ID B2NIW2_CYAPA Unreviewed; 439 AA.
AC B2NIW2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
DE Flags: Fragment;
GN Name=gnd {ECO:0000313|EMBL:BAG32444.1};
OS Cyanophora paradoxa.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762 {ECO:0000313|EMBL:BAG32444.1};
RN [1] {ECO:0000313|EMBL:BAG32444.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIES-547 {ECO:0000313|EMBL:BAG32444.1};
RX PubMed=18485228; DOI=10.1186/1471-2148-8-151;
RA Maruyama S., Misawa K., Iseki M., Watanabe M., Nozaki H.;
RT "Origins of a cyanobacterial 6-phosphogluconate dehydrogenase in plastid-
RT lacking eukaryotes.";
RL BMC Evol. Biol. 8:151-151(2008).
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:0000256|ARBA:ARBA00002526}.
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 Evidence={ECO:0000256|RuleBase:RU000485};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000256|ARBA:ARBA00004874, ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|RuleBase:RU000485}.
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DR EMBL; AB425331; BAG32444.1; -; mRNA.
DR AlphaFoldDB; B2NIW2; -.
DR BRENDA; 1.1.1.44; 1772.
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:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485}; NADP {ECO:0000256|RuleBase:RU000485};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000485,
KW ECO:0000313|EMBL:BAG32444.1};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU000485}.
FT DOMAIN 170..439
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAG32444.1"
FT NON_TER 439
FT /evidence="ECO:0000313|EMBL:BAG32444.1"
SQ SEQUENCE 439 AA; 47336 MW; 077943D6D74C03C6 CRC64;
AVMGQNLALN IAEEGLPISV FNRSPDKVDD TVARAAREGN LPLTGFKNVK EFVDSIEKPR
SIIILVKAGA PVDATISALS EHLEEGDLII DGGNEWYENT ERRAAECAKR GINYMGMGVS
GGEEGARNGP SLMPGGPKDA YDRIKPILDK VAAQVDDGPC VTYIGPGGAG NYVKMIHNGI
EYGDMQLIGE AYDILKTVGG LSNAELKAVF EDWNKGELQS FLVEITTKIF GKKDDLAEGD
LVDKIVDRTG SKGTGKWTIQ QAAELGIAAP TMAAALDSRY ISSLKDERIA ASSVLASATS
LSPVDKAKLI DDVRKALYAS KICSYAQGMN LIKAASDVNG WNLDLGAIAR IWKGGCIIRA
VFLDRIKQAY DRDAALPSLL VDKEFAKELS ERSEAWRRIV SLSIQAGITA PAFSASLAYF
DSYRRARLPA NLIQAQRDF
//
