ID A0A1G7DMH5_9SPHI Unreviewed; 476 AA.
AC A0A1G7DMH5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN ORFNames=SAMN05216464_10744 {ECO:0000313|EMBL:SDE52737.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDE52737.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDE52737.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDE52737.1,
RC ECO:0000313|Proteomes:UP000199072};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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|PIRNR:PIRNR000109,
CC 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|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {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; FNAI01000007; SDE52737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7DMH5; -.
DR STRING; 1391627.SAMN05216464_10744; -.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000199072; 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; 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.
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|PIRNR:PIRNR000109,
KW ECO:0000256|RuleBase:RU000485};
KW Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW ECO:0000256|RuleBase:RU000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000199072}.
FT DOMAIN 182..472
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT BINDING 106
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 132..134
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 189..190
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 194
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 264
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 291
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 450
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 456
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ SEQUENCE 476 AA; 51796 MW; C870996E7469E627 CRC64;
MSATTDKYAF GMIGLGVMGR SLLLNMADHG FAVAGHDKDA AKVASLNDEA GDLAVKGFGD
VKEFIQSLTT PRAIMMLVPA GKIVDAVIEE LTPLLEKGDI LIDGGNSHFT DTNRRVEELE
AIGLHFFGMG VSGGEEGARR GPSMMPGGDK EAYNVMKPIF EAIAAKVDGA PCVTYIGPGA
SGHFVKMVHN GIEYGIMQLL AETYEIMKKG LKLDNAAIGK IFTDWNNGRL QSFLLDITKD
IFAFKAPGTD HLLLDDIKDE ARAKGTGKWT SQSAMDLQAP IPTVDTAVSM RDLSKYKALR
TKAAGIYSTQ DRQAIEGKVE ELLTALEQAF YFTMIISYAQ GMHMLSRASE EYQYDLKLDE
IAKIWRGGCI IRSKFLENIY GAYGKDKNLE HLLLDGDVAA LVEGTLPGIR KIVASAVNAG
IAAPAYAASL SYFDAFRSER MPSNLTQAQR DYFGAHTYEL IGKEGTFHTQ WAPSED
//
