ID A0A0N4TSV1_BRUPA Unreviewed; 472 AA.
AC A0A0N4TSV1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN ORFNames=BPAG_LOCUS11752 {ECO:0000313|EMBL:VDN92938.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001179001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0001179001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN92938.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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:0000256|ARBA:ARBA00002526,
CC ECO:0000256|PIRNR:PIRNR000109}.
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|PIRNR:PIRNR000109,
CC 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|PIRNR:PIRNR000109,
CC ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000109}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109,
CC ECO:0000256|RuleBase:RU000485}.
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; UZAD01013247; VDN92938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4TSV1; -.
DR STRING; 6280.A0A0N4TSV1; -.
DR WBParaSite; BPAG_0001179001-mRNA-1; BPAG_0001179001-mRNA-1; BPAG_0001179001.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
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; 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 {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485};
KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109,
KW ECO:0000256|RuleBase:RU000485};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|PIRNR:PIRNR000109};
KW Reference proteome {ECO:0000313|Proteomes:UP000278627}.
FT DOMAIN 179..459
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 103
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 129..131
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 186..187
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 191
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 260
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 287
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 436
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 442
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ SEQUENCE 472 AA; 51635 MW; 80C18A1C3A49DC2B CRC64;
MDKADIAVIG LAVMGQNLIL NMLEKGFVVC VYNRTVSKVD DFLANEGKGL RALGAHSLSE
LAEVLKKPRR IMLMVKAGQP VDAMISSILP FLDKGDIIID GGNSEYTDTA RRCTELKEKN
IRFVGCGVSG GEEGARHGPS LMPGGSAEAW PYIKDIFQAI AAKVDNEPCC DWVGENGAGH
FVKMVHNGIE YGDMQLIAEA YSLLKDGADL THDEMAEVFA EWNKGALDSY LIEITSHILK
FKDENKQTLL PNIRDAAGQK GTGKWTGIVA LNYGIPLTLI GEAVFARCLS SLKDDRLAAA
KVLPGPNPDK AVIQALYASK IISYAQGFML LAEANRVFKW NLNFGSIALM WRGGCIIRSR
FLGEIKKAYD TNPKLSNLLM DSFFLNAIRK CQESWRIISA AGILLGIPTP AFSTALAFYD
GFRCKVLPAN LIQAQRDYFG AHMYELMDKP GTFLHTNWTG TGGNVTSTAY IQ
//
