6PGD_SHEEP
ID 6PGD_SHEEP Reviewed; 483 AA.
AC P00349;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=PGD;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1471978; DOI=10.1042/bj2881061;
RA Somers D.O., Medd S.M., Walker J.E., Adams M.J.;
RT "Sheep 6-phosphogluconate dehydrogenase. Revised protein sequence based
RT upon the sequences of cDNA clones obtained with the polymerase chain
RT reaction.";
RL Biochem. J. 288:1061-1067(1992).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-483, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC TISSUE=Liver;
RX PubMed=6685125; DOI=10.1016/s0021-9258(17)44055-5;
RA Carne A., Walker J.E.;
RT "Amino acid sequence of ovine 6-phosphogluconate dehydrogenase.";
RL J. Biol. Chem. 258:12895-12906(1983).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=6641716; DOI=10.1002/j.1460-2075.1983.tb01535.x;
RA Adams M.J., Archibald I.G., Bugg C.E., Carne A., Gover S., Helliwell J.R.,
RA Pickersgill R.W., White S.W.;
RT "The three dimensional structure of sheep liver 6-phosphogluconate
RT dehydrogenase at 2.6-A resolution.";
RL EMBO J. 2:1009-1014(1983).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1793548; DOI=10.1107/s0108768191010315;
RA Adams M.J., Gover S., Leaback R., Phillips C., Somers D.O.;
RT "The structure of 6-phosphogluconate dehydrogenase refined at 2.5-A
RT resolution.";
RL Acta Crystallogr. B 47:817-820(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-483 IN COMPLEXES WITH NADP AND
RP SUBSTRATE, AND SUBUNIT.
RX PubMed=7922042; DOI=10.1016/s0969-2126(00)00066-6;
RA Adams M.J., Ellis G.H., Gover S., Naylor C.E., Phillips C.;
RT "Crystallographic study of coenzyme, coenzyme analogue and substrate
RT binding in 6-phosphogluconate dehydrogenase: implications for NADP
RT specificity and the enzyme mechanism.";
RL Structure 2:651-668(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-483, AND SUBUNIT.
RX PubMed=15299295; DOI=10.1107/s0907444994012229;
RA Phillips C., Gover S., Adams M.J.;
RT "Structure of 6-phosphogluconate dehydrogenase refined at 2-A resolution.";
RL Acta Crystallogr. D 51:290-304(1995).
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.
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:15299295,
CC ECO:0000269|PubMed:7922042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=Incorrect CNBR peptide order. Many sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; X60195; CAA42751.1; -; mRNA.
DR PIR; S15280; S15280.
DR PIR; S27359; DESHGC.
DR RefSeq; NP_001009467.1; NM_001009467.2.
DR PDB; 1PGN; X-ray; 2.30 A; A=2-483.
DR PDB; 1PGO; X-ray; 2.50 A; A=2-483.
DR PDB; 1PGP; X-ray; 2.50 A; A=2-483.
DR PDB; 1PGQ; X-ray; 3.17 A; A=2-483.
DR PDB; 2PGD; X-ray; 2.00 A; A=2-483.
DR PDBsum; 1PGN; -.
DR PDBsum; 1PGO; -.
DR PDBsum; 1PGP; -.
DR PDBsum; 1PGQ; -.
DR PDBsum; 2PGD; -.
DR AlphaFoldDB; P00349; -.
DR SMR; P00349; -.
DR STRING; 9940.ENSOARP00000005726; -.
DR BindingDB; P00349; -.
DR ChEMBL; CHEMBL1169597; -.
DR GeneID; 443541; -.
DR KEGG; oas:443541; -.
DR CTD; 5226; -.
DR eggNOG; KOG2653; Eukaryota.
DR OrthoDB; 847823at2759; -.
DR BRENDA; 1.1.1.44; 2668.
DR SABIO-RK; P00349; -.
DR UniPathway; UPA00115; UER00410.
DR EvolutionaryTrace; P00349; -.
DR PRO; PR:P00349; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IDA:UniProtKB.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6685125"
FT CHAIN 2..483
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090066"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT ACT_SITE 191
FT /note="Proton donor"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 103
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 129
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 131
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 187..188
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 192
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 288
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 447
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 478..481
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD0"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD0"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD0"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:2PGD"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2PGD"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:2PGD"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1PGN"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1PGN"
FT HELIX 179..207
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:2PGD"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 316..349
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 393..416
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:2PGD"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:2PGD"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:2PGD"
SQ SEQUENCE 483 AA; 52970 MW; F4AC5DB414385F11 CRC64;
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVLGAHSLEE
MVSKLKKPRR IILLVKAGQA VDNFIEKLVP LLDIGDIIID GGNSEYRDTM RRCRDLKDKG
ILFVGSGVSG GEDGARYGPS LMPGGNKEAW PHIKAIFQGI AAKVGTGEPC CDWVGDDGAG
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG LGHKEMAKAF EEWNKTELDS FLIEITASIL
KFQDADGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA
SKKLKGPQNI PFEGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL
MWRGGCIIRS VFLGKIKDAF DRNPGLQNLL LDDFFKSAVE NCQDSWRRAI STGVQAGIPM
PCFTTALSFY DGYRHAMLPA NLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGSVSSSS
YNA
