ID 6PGD_LACLA Reviewed; 472 AA. AC Q9CHU6; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 16-JUN-2009, entry version 55. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=LL0622; ORFNames=L0046; OS Lactococcus lactis subsp. lactis (Streptococcus lactis). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus. OX NCBI_TaxID=1360; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403; RX MEDLINE=21235186; PubMed=11337471; DOI=10.1101/gr.GR-1697R; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(2001). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006295; AAK04720.1; -; Genomic_DNA. DR PIR; F86702; F86702. DR RefSeq; NP_266778.1; -. DR HSSP; P00349; 2PGD. DR SMR; Q9CHU6; 1-469. DR GeneID; 1114242; -. DR GenomeReviews; AE005176_GR; LL0622. DR KEGG; lla:L0046; -. DR NMPDR; fig|272623.1.peg.637; -. DR HOGENOM; Q9CHU6; -. DR OMA; Q9CHU6; PRKVMLM. DR BioCyc; LLAC272623:L0046-MON; -. DR BRENDA; 1.1.1.44; 278870. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:EC. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW. DR InterPro; IPR006183; 6-phosphogluconate_DH. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NAD-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 472 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090045. SQ SEQUENCE 472 AA; 52424 MW; 6EF4F504F217E55F CRC64; MAQANFGVVG MAVMGKNLAL NVESRGYTVA IYNRTTSKTE EVYKEHQDKN LVLTKTLEEF VGSLEKPRRI MLMVQAGAAT DATIKSLLPL LDKGDILIDG GNTHFPDTMR RNAELADSGI NFIGTGVSGG EKGALLGPSM MPGGQKEAYD LVAPIFEQIA AKAPQDGKPC VAYMGANGAG HYVKMVHNGI EYGDMQLIAE SYDLLKRVLG LSNAEIQAIF EEWNEGELDS YLIEITKEVL KRKDDEGEGY IVDKILDKAG NKGTGKWTSE SALDLGVPLP LITESVFARY ISTYKDERVK ASKVLSGPAV NFSGDKKEVI EKIRKALYFS KIMSYAQGFA QLRKASEEFD WDLPYGTIAQ IWRAGCIIRA EFLQNITDAF DKDSELENLL LDDYFVDITK RYQEAVRDVV SLAVQAGIPI PTFTSAISYY DSYRSENLPA NLIQAQRDYF GAHTYERTDK AGIFHYDWYT ED //