6PGD_BUCAP
ID 6PGD_BUCAP Reviewed; 473 AA.
AC Q9ZHD9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; OrderedLocusNames=BUsg_100;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9767718; DOI=10.1007/s002849900392;
RA Clark M.A., Baumann L., Baumann P.;
RT "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes
RT of histidine biosynthesis.";
RL Curr. Microbiol. 37:356-358(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF067228; AAC97362.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67670.1; -; Genomic_DNA.
DR RefSeq; WP_011053636.1; NC_004061.1.
DR AlphaFoldDB; Q9ZHD9; -.
DR SMR; Q9ZHD9; -.
DR STRING; 198804.BUsg_100; -.
DR EnsemblBacteria; AAM67670; AAM67670; BUsg_100.
DR KEGG; bas:BUsg_100; -.
DR eggNOG; COG0362; Bacteria.
DR HOGENOM; CLU_024540_4_2_6; -.
DR OMA; VIMVKAG; -.
DR OrthoDB; 1245550at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR GO; GO:0006098; P:pentose-phosphate shunt; ISS: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 3: Inferred from homology;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT CHAIN 1..473
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090029"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 74..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 128..130
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT CONFLICT 158
FT /note="K -> N (in Ref. 1; AAC97362)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..326
FT /note="RRA -> TKS (in Ref. 1; AAC97362)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="K -> I (in Ref. 1; AAC97362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53805 MW; A11842A037E1E984 CRC64;
MLKQQVGVIG MAVMGRNLAL NIESKKYTVS IFNRTQSVTE EVINNNKEKK IFPYFSIKDF
VNSLRKPRCI LLMVKSGQPT DETIQFILPY LNKGDILIDG GNTFYKDSIR RSNDLMKCGI
NFIGMGVSGG ELGALNGPSI MPGGSREAYD LVSSMLKKIS AKFKNEPCVS YIGPNGAGHY
VKMIHNGIEY GDMQLISESY FILKNVLNMK NEELSNTFSQ WNKGELNSYL IEITKNIFLK
KEKDGIHYLI DSILDHAEDK GTGKWISQDA LELHEPLSLI TESVFARYLS SLKDQRLIAS
KILKGPILKC ISSQNKELFV EEVRRALYLG KIISYAQGFS QLKKASEKYS WNLQYGKIAK
IFRAGCIIRA DFLERITDAF KSNNVTNLLL TPYFSEISNK YEKSLRYITS YAIKYGIPVP
TFASAISYYD NYRTMSSSAN LIQAQRDYFG AHTYRRTDKK GYFHTNWLTK KEL
