ID K2RRS5_MACPH Unreviewed; 466 AA.
AC K2RRS5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109};
DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109};
GN ORFNames=MPH_09926 {ECO:0000313|EMBL:EKG12934.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG12934.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG12934.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG12934.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG12934.1}.
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DR EMBL; AHHD01000422; EKG12934.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RRS5; -.
DR STRING; 1126212.K2RRS5; -.
DR VEuPathDB; FungiDB:MPH_09926; -.
DR eggNOG; KOG2653; Eukaryota.
DR HOGENOM; CLU_024540_4_0_1; -.
DR InParanoid; K2RRS5; -.
DR OrthoDB; 3013545at2759; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000007129; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
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.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW NADP {ECO:0000256|PIRNR:PIRNR000109};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|PIRNR:PIRNR000109};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 147..459
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT REGION 441..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
SQ SEQUENCE 466 AA; 51128 MW; FD69C0420DA819B9 CRC64;
MDSIVEQANQ ADTIPDGAVR KYSDYASLCS SLDSPKVFVF SLPHGSVGDS VLGGLMPYLD
KGDIIIDAGN ENWQNTERRQ SKCYTRGVRY IGMGVSGGYQ AARQGPSMCP GGDDESLDLV
MPLLKKVAAK DRKGVPCVGK AGTGGSGHYV KMIHNGIEHG MISAVSEAYD LMKKGLGMNN
DEIADVFEQW NKEGELQGTF LIWISADICR AKDKSRNDEY VLDTVEDKVV QDITGEEGTG
IWSNEQAVSY HIPAPTLTTA HYLRLASADR NQRIRAQETI GVEFTPRSLN LSGESKQDFL
EALRRATYAA FLASYIQGIN IIERADRANH WNIDYSAVLQ IWAAGCIIQA DHIASLLHPI
LTNHRALDTI NLLFQPSAMS ELKACVASLR DVVVKATTTD HVIPALSASL EYVKYQTSTN
LPTSFSEAQL DYFGAHMYDR KGEEGTGAPS EGKHHFEWKP ARSSKL
//
