ID Q6Y9R3_9TRYP Unreviewed; 274 AA.
AC Q6Y9R3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating) {ECO:0000256|ARBA:ARBA00013011};
DE EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011};
DE Flags: Fragment;
OS Leptomonas sp. FA-2003.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=218935 {ECO:0000313|EMBL:AAO38989.1};
RN [1] {ECO:0000313|EMBL:AAO38989.1}
RP NUCLEOTIDE SEQUENCE.
RA Aguiar-Alves F., Noyes H., Cupolillo E., Grimaldi G., Kemp S.;
RT "A phylogeny of the genus Leishmania based on 6-phosphgluconate
RT dehydrogenase (6PGDH) gene sequences.";
RL Submitted (OCT-2002) 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; AY168569; AAO38989.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Y9R3; -.
DR UniPathway; UPA00115; UER00410.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR006184; 6PGdom_BS.
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; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
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.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126}.
FT DOMAIN 85..274
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAO38989.1"
FT NON_TER 274
FT /evidence="ECO:0000313|EMBL:AAO38989.1"
SQ SEQUENCE 274 AA; 29612 MW; 2C5BAAA2A79EF5D9 CRC64;
DIIIDTGNAN FKDQGKRATH LESCGLRFLG MGISGGEEGA RKGPAFFPGG TPSVWEEVRP
IVEAAAAKAE DGRPCVTFNG KGGAGSCVKM YHNAGEYAIL QIWGEAFNAL SAIGFNNDEI
ADVFQAWKDE GFLKSYMLDI SIAACRAKEP AGTFLTEKVK DRIGSKGTGL WSAQEALEVG
VPAPSLNMAV ISREMTMFKD ERIANAKAFP QFPHGLGHVV KDKSPNAPEV KQLYHAVVIS
IIASYSQMFQ CLRELDKVYD FGLNLPATIA TFRA
//
