6PGD_AGGAC
ID 6PGD_AGGAC Reviewed; 484 AA.
AC P70718;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000305};
DE EC=1.1.1.44 {ECO:0000269|PubMed:9020051};
GN Name=gnd {ECO:0000303|PubMed:9020051};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RX PubMed=9020051; DOI=10.1006/bbrc.1996.5917;
RA Yoshida Y., Nakano Y., Yamashita Y., Koga T.;
RT "The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its
RT adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNA.";
RL Biochem. Biophys. Res. Commun. 230:220-225(1997).
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:0000269|PubMed:9020051}.
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:0000269|PubMed:9020051};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000250|UniProtKB:P00350}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00350}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; D88189; BAA13558.1; -; Genomic_DNA.
DR PIR; JC5282; JC5282.
DR RefSeq; WP_005545119.1; NZ_VSEV01000005.1.
DR AlphaFoldDB; P70718; -.
DR SMR; P70718; -.
DR STRING; 714.ACT75_04165; -.
DR OMA; VIMVKAG; -.
DR UniPathway; UPA00115; UER00410.
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; 1.10.1040.10; -; 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 1: Evidence at protein level;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT CHAIN 1..484
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090024"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 34..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 76..78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 104
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 130..132
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 188..189
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 193
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 262
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 289
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 447
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 453
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P96789"
SQ SEQUENCE 484 AA; 53289 MW; F7BD0B2EA3BF624D CRC64;
MSVKGDIGVI GLAVMGQNLI LNMNDHGFKV VAYNRTTSKV DEFLEGAAKG TNIIGAYSLE
DLANKLEKPR KVMLMVRAGE VVDHFIDALL PHLEAGDIII DGGNSNYPDT NRRVAALREK
GIRFIGTGVS GGEEGARHGP SIMPGGNEEA WQFVKPVLQA ISAKTEQGEP CCDWVGKDGA
GHFVKMVHNG IEYGDMQLIC EAYQFLKEGV GLSDDELQAT FNEWRNTELD SYLIDITADI
LGYKDADGSR LVDKVLDTAG QKGTGKWTGI NALDFGIPLT LITESVFARC VSAFKDQRVA
ASKLFHKTIG KVEGDKKVWI EAVRKALLAS KIISYAQGFM LIREASEHFN WNINYGNTAL
LWREGCIIRS RFLGNIRDAY EANPDLIFLG SDSYFKGILE NAMSDWRKVV AKSIEVGIPM
PCMASAITFL DGYTSARLPA NLLQAQRDYF GAHTYERTDK PRGEFFHTNW TGRGGNTAST
TYDV
