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 25-NOV-2008, entry version 60. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=GND; OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=427; RX MEDLINE=93149212; 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). RX MEDLINE=98411456; 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 RT the protozoan parasite Trypanosoma brucei: comparison with the sheep RT enzyme accounts for differences in activity with coenzyme and RT substrate analogues."; RL J. Mol. Biol. 282:667-681(1998). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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 GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:InterPro. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR InterPro; IPR006183; 6-phosphogluconate_DHase. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NAD-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DHase_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 1: Evidence at protein level; KW 3D-structure; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 479 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090071. FT STRAND 3 8 FT HELIX 12 23 FT STRAND 28 31 FT HELIX 35 44 FT TURN 45 47 FT HELIX 51 53 FT STRAND 54 56 FT HELIX 60 66 FT STRAND 72 75 FT HELIX 81 93 FT STRAND 99 102 FT HELIX 108 119 FT TURN 120 122 FT STRAND 124 132 FT HELIX 133 139 FT STRAND 142 147 FT HELIX 149 162 FT HELIX 181 209 FT HELIX 214 226 FT HELIX 233 243 FT STRAND 249 251 FT HELIX 252 255 FT HELIX 265 276 FT HELIX 281 294 FT HELIX 296 305 FT TURN 307 310 FT HELIX 325 356 FT HELIX 362 367 FT STRAND 370 373 FT HELIX 380 389 FT HELIX 398 400 FT HELIX 401 421 FT HELIX 427 439 FT HELIX 446 458 FT STRAND 462 471 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 //