6PGDH_GLUOX
ID 6PGDH_GLUOX Reviewed; 332 AA.
AC G5EBD7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating {ECO:0000305};
DE Short=6PGDH {ECO:0000303|PubMed:20676631};
DE EC=1.1.1.343 {ECO:0000269|PubMed:20676631};
GN OrderedLocusNames=GOX1705 {ECO:0000312|EMBL:AAW61445.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=621H;
RX PubMed=20676631; DOI=10.1007/s00253-010-2779-9;
RA Rauch B., Pahlke J., Schweiger P., Deppenmeier U.;
RT "Characterization of enzymes involved in the central metabolism of
RT Gluconobacter oxydans.";
RL Appl. Microbiol. Biotechnol. 88:711-718(2010).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to
CC NADH. {ECO:0000269|PubMed:20676631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NAD(+) = CO2 + D-ribulose 5-phosphate
CC + NADH; Xref=Rhea:RHEA:33023, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58121, ChEBI:CHEBI:58759;
CC EC=1.1.1.343; Evidence={ECO:0000269|PubMed:20676631};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 mM for 6-phosphogluconate {ECO:0000269|PubMed:20676631};
CC KM=64 uM for NAD(+) {ECO:0000269|PubMed:20676631};
CC KM=440 uM for NADP(+) {ECO:0000269|PubMed:20676631};
CC Vmax=41.7 umol/min/mg enzyme {ECO:0000269|PubMed:20676631};
CC Note=kcat is 23 sec(-1). Can use NAD or NADP, but has a clear
CC preference for NAD in vivo. {ECO:0000269|PubMed:20676631};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000305|PubMed:20676631}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20676631}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000009; AAW61445.1; -; Genomic_DNA.
DR RefSeq; WP_011253227.1; NZ_LT900338.1.
DR PDB; 6XEQ; X-ray; 3.20 A; A/B/C/D=1-332.
DR PDBsum; 6XEQ; -.
DR AlphaFoldDB; G5EBD7; -.
DR SMR; G5EBD7; -.
DR STRING; 290633.GOX1705; -.
DR EnsemblBacteria; AAW61445; AAW61445; GOX1705.
DR KEGG; gox:GOX1705; -.
DR eggNOG; COG1023; Bacteria.
DR HOGENOM; CLU_024540_0_0_5; -.
DR OMA; NGYALMY; -.
DR BRENDA; 1.1.1.343; 38.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro.
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; IPR004849; 6DGDH_YqeC.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
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 PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00872; gnd_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Gluconate utilization; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..332
FT /note="6-phosphogluconate dehydrogenase, NAD(+)-dependent,
FT decarboxylating"
FT /id="PRO_0000434436"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 30..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6XEQ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:6XEQ"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:6XEQ"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 192..220
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:6XEQ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:6XEQ"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:6XEQ"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:6XEQ"
SQ SEQUENCE 332 AA; 35876 MW; 2D7466AEF76E8B08 CRC64;
MRIGIIGLGR MGGNIAVRLT RHGHDVVVHD RTSEVTTSVV GRCEAGRATP ADTLADMAKL
LEGDEHRVVW VMLPAGAITE DCVQQLGGLL GRGDIIIDGG NTYYKDDVRR SAELAEKGIS
YVDVGTSGGV WGLERGYCMM FGGTKETAEY IDPILSALAP GIGDVPRTPG RDEAGHDPRA
EQGYLHCGPA GSGHFVKMVH NGIEYGMMQA FAEGFDIMKS KNSPILAEKD RFELNMGDIA
EVWRRGSVVS SWLLDLTAEA LTRSETLNEF SGEVADSGEG RWTIEAAIEE DVPAPVMTAA
LFTRFRSRSG NNFAEKILSA QRFGFGGHVE KK
