ID K0ID35_NITGG Unreviewed; 311 AA.
AC K0ID35;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000313|EMBL:AFU57575.1};
DE EC=1.1.1.44 {ECO:0000313|EMBL:AFU57575.1};
GN Name=gnd1 {ECO:0000313|EMBL:AFU57575.1};
GN OrderedLocusNames=Ngar_c06320 {ECO:0000313|EMBL:AFU57575.1};
OS Nitrososphaera gargensis (strain Ga9.2).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU57575.1, ECO:0000313|Proteomes:UP000008037};
RN [1] {ECO:0000313|EMBL:AFU57575.1, ECO:0000313|Proteomes:UP000008037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA Spieck E., Streit W., Wagner M.;
RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT insights into metabolic versatility and environmental adaptations.";
RL Environ. Microbiol. 14:3122-45(2012).
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CP002408; AFU57575.1; -; Genomic_DNA.
DR AlphaFoldDB; K0ID35; -.
DR STRING; 1237085.Ngar_c06320; -.
DR KEGG; nga:Ngar_c06320; -.
DR PATRIC; fig|1237085.11.peg.609; -.
DR HOGENOM; CLU_024540_0_0_2; -.
DR InParanoid; K0ID35; -.
DR OrthoDB; 23890at2157; -.
DR Proteomes; UP000008037; 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:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR004849; 6DGDH_YqeC.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR NCBIfam; TIGR00872; gnd_rel; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF67; 6-PHOSPHOGLUCONATE DEHYDROGENASE YQEC-RELATED; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
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 Oxidoreductase {ECO:0000313|EMBL:AFU57575.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008037}.
FT DOMAIN 4..152
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 166..277
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00393"
SQ SEQUENCE 311 AA; 34514 MW; D0BA61D446D013E5 CRC64;
MRQLGIVGLG KMGGNLAMQA HEKKIDVIGK ARKSKPELEK QGIRVVTDYD SFARHLKQPR
VVYLSLPAGP TVDTVLDELA AYLAKGDVVM DGGNSFYLDS IEREKRMWEK GIYFLDCGTS
GGLEGARYGA CFMVGGRQEG VRIAEPLLTA LSVKDGYVHT GQPGSGHFVK LVHNGIEFGM
LQSIGEGVEL LRKSDFRLDL QKIFKNWSNG SVIRGWLVEL MERGLREQGI DKVESYVEDT
GEVNWLVQDA VSKEIPIPII SQAVMELFKS RMSESNAYKA IALMRHGFGG HPFGKDKDIA
EERKTSRVHK V
//
