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Database: UniProt
Entry: A0A067D7K8_CITSI
LinkDB: A0A067D7K8_CITSI
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ID   A0A067D7K8_CITSI        Unreviewed;       426 AA.
AC   A0A067D7K8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating) {ECO:0000256|ARBA:ARBA00013011};
DE            EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011};
GN   ORFNames=CISIN_1g043238mg {ECO:0000313|EMBL:KDO38793.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO38793.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO38793.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002526}.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3. {ECO:0000256|ARBA:ARBA00004874}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419}.
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DR   EMBL; KK787429; KDO38793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067D7K8; -.
DR   STRING; 2711.A0A067D7K8; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0008114; F:phosphogluconate 2-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
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   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 2.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT   DOMAIN          154..402
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   REGION          51..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  46837 MW;  7C3561DE1C2BA97C CRC64;
     MEASALSRIG LAGLAVMGQK LALNVPEKGF QISVYNRTTS KVDETLDRAH REDRPLHSQG
     LRPLHPTPQI HHHRPLGETS GTSTPSAVSM KPVRRVCFIS AWGSPGARKA RHGPSLMPGG
     SFEAYNNIRD ILQRVAAHVD DGPCITYIGE GGSGNFVKMV HNGIEYGDMQ LISQAYDVLK
     HVGGVSNAEL AEIFDEWNKG ELESFLVQIT ADIFKVKDEY GEGELVDKIL DKTGMKGTRK
     WTIQQAAELL VAALTIAASL DCRYLSGLKE ERQEAAKVLK EAGLKDEVQN VGVHVDKKRL
     IDDVRQALIK NAYQRNPNLA SLVVDPEFAR EMVQRQAAWR RVVGLAISAG ISTPGMCASL
     SYFDTYRRAR LPANLVQAQR DLFGAHAYER IDRPGSFHTE WTKLARQTGA GVGAFNSAAA
     FCYLFV
//
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