ID R4VS49_9EURY Unreviewed; 297 AA.
AC R4VS49;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating {ECO:0000256|HAMAP-Rule:MF_02047};
DE Short=6PGDH {ECO:0000256|HAMAP-Rule:MF_02047};
DE EC=1.1.1.343 {ECO:0000256|HAMAP-Rule:MF_02047};
GN ORFNames=L593_00450 {ECO:0000313|EMBL:AGN00045.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00045.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN00045.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00045.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
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:0000256|HAMAP-Rule:MF_02047}.
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:0000256|HAMAP-Rule:MF_02047};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000256|HAMAP-Rule:MF_02047}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_02047}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|HAMAP-Rule:MF_02047}.
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DR EMBL; CP005962; AGN00045.1; -; Genomic_DNA.
DR RefSeq; WP_020444939.1; NC_021313.1.
DR AlphaFoldDB; R4VS49; -.
DR STRING; 1333523.L593_00450; -.
DR GeneID; 16182085; -.
DR KEGG; sali:L593_00450; -.
DR PATRIC; fig|1333523.5.peg.92; -.
DR eggNOG; arCOG00248; Archaea.
DR HOGENOM; CLU_024540_0_0_2; -.
DR OrthoDB; 23890at2157; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000014072; Chromosome.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00872; gnd_rel; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF67; 6-PHOSPHOGLUCONATE DEHYDROGENASE YQEC-RELATED; 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; 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, ECO:0000256|HAMAP-
KW Rule:MF_02047}; NAD {ECO:0000256|HAMAP-Rule:MF_02047};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02047};
KW Reference proteome {ECO:0000313|Proteomes:UP000014072}.
FT DOMAIN 165..297
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 67..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 118..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 172..173
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02047"
SQ SEQUENCE 297 AA; 31853 MW; 0291C74FF339A73A CRC64;
MHIGVIGLGR MGRIVVDRLL DAGHDVVAFD IDDDAVAAAA DAGVTPADSI PDVADELGSE
RRIWLMVPAG DPVDAALAEL DGHVDGDDVI VDGGNSHFEA SVRRADATDA AYLDCGTSGG
PAGAELGFSL MIGGPEWAYE AMVPAFDAVA TGPDGHDRMG PVGSGHYVKM VHNGIEYALM
QAYGEGFELL ARGRYDLDLE SVARTWTNGA VIRSWLLDLC EEAFREEGSD LGDVADHVQG
GSTGTWTVQE ALEQEVPVPL IYQALAERFD SRKDRFARKL ANRLRYGFGR HEVVREN
//
