6PGD_HALVD
ID 6PGD_HALVD Reviewed; 299 AA.
AC D4GST8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating {ECO:0000305};
DE Short=6PGDH {ECO:0000303|PubMed:25836736};
DE EC=1.1.1.343 {ECO:0000269|PubMed:25836736};
GN Name=gndA {ECO:0000303|PubMed:25836736};
GN OrderedLocusNames=HVO_1830 {ECO:0000312|EMBL:ADE04956.1};
GN ORFNames=C498_04458 {ECO:0000312|EMBL:ELY35096.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=H26;
RX PubMed=25836736; DOI=10.1016/j.febslet.2015.03.026;
RA Pickl A., Schoenheit P.;
RT "The oxidative pentose phosphate pathway in the haloarchaeon Haloferax
RT volcanii involves a novel type of glucose-6-phosphate dehydrogenase -- The
RT archaeal Zwischenferment.";
RL FEBS Lett. 589:1105-1111(2015).
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:25836736}.
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:25836736};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.021 mM for 6-phosphogluconate {ECO:0000269|PubMed:25836736};
CC KM=0.033 mM for NAD(+) {ECO:0000269|PubMed:25836736};
CC KM=2.94 mM for NADP(+) {ECO:0000269|PubMed:25836736};
CC Vmax=10 umol/min/mg enzyme (with NAD(+) as electron acceptor)
CC {ECO:0000269|PubMed:25836736};
CC Vmax=0.42 umol/min/mg enzyme (with NADP(+) as electron acceptor)
CC {ECO:0000269|PubMed:25836736};
CC Note=The catalytic efficiency with NAD(+) is about 2000-fold higher
CC than with NADP(+), indicating that NAD(+) is the physiological
CC electron acceptor. {ECO:0000269|PubMed:25836736};
CC pH dependence:
CC Optimum pH is 10.5. {ECO:0000269|PubMed:25836736};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000269|PubMed:25836736}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:25836736}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants do not grow on glucose.
CC {ECO:0000269|PubMed:25836736}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE04956.1; -; Genomic_DNA.
DR EMBL; AOHU01000034; ELY35096.1; -; Genomic_DNA.
DR RefSeq; WP_004041720.1; NZ_AOHU01000034.1.
DR AlphaFoldDB; D4GST8; -.
DR SMR; D4GST8; -.
DR STRING; 309800.C498_04458; -.
DR EnsemblBacteria; ADE04956; ADE04956; HVO_1830.
DR EnsemblBacteria; ELY35096; ELY35096; C498_04458.
DR GeneID; 8925721; -.
DR KEGG; hvo:HVO_1830; -.
DR PATRIC; fig|309800.29.peg.868; -.
DR eggNOG; arCOG00248; Archaea.
DR HOGENOM; CLU_024540_0_0_2; -.
DR OMA; NGYALMY; -.
DR OrthoDB; 30530at2157; -.
DR BRENDA; 1.1.1.343; 2561.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
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-UniRule.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_02047; 6PGDH_archaea; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR004849; 6DGDH_YqeC.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR032883; 6PGDH_archaea.
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 Gluconate utilization; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..299
FT /note="6-phosphogluconate dehydrogenase, NAD(+)-dependent,
FT decarboxylating"
FT /id="PRO_0000434434"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 67..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 172..173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00349, ECO:0000255|HAMAP-
FT Rule:MF_02047"
SQ SEQUENCE 299 AA; 31983 MW; A44AAA01404C926F CRC64;
MQLGVIGLGR MGRIVVDRVL DAGHEVVAFD LSAEAVAAAA DAGAEPADSV ADLVDRLGDD
KRIWLMVPAG DAVDATLDDL DPHLDGDDVV VDGGNSHFEE SVRRAEACSA AYLDCGTSGG
PAGAELGFSL MVGGPQWAYD ELTPVFDAVA TGPDGHGHMG DSGSGHYVKM VHNGVEYALM
QAYGEGFELL AEGRYDLDLE SVAKTWNNGA VIRSWLLELC EEAFREEGSD LGDVDDHVAG
GSTGTWTVQE ALEQEVPVPL IYQSLAERFG SRADDRFSRR LANRLRYGFG RHEVARKDD