAWRWVVAR AVEAGISTPG MSASLSYFDT YRCSRLPANL IQAQRDLFGA
HTYERIDRPG SFHTEWTKLA RKSNGAAI
