6PGD_PSEVU
ID 6PGD_PSEVU Reviewed; 445 AA.
AC P41574;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
DE Flags: Fragment;
GN Name=gnd;
OS Pseudescherichia vulneris (Escherichia vulneris).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pseudescherichia.
OX NCBI_TaxID=566;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33821 / DSM 4564 / JCM 1688 / BCRC 15953 / CCUG 15715 / LMG
RC 7868 / NBRC 102420 / NCTC 12130 / CDC 875-72 / NIH 580;
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; U14465; AAC43815.1; -; Genomic_DNA.
DR AlphaFoldDB; P41574; -.
DR SMR; P41574; -.
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_0000090039"
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; 48806 MW; 0315BE126C2A45FE CRC64;
AVMGRNLALN IESRGYTVSV FNRSREKTEE VVAENPGKKL VPYYTVQEFV ESLETPRRIL
LMVQAGAGTD AAINSLKPYL DKGDIIIDGG NTFFHDTIRR NRELSAEGFN FIGTGVSGGE
EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY
GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNKGELSSYL IDITKDIFTK KDEEGKYLVD
VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKEQRVAASK VLSGPQSQPA
GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL
QKITDAYAET PAIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF GAAVAYYDSY
RAAVLPANLI QAQRDYFGAH TYKRT
