6PGD_BUCBP
ID 6PGD_BUCBP Reviewed; 468 AA.
AC Q89AX5;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; OrderedLocusNames=bbp_101;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26836.1; -; Genomic_DNA.
DR RefSeq; WP_011091237.1; NC_004545.1.
DR AlphaFoldDB; Q89AX5; -.
DR SMR; Q89AX5; -.
DR STRING; 224915.bbp_101; -.
DR EnsemblBacteria; AAO26836; AAO26836; bbp_101.
DR GeneID; 56470645; -.
DR KEGG; bab:bbp_101; -.
DR eggNOG; COG0362; Bacteria.
DR HOGENOM; CLU_024540_4_2_6; -.
DR OMA; VIMVKAG; -.
DR OrthoDB; 1245550at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000000601; 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;
KW Reference proteome.
FT CHAIN 1..468
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090030"
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 259
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 52646 MW; C28B8C09CCB64E11 CRC64;
MAKQQIGVIG MAVMGRNLAL NMERNQYTVS IFNRSLDITE KIILNNPNKN LFPFFSIKDF
VLSLIVPRCI VLMIKSGVAT DDTIKSLIPY LSKGDIIIDG GNTFYKDTIQ RGYELLKIGV
NLIGAGFSGG EKGALYGPSI MPGGRQEAYN YVSPILKKIA SNSEGIPCVT YIGPDGSGHY
VKMVHNGIEY GDMQLIAESY FILKTLLRLD NQSISKIFDI WNQGELNSYL IDITKDILIK
KDDQNNYLID CILDEGSSKG TGTWTTKSAL DLNEPLTLIT ESVFFRYLSS LKSQRLLASK
ILCGPKDFFI VLNRDDFIEK IRQALYLGKI ISYAQGFSQL NSASQKYNWN LKLGEISRIF
QSGCIIRAKL LKNITQEYSS NNNFVNLLLT PYFREIANTY HSSLREIVSI SVKYGIPIPA
LSSAISYFDS YRSAFLPSNL IQAQRDFFGA HTYKRIDKSG IFHTNWYS
