ID A1AR86_PELPD Unreviewed; 341 AA.
AC A1AR86;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=6-phosphogluconate dehydrogenase (Decarboxylating) {ECO:0000313|EMBL:ABK99856.1};
DE EC=1.1.1.44 {ECO:0000313|EMBL:ABK99856.1};
GN OrderedLocusNames=Ppro_2249 {ECO:0000313|EMBL:ABK99856.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99856.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK99856.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CP000482; ABK99856.1; -; Genomic_DNA.
DR RefSeq; WP_011736116.1; NC_008609.1.
DR AlphaFoldDB; A1AR86; -.
DR STRING; 338966.Ppro_2249; -.
DR KEGG; ppd:Ppro_2249; -.
DR eggNOG; COG1023; Bacteria.
DR HOGENOM; CLU_024540_0_0_7; -.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000006732; 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; 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; 2.
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 Oxidoreductase {ECO:0000313|EMBL:ABK99856.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732}.
FT DOMAIN 184..332
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 36721 MW; 8AF4886C0DC1DEFD CRC64;
MRMGMIGVGR MGGDMVRRLL KGGHECVVHA RRPSSMEPLV REGALGAAPL AELVSLLPKP
RVVWLMIPAA SVDRVIADIA PLLDAGDILI DGGNSHYHDD IRRCDELRDR SIHYLDVGTS
GGVWGLERGY CLMIGGEREA VQYLDPLFAT LAPGRGAAPD SPGRSDSGSS AERGYLHCGP
SGAGHFVKMV HNGIEYGMMA AYAEGFNILA HANIGSQERE TDAETTPLRD PRHFRFELNL
ADIAELWRRG SVVSSWLLDL TARALAAGQG LERFSGQVSD SGEGRWTVAT AIEAGVPAPV
LATALFQRFS SRGEADFADR LLSAMRYEFG GHHEKSTSGE G
//
