6PGD_SYNE7
ID 6PGD_SYNE7 Reviewed; 471 AA.
AC P21577; Q31S98;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; OrderedLocusNames=Synpcc7942_0039;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBSTRATE-BINDING SITE.
RX PubMed=2113917; DOI=10.1128/jb.172.7.4023-4031.1990;
RA Broedel S.E. Jr., Wolf R.E. Jr.;
RT "Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain
RT PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase.";
RL J. Bacteriol. 172:4023-4031(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Culler D.C., Krogmann D.W.;
RT "Amino acid sequence comparisons of 6-phosphogluconate dehydrogenase.";
RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; M55002; AAA27330.1; -; Genomic_DNA.
DR EMBL; X58719; CAA41555.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB56071.1; -; Genomic_DNA.
DR PIR; S14628; S14628.
DR RefSeq; WP_011377413.1; NC_007604.1.
DR AlphaFoldDB; P21577; -.
DR SMR; P21577; -.
DR STRING; 1140.Synpcc7942_0039; -.
DR PRIDE; P21577; -.
DR EnsemblBacteria; ABB56071; ABB56071; Synpcc7942_0039.
DR KEGG; syf:Synpcc7942_0039; -.
DR eggNOG; COG0362; Bacteria.
DR HOGENOM; CLU_024540_4_2_3; -.
DR OMA; VIMVKAG; -.
DR OrthoDB; 1245550at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0039-MON; -.
DR UniPathway; UPA00115; UER00410.
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; 1.10.1040.10; -; 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 Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT CHAIN 1..471
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090060"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
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 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 186..187
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 191
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 449
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT CONFLICT 154..159
FT /note="EPIVRS -> SRSVPT (in Ref. 1; AAA27330)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> T (in Ref. 2; CAA41555)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="A -> R (in Ref. 2; CAA41555)"
FT /evidence="ECO:0000305"
FT CONFLICT 415..439
FT /note="AAERGIPVPAFSASLDYFDSYRRDR -> RQNEEFRFRFQCFPGLLRQLPAR
FT S (in Ref. 2; CAA41555)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..441
FT /note="RDRLP -> ASPA (in Ref. 1; AAA27330)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..453
FT /note="DYFG -> TTC (in Ref. 1; AAA27330)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..465
FT /note="ERTDRSGS -> KAPIALL (in Ref. 1; AAA27330)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..470
FT /note="QW -> M (in Ref. 1; AAA27330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 51073 MW; 0C75D58209E124E7 CRC64;
MALQQFGLIG LAVMGENLAL NIERNGFSLT VYNRTAEKTE AFMADRAQGK NIVPAYSLED
FVASLERPRR ILVMVKAGGP VDAVVEQLKP LLDPGDLIID GGNSLFTDTE RRVKDLEALG
LGFMGMGVSG GEEGALNGPS LMPGGTQAAY EAVEPIVRSI AAQVDDGPCV TYIGPGGSGH
YVKMVHNGIE YGDMQLIAEA YDLLKSVAGL NASELHDVFA AWNKTPELDS FLIEITADIF
TKVDDLGTGQ PLVELILDAA GQKGTGRWTV ETALEIGVAI PTIIAAVNAR ILSSIKAERQ
AASEILSGPI TEPFSGDRQA FIDSVRDALY CSKICSYAQG MALLAKASQV YNYGLNLGEL
ARIWKGGCII RAGFLNKIKQ AYDADPTLAN LLLAPEFRQT ILDRQLAWRR VIAIAAERGI
PVPAFSASLD YFDSYRRDRL PQNLTQAQRD YFGAHTYERT DRSGSFHAQW F
