ID   A0A087BSU1_9BIFI        Unreviewed;       297 AA.
AC   A0A087BSU1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN   ORFNames=BMON_1907 {ECO:0000313|EMBL:KFI74091.1};
OS   Bifidobacterium mongoliense DSM 21395.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI74091.1, ECO:0000313|Proteomes:UP000029082};
RN   [1] {ECO:0000313|EMBL:KFI74091.1, ECO:0000313|Proteomes:UP000029082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI74091.1,
RC   ECO:0000313|Proteomes:UP000029082};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000485}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|RuleBase:RU000485}.
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:KFI74091.1}.
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DR   EMBL; JGZE01000029; KFI74091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087BSU1; -.
DR   STRING; 1437603.GCA_000771525_01684; -.
DR   eggNOG; COG0362; Bacteria.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000029082; 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:0016054; P:organic acid catabolic process; IEA:UniProt.
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   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   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   ECO:0000256|RuleBase:RU000485}; NADP {ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000485,
KW   ECO:0000313|EMBL:KFI74091.1};
KW   Pentose shunt {ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029082}.
FT   DOMAIN          181..297
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
SQ   SEQUENCE   297 AA;  31690 MW;  F73309F43B3BB806 CRC64;
     MAEGTANIGV VGLAAMGSNL ARNLAHHGNT VALYNRHYER TEKLMAEHGD EGSFVPSRTV
     EEFVASLARP RTAIILVKAG APTDAVIGEL ADAMEPGDII VDGGNSYFKD TIRREKEIRA
     RGLHYVGCGV SGGEEGALNG PSLMPGGTDE SWRTLGPILK SIAAVAEGEP CVTHIGKDGA
     GHFVKMVHNG IEYADMQLIA ESYDLMRRGL GMEPGEIADV FAQWNTTELN SYLIEITAEV
     LRQKDDKTGK PLVDVIVDHA GMKGTGTWTV QTALSLATPV TGIAEAVFAR GLSSRYR
//