ID Q762L5_KLEPN Unreviewed; 468 AA.
AC Q762L5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|ARBA:ARBA00018193, ECO:0000256|PIRNR:PIRNR000109};
DE EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011, ECO:0000256|PIRNR:PIRNR000109};
GN Name=gnd {ECO:0000313|EMBL:AAV27335.1};
GN Synonyms=gndA {ECO:0000313|EMBL:MDH8290697.1};
GN ORFNames=HJX03_08615 {ECO:0000313|EMBL:QJL28622.1}, NCTC9601_02223
GN {ECO:0000313|EMBL:SPX55056.1}, NCTC9645_00003
GN {ECO:0000313|EMBL:SPX50509.1}, QIG75_19150
GN {ECO:0000313|EMBL:MDH8290697.1}, SAMEA4364603_01170
GN {ECO:0000313|EMBL:SSK25472.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:BAD03943.1};
RN [1] {ECO:0000313|EMBL:BAD03943.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NTUH-K2044 {ECO:0000313|EMBL:BAD03943.1};
RA Fang C., Lai S., Chuang Y., Wang J.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAD03943.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NTUH-K2044 {ECO:0000313|EMBL:BAD03943.1};
RA Fang C.-T., Chuang Y.-P., Shun C.-T., Chang S.-C., Wang J.-T.;
RT "A novel virulence gene in Klebsiella pneumoniae strains causing primary
RT liver abscess and septic metastatic complications.";
RL J. Exp. Med. 199:697-705(2004).
RN [3] {ECO:0000313|EMBL:AAV27335.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DTS {ECO:0000313|EMBL:AAV27335.1};
RA Chang J.C., Yeh K.M., Chang F.Y., Fung C.P., Siu L.K.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:BAD86781.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NTUH-K2044 {ECO:0000313|EMBL:BAD86781.1};
RA Chuang Y., Fang C., Lai S., Wang J.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BAD86781.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NTUH-K2044 {ECO:0000313|EMBL:BAD86781.1};
RX PubMed=16453259; DOI=10.1086/499968;
RA Chuang Y.P., Fang C.T., Lai S.Y., Chang S.C., Wang J.T.;
RT "Genetic determinants of capsular serotype K1 of Klebsiella pneumoniae
RT causing primary pyogenic liver abscess.";
RL J. Infect. Dis. 193:645-654(2006).
RN [6] {ECO:0000313|EMBL:AAV27335.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DTS {ECO:0000313|EMBL:AAV27335.1};
RX PubMed=16687604; DOI=10.1099/jmm.0.46368-0;
RA Yeh K.M., Chang F.Y., Fung C.P., Lin J.C., Siu L.K.;
RT "magA is not a specific virulence gene for Klebsiella pneumoniae strains
RT causing liver abscess but is part of the capsular polysaccharide gene
RT cluster of K. pneumoniae serotype K1.";
RL J. Med. Microbiol. 55:803-804(2006).
RN [7] {ECO:0000313|Proteomes:UP000250675, ECO:0000313|Proteomes:UP000251123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC9601 {ECO:0000313|EMBL:SPX55056.1,
RC ECO:0000313|Proteomes:UP000251123}, and NCTC9645
RC {ECO:0000313|EMBL:SPX50509.1, ECO:0000313|Proteomes:UP000250675};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:SSK25472.1, ECO:0000313|Proteomes:UP000252603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4300STDY6470422 {ECO:0000313|EMBL:SSK25472.1,
RC ECO:0000313|Proteomes:UP000252603};
RG Pathogen Informatics;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|EMBL:QJL28622.1, ECO:0000313|Proteomes:UP000503203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C16KP0122 {ECO:0000313|EMBL:QJL28622.1,
RC ECO:0000313|Proteomes:UP000503203};
RA Yoon E.-J., Gwon B., Liu C., Kim D., Won D., Park S.G., Choi J.R.,
RA Jeong S.H.;
RT "Built-in CTX-M extended-spectrum beta-lactamase gene in Klebsiella
RT pneumoniae ensuring stable propagation of the multidrug-resistant pathogen
RT in clinical settings.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [10] {ECO:0000313|EMBL:MDH8290697.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sgh23 {ECO:0000313|EMBL:MDH8290697.1};
RA Chen Y., Gan Y.-H.;
RT "WGS of Klebsiella strains from the Antibiotics for Klebsiella Liver
RT Abscess Syndrome Study (A-KLASS) clinical trial, Singapore.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002526,
CC ECO:0000256|PIRNR:PIRNR000109}.
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 Evidence={ECO:0000256|ARBA:ARBA00000530,
CC ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000256|ARBA:ARBA00004874, ECO:0000256|PIRNR:PIRNR000109,
CC ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000109}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109,
CC ECO:0000256|RuleBase:RU000485}.
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DR EMBL; AY762939; AAV27335.1; -; Genomic_DNA.
DR EMBL; AB117611; BAD03943.1; -; Genomic_DNA.
DR EMBL; AB198423; BAD86781.1; -; Genomic_DNA.
DR EMBL; JARYWG010000018; MDH8290697.1; -; Genomic_DNA.
DR EMBL; CP052431; QJL28622.1; -; Genomic_DNA.
DR EMBL; UASO01000001; SPX50509.1; -; Genomic_DNA.
DR EMBL; UASN01000018; SPX55056.1; -; Genomic_DNA.
DR EMBL; UFEU01000003; SSK25472.1; -; Genomic_DNA.
DR RefSeq; WP_014907233.1; NZ_WYAM01000006.1.
DR SMR; Q762L5; -.
DR KEGG; kpnu:LI86_08590; -.
DR PATRIC; fig|573.1370.peg.3596; -.
DR BRENDA; 1.1.1.44; 2814.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000250675; Unassembled WGS sequence.
DR Proteomes; UP000251123; Unassembled WGS sequence.
DR Proteomes; UP000252603; Unassembled WGS sequence.
DR Proteomes; UP000503203; Chromosome.
DR Proteomes; UP001157099; Unassembled WGS sequence.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00873; gnd; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485};
KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000109};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|PIRNR:PIRNR000109}.
FT DOMAIN 179..467
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 74..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 102
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 128..130
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 186..187
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 191
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 260
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 287
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 451
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ SEQUENCE 468 AA; 51430 MW; F72A136EEBD01CFC CRC64;
MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVQEF
VESLETPRRI LLMVKAGAGT DSAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF
NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILKQIA AVAEDGEPCV TYIGADGAGH
YVKMVHNGIE YGDMQLIAEA YALLKGGLAL SNEELAQTFT EWNEGELSSY LIDITKDIFT
KKDEEGKYLV DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFARYIS SLKDQRVAAS
KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWD LNYGEIAKIF
RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT
FSAAIAYYDS YRSAVLPANL IQAQRDYFGA HTYKRTDKEG IFHTEWLE
//
