ID   6PGD_TREPA              Reviewed;         488 AA.
AC   O83351;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; OrderedLocusNames=TP_0331;
OS   Treponema pallidum.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
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.
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DR   EMBL; AE000520; AAC65319.1; -; Genomic_DNA.
DR   PIR; A71337; A71337.
DR   RefSeq; NP_218771.1; -.
DR   HSSP; P00349; 2PGD.
DR   GeneID; 2611604; -.
DR   GenomeReviews; AE000520_GR; TP_0331.
DR   KEGG; tpa:TP0331; -.
DR   NMPDR; fig|243276.1.peg.330; -.
DR   TIGR; TP_0331; -.
DR   HOGENOM; O83351; -.
DR   OMA; O83351; HTFRVLP.
DR   BioCyc; TPAL243276:TP_0331-MON; -.
DR   BRENDA; 1.1.1.44; 142600.
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    488       6-phosphogluconate dehydrogenase,
FT                                decarboxylating.
FT                                /FTId=PRO_0000090062.
SQ   SEQUENCE   488 AA;  52767 MW;  FB69CCCA98DEE6B5 CRC64;
     MGADIGFIGL AVMGENLVLN IERNGFSVAV FNRTTTVVDR FLAGRAHGKR ITGAHSIAEL
     VSLLARPRKI MLMVKAGSAV DAVIDQILPL LEKGDLVIDG GNSHYQDTIR RMHALEAAGI
     HFIGTGVSGG EEGALRGPSL MPGGSAQAWP LVSPIFCAIA AKADDGTPCC DWVGSDGAGH
     YVKMIHNGIE YGDMQIIAEG YWFMKHALGM SYEHMHHTFT RWNTGRLHSY LIEITAAILA
     HQDTDGTPLL EKILDAAGQK GTGRWTCVAA LEEGSPLTLI TESVMARSLS AQKQARCKAH
     RVFGSPVKVS KAETLSAQQR EELVSALEDA LYCAKIVSYA QGFELLSHTA KRRGWTLDFS
     RIASLWRGGC IIRSGFLSKI SAAFAQQHDL ENLVLAPFFA EELKRACPGW RTIVAESVRQ
     ALPVPALSAA LAWFDGFTGA ALPANLLQAQ RDYFGAHTYE RTDAPRGEFF HTNWTGTGGD
     TIAGTYSI
//