ID   6PGD_CITAM              Reviewed;         445 AA.
AC   P41581;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
DE   Flags: Fragment;
GN   Name=gnd;
OS   Citrobacter amalonaticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=35703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CT28;
RX   MEDLINE=95024018; PubMed=7937867; DOI=10.1073/pnas.91.21.10227;
RA   Nelson K., Selander R.K.;
RT   "Intergeneric transfer and recombination of the 6-phosphogluconate
RT   dehydrogenase gene (gnd) in enteric bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994).
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; U14426; AAC43773.1; -; Genomic_DNA.
DR   PIR; I40629; I40629.
DR   HSSP; P00349; 2PGD.
DR   BRENDA; 1.1.1.44; 3850.
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   Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT   CHAIN        <1   >445       6-phosphogluconate dehydrogenase,
FT                                decarboxylating.
FT                                /FTId=PRO_0000090034.
FT   NON_TER       1      1
FT   NON_TER     445    445
SQ   SEQUENCE   445 AA;  48887 MW;  A3771DFC9678EEF1 CRC64;
     AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPYYTVQEFV ESLETPRRIL
     LMVKAGAGTD SAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSEEGFN FIGTGVSGGE
     EGALKGPSIM PGGQKEAYEL VAPILKQIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY
     GDMQLIAEAY SLLKGGLNLS NEELATTFSE WNKGELSSYL IDITKDIFTK KDEEGKYLVD
     VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKTQRVAASK VLTGPQAQPA
     GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASDEYNWDL NYGEIAKIFR AGCIIRAQFL
     QKITDAYAEN PAIANLLLAP YFKQIADDYQ QALRDVVSYA VQNGIPVPTF SAAVAYYDSY
     RAAVLPANLI QAQRDYFGAH TYKRT
//