6PGD_SHISO
ID 6PGD_SHISO Reviewed; 445 AA.
AC P41580;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
DE Flags: Fragment;
GN Name=gnd;
OS Shigella sonnei.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29930 / DSM 5570 / NCTC 12984;
RX 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 -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC to NADPH. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U14470; AAC43835.1; -; Genomic_DNA.
DR EMBL; U14440; AAC43790.1; -; Genomic_DNA.
DR AlphaFoldDB; P41580; -.
DR SMR; P41580; -.
DR STRING; 216599.GCA_000283715_02386; -.
DR UniPathway; UPA00115; UER00410.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR PANTHER; PTHR11811; PTHR11811; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090051"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 1..4
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 22..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 63..65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 117..119
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 175..176
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 445
SQ SEQUENCE 445 AA; 48824 MW; 07F8D753DBB0366E CRC64;
AVMGRNLALN IESRGYTVSI FNRSREKTEE VIAENPGKKL VPYYTVKEFV ESLETPRRIL
LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE
EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY
GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNNGELSSYL IDITKDIFTK KDEDGNYLVD
VILDEAANKG TGKWTSQSAL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLSGPQAQSA
GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL
QKITDAYAEN PQIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF AAAVAYYDSY
RAAVLPANLI QAQRDYFGAH TYKRI
