ID I3DBM8_9PAST Unreviewed; 484 AA.
AC I3DBM8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:EIJ69121.1};
GN ORFNames=HMPREF1052_0310 {ECO:0000313|EMBL:EIJ69121.1};
OS Pasteurella bettyae CCUG 2042.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ69121.1, ECO:0000313|Proteomes:UP000006457};
RN [1] {ECO:0000313|EMBL:EIJ69121.1, ECO:0000313|Proteomes:UP000006457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ69121.1,
RC ECO:0000313|Proteomes:UP000006457};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIJ69121.1}.
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DR EMBL; AJSX01000033; EIJ69121.1; -; Genomic_DNA.
DR RefSeq; WP_005760875.1; NZ_AJSX01000033.1.
DR AlphaFoldDB; I3DBM8; -.
DR PATRIC; fig|1095749.3.peg.1248; -.
DR eggNOG; COG0362; Bacteria.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000006457; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006457}.
FT DOMAIN 181..471
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 34..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 76..78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 104
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 130..132
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 188..189
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 193
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 262
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 289
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 447
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 453
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ SEQUENCE 484 AA; 53314 MW; A36BCE31C5FCFB8B CRC64;
MSTKGDIGVI GLAVMGQNLI LNMNDHGFKV VAFNRTTSKV DEFLEGAAKD TNIIGAYSLE
DLAAKLEKPR KVMLMVRAGD VVDQFIDALL PHLEEGDIII DGGNSNYPDT NRRAKSLAEK
GIRFIGTGVS GGEEGARHGP SIMPGGNEEA WPYVKPILQA ISAKTDKGEP CCDWVGKEGA
GHFVKMVHNG IEYGDMQLIC EAYQFLKDGL GLSYEEMQSI FAEWKKTELD SYLIDITTDI
LGYKEADGET LVEKILDTAG QKGTGKWTGI NALDFGIPLT LITESVFARC VSSFKDQRVA
ASQLFNKTIE PVEGDKKVWI EAVRKALLAS KIISYAQGFM LIREASENFE WNINYGATAL
LWREGCIIRS AFLGNIRDAY EANPGLVFLG SDPYFKGILE DALKDWRKVV AKSIEVGIPM
PCMASAITFL DGYTSERVPA NLLQAQRDYF GAHTYERTDK PRGKYFHTNW TGRGGDTAST
TYDV
//
