6PGD_TRYBB
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 03-AUG-2022, entry version 119.
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}.
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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; 1.10.1040.10; -; 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; IPR006184; 6PGdom_BS.
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.
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
