ID X4ZJW5_9BACL Unreviewed; 466 AA.
AC X4ZJW5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=PSAB_10300 {ECO:0000313|EMBL:AHV96990.1};
OS Paenibacillus sabinae T27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV96990.1, ECO:0000313|Proteomes:UP000019772};
RN [1] {ECO:0000313|EMBL:AHV96990.1, ECO:0000313|Proteomes:UP000019772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T27 {ECO:0000313|EMBL:AHV96990.1,
RC ECO:0000313|Proteomes:UP000019772};
RX PubMed=24651173;
RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA Chen X., Cheng Q., Chen S., Li J.;
RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT Genes.";
RL PLoS Genet. 10:E1004231-E1004231(2014).
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|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|PIRNR:PIRNR000109, 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}.
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DR EMBL; CP004078; AHV96990.1; -; Genomic_DNA.
DR RefSeq; WP_025334528.1; NZ_CP004078.1.
DR AlphaFoldDB; X4ZJW5; -.
DR STRING; 1268072.PSAB_10300; -.
DR KEGG; psab:PSAB_10300; -.
DR PATRIC; fig|1268072.3.peg.2149; -.
DR eggNOG; COG0362; Bacteria.
DR HOGENOM; CLU_024540_4_2_9; -.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000019772; Chromosome.
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; 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|PIRNR:PIRNR000109,
KW ECO:0000256|RuleBase:RU000485}.
FT DOMAIN 178..466
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 189
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 74..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 102
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 128..130
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 185..186
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 190
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 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 451
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ SEQUENCE 466 AA; 51291 MW; 0FC8CADCEB429A1D CRC64;
MSKQQVGVVG LAVMGKNLAL NIAGHGYSVA VYNRSKEKTD LLLAEAGEKD IRGAYTLQDL
AETLERPRKI LLMVKAGQPV DEAIAQLLPY LEPGDVLVDG GNSFYKDTIR RSRELEDRGI
YFVGTGISGG EEGALKGPSI MPGGNYEAYQ LIAPILNDIS AKVEGEPCCT YTGGDGAGHF
VKMVHNGIEY ADMQLIGEAY VLMQRLLGLS PADIRQAFTE WNEGELNSYL IEITADIFGK
TDPDTGQYLV DVILDSAGQK GTGKWTSQNA LDIGTPVPTI TAAVFERYLS ALKEERVTAS
KAFSDPAPRE AEIPAGFIES IRRALYVSKI CAYAQGFSLL AKASKEYNWN LDLGSIAMIF
RGGCIIRAQF LNKIKQAYDH NPDLTNLLLD DYFQHIIGQY QQDWRDTVMA AVGQGISVPA
FASAISYFDS YRTERLPANL LQAQRDYFGA HTYERTDKEG IFHTEW
//
