6PGD1_ORYSJ
ID 6PGD1_ORYSJ Reviewed; 480 AA.
AC Q9LI00; A0A0P0WRR6; Q7FRX8;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating 1;
DE Short=OsG6PGH1;
DE EC=1.1.1.44;
GN Name=G6PGH1; OrderedLocusNames=Os06g0111500, LOC_Os06g02144;
GN ORFNames=OsJ_19864, P0029D06.14-1;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY SALT.
RC STRAIN=cv. Jiu Caiqing; TISSUE=Seedling;
RX PubMed=14672408; DOI=10.1023/a:1026392422995;
RA Huang J., Zhang H., Wang J., Yang J.;
RT "Molecular cloning and characterization of rice 6-phosphogluconate
RT dehydrogenase gene that is up-regulated by salt stress.";
RL Mol. Biol. Rep. 30:223-227(2003).
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 GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
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 [7]
RP INDUCTION.
RC STRAIN=cv. Jiu Caiqing;
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: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in inflorescence, lowly expressed
CC in root and embryos and almost absent in leaves.
CC {ECO:0000269|PubMed:14672408}.
CC -!- INDUCTION: By drought, cold, high salinity and abscisic acid (ABA)
CC treatments. {ECO:0000269|PubMed:14672408, ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF486280; AAL92029.1; -; mRNA.
DR EMBL; AP001552; BAA93024.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18500.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95792.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ35578.1; -; Genomic_DNA.
DR EMBL; AK065920; BAG89736.1; -; mRNA.
DR RefSeq; XP_015642949.1; XM_015787463.1.
DR RefSeq; XP_015642950.1; XM_015787464.1.
DR AlphaFoldDB; Q9LI00; -.
DR SMR; Q9LI00; -.
DR STRING; 4530.OS06T0111500-01; -.
DR PaxDb; Q9LI00; -.
DR PRIDE; Q9LI00; -.
DR EnsemblPlants; Os06t0111500-01; Os06t0111500-01; Os06g0111500.
DR GeneID; 4339892; -.
DR Gramene; Os06t0111500-01; Os06t0111500-01; Os06g0111500.
DR KEGG; osa:4339892; -.
DR eggNOG; KOG2653; Eukaryota.
DR HOGENOM; CLU_024540_4_2_1; -.
DR InParanoid; Q9LI00; -.
DR OMA; VIMVKAG; -.
DR OrthoDB; 847823at2759; -.
DR BRENDA; 1.1.1.44; 4460.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q9LI00; baseline and differential.
DR Genevisible; Q9LI00; OS.
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 Cytoplasm; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW Reference proteome.
FT CHAIN 1..480
FT /note="6-phosphogluconate dehydrogenase, decarboxylating 1"
FT /id="PRO_0000421101"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 77..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 131..133
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 189..190
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52721 MW; A39AC9C0D9625355 CRC64;
MAVTRIGLAG LAVMGQNLAL NIAEKGFPIS VYNRTTSKVD ETVQRAKVEG NLPVYGFHDP
ASFVNSIQKP RVVIMLVKAG APVDQTIATL AAHLEQGDCI IDGGNEWYEN TERREKAMEE
RGLLYLGMGV SGGEEGARNG PSLMPGGSFE AYKYIEDILL KVAAQVPDSG PCVTYIGKGG
SGNFVKMVHN GIEYGDMQLI SEAYDVLKSV GKLTNSELQQ VFSEWNKGEL LSFLIEITAD
IFSIKDDQGS GHLVDKVLDK TGMKGTGKWT VQQAAELSVA APTIEASLDS RFLSGLKDER
VEAAKVFQGD FSSNLPVDKA QLIEDVRQAL YASKICSYAQ GMNIIKAKSM EKGWSLNLGE
LARIWKGGCI IRAIFLDRIK KAYDRNSDLA NLLVDPEFAQ EIMDRQAAWR RVVCLAINNG
VSTPGMSASL AYFDSYRRDR LPANLVQAQR DYFGAHTYER VDMPGSFHTE WFKIARAAKM
