ID 6PGD_TRYBB Reviewed; 479 AA. AC P31072; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 13-SEP-2023, entry version 122. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=GND; OS Trypanosoma brucei brucei. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=427; RX PubMed=8426618; DOI=10.1016/0166-6851(93)90247-u; RA Barrett M.P., le Page R.W.F.; RT "A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei."; RL Mol. Biochem. Parasitol. 57:89-100(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT. RX PubMed=9737929; DOI=10.1006/jmbi.1998.2059; RA Phillips C., Dohnalek J., Gover S., Barrett M.P., Adams M.J.; RT "A 2.8-A resolution structure of 6-phosphogluconate dehydrogenase from the RT protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme RT accounts for differences in activity with coenzyme and substrate RT analogues."; RL J. Mol. Biol. 282:667-681(1998). 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:0000269|PubMed:9737929}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X65623; CAA46577.1; -; Genomic_DNA. DR PIR; A48565; A48565. DR PDB; 1PGJ; X-ray; 2.82 A; A/B=2-479. DR PDBsum; 1PGJ; -. DR AlphaFoldDB; P31072; -. DR SMR; P31072; -. DR BRENDA; 1.1.1.44; 6519. DR SABIO-RK; P31072; -. DR UniPathway; UPA00115; UER00410. DR EvolutionaryTrace; P31072; -. DR GO; GO:0097014; C:ciliary plasm; IDA:GeneDB. DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB. DR GO; GO:0020015; C:glycosome; IDA:GeneDB. DR GO; GO:0050661; F:NADP binding; EXP:GeneDB. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; EXP:GeneDB. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; ISM:GeneDB. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. 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; IPR006113; 6PGDH_Gnd/GntZ. 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 NCBIfam; TIGR00873; gnd; 1. 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 PIRSF; PIRSF000109; 6PGD; 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 1: Evidence at protein level; KW 3D-structure; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1..479 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090071" 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 9..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 32..34 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 263 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 290 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 454 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 460 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 12..23 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 35..44 FT /evidence="ECO:0007829|PDB:1PGJ" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 60..66 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 81..93 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 108..119 FT /evidence="ECO:0007829|PDB:1PGJ" FT TURN 120..122 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 124..132 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 133..139 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 181..209 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 214..226 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 233..243 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 265..276 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 281..294 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 296..305 FT /evidence="ECO:0007829|PDB:1PGJ" FT TURN 307..310 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 325..356 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 362..367 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 380..389 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 401..421 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 427..439 FT /evidence="ECO:0007829|PDB:1PGJ" FT HELIX 446..458 FT /evidence="ECO:0007829|PDB:1PGJ" FT STRAND 462..471 FT /evidence="ECO:0007829|PDB:1PGJ" SQ SEQUENCE 479 AA; 52154 MW; 64FED260915ABC2F CRC64; MSMDVGVVGL GVMGANLALN IAEKGFKVAV FNRTYSKSEE FMKANASAPF AGNLKAFETM EAFAASLKKP RKALILVQAG AATDSTTEQL KKVFEKGDIL VDTGNAHFKD QGRRAQQLEA AGLRFLGMGI SGGEEGARKG PAFFPGGTLS VWEEIRPIVE AAAAKADDGR PCVTMNGSGG AGSCVKMYHN SGEYAILQIW GEVFDILRAM GLNNDEVAAV LEDWKSKNFL KSYMLDISIA AARAKDKDGS YLTEHVMDRI GSKGTGLWSA QEALEIGVPA PSLNMAVVSR QFTMYKTERQ ANASNAPGIT QSPGYTLKNK SPSGPEIKQL YDSVCIAIIS CYAQMFQCLR EMDKVHNFGL NLPATIATFR AGCILQGYLL KPMTEAFEKN PNISNLMCAF QTEIRAGLQN YRDMVALITS KLEVSIPVLS ASLNYVTAMF TPTLKYGQLV SLQRDVFGRH GYERVDKDGR ESFQWPELQ //