ID A0A0D2CSD5_9EURO Unreviewed; 518 AA.
AC A0A0D2CSD5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109};
DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109};
GN ORFNames=PV05_08545 {ECO:0000313|EMBL:KIW52937.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW52937.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW52937.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW52937.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) 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 -!- 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}.
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DR EMBL; KN847321; KIW52937.1; -; Genomic_DNA.
DR RefSeq; XP_013313521.1; XM_013458067.1.
DR AlphaFoldDB; A0A0D2CSD5; -.
DR STRING; 348802.A0A0D2CSD5; -.
DR GeneID; 25330453; -.
DR HOGENOM; CLU_024540_4_0_1; -.
DR OrthoDB; 3013545at2759; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000054342; 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; 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:UP000054342}.
FT DOMAIN 192..503
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
SQ SEQUENCE 518 AA; 57817 MW; 94684A93B7C8E405 CRC64;
MGQGDGLEFK KLGMCGTGSM GGMMSLLYAE HGVEVFYYDP SDENVKKLQQ EATDTGLDKS
IHAQKDYKEM CESLASGNEP KLFVFSIPHG GAGDAVLKDL RPHLQKGDII LDCSNEYWKF
TERRQRELEP DGIHYIGCGV SGGYQSARHG PSMSPGGDAE TLKKVMPFLQ RVAAKDKQGR
ACTTPIGPHG SGHYVKMIHN GIEQGMMSAI AEVWFIMNKC LKMKYEKIAD VFESWNKDGP
LRDNFLVSIG ADINRTKKDD GSFVLSEVRD KVVQDADDSE GTGIWTNEEA IRLHVPAPTI
ASAHMFRCGS ADAASRLAVN KVFNDGVKPA IIKLEVPHEK ALPAFIEELR LALYAAFMCS
FIQGLHILKK MDRQEKWNLD YRKILQIWRG GCIIQSDHIS DVLDSVHARE DHDDDNLLAN
REIAEELGNS FSSLKNVVLK SVEADAYVPS LSATLEYYKY SSSTVLPTQF MEAELDYFGS
HNYEKWEEGP GKPVKGPHHY EWKAAKGLVD EKKKENKL
//
