6PGD_CITKO
ID 6PGD_CITKO Reviewed; 445 AA.
AC P41582;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
DE Flags: Fragment;
GN Name=gnd;
OS Citrobacter koseri (Citrobacter diversus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=545;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CT19, CT27, CT4, CT42, CT45, and CT9;
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; U14424; AAC43774.1; -; Genomic_DNA.
DR EMBL; U14425; AAC43775.1; -; Genomic_DNA.
DR EMBL; U14427; AAC43776.1; -; Genomic_DNA.
DR EMBL; U14428; AAC43777.1; -; Genomic_DNA.
DR EMBL; U14429; AAC43778.1; -; Genomic_DNA.
DR EMBL; U14432; AAC43779.1; -; Genomic_DNA.
DR PIR; I40681; I40681.
DR PIR; I40682; I40682.
DR PIR; I40684; I40684.
DR PIR; I40685; I40685.
DR AlphaFoldDB; P41582; -.
DR SMR; P41582; -.
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_0000090035"
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 VARIANT 31
FT /note="V -> G (in strain: CT45)"
FT VARIANT 206
FT /note="E -> D (in strain: CT42)"
FT VARIANT 300
FT /note="A -> E (in strain: CT27)"
FT NON_TER 1
FT NON_TER 445
SQ SEQUENCE 445 AA; 48829 MW; 9DB96925EC40EDC4 CRC64;
AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPYYTVKEFV ESLETPRRIL
LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE
EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY
GDMQLIAEAY SLLKGGLNLS NEELAETFTE WNKGELNSYL IDITKDIFTK KDEEGKYLVD
VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKEQRVAASK VLSGPKAQLA
GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASDEYNWDL NYGEIAKIFR AGCIIRAQFL
QKITDAYAEN AGIANLLLAP YFKKIADDYQ QALRDVVAYA VQNGIPVPTF SAAVAYYDSY
RAAVLPANLI QAQRDYFGAH TYKRT
