ID 6PGD_STAAC Reviewed; 468 AA. AC Q5HFR2; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=SACOL1554; OS Staphylococcus aureus (strain COL). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COL; RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., RA Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete genome RT analysis of an early methicillin-resistant Staphylococcus aureus strain and RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis RT strain."; RL J. Bacteriol. 187:2426-2438(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000046; AAW36746.1; -; Genomic_DNA. DR RefSeq; WP_000193707.1; NC_002951.2. DR AlphaFoldDB; Q5HFR2; -. DR SMR; Q5HFR2; -. DR KEGG; sac:SACOL1554; -. DR HOGENOM; CLU_024540_4_2_9; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000530; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. 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; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00873; gnd; 1. DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1. DR PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1..468 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090052" 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 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 73..75 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 101 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 101 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 127..129 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 444 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 450 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" SQ SEQUENCE 468 AA; 51803 MW; 61A5C2CAF3CCD011 CRC64; MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE //