ID A0A0F8CLC8_9EURY Unreviewed; 301 AA.
AC A0A0F8CLC8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=FK85_26750 {ECO:0000313|EMBL:KKF39677.1};
OS Halorubrum saccharovorum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39677.1, ECO:0000313|Proteomes:UP000053331};
RN [1] {ECO:0000313|EMBL:KKF39677.1, ECO:0000313|Proteomes:UP000053331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KKF39677.1,
RC ECO:0000313|Proteomes:UP000053331};
RA Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT "Full genome sequence of Halorubrum H3 strain isolated from Burlinskoye
RT Salt Lake (Altai Krai, Russia).";
RL Submitted (MAR-2015) 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 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKF39677.1}.
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DR EMBL; JNFH02000027; KKF39677.1; -; Genomic_DNA.
DR RefSeq; WP_050024755.1; NZ_JNFH02000027.1.
DR AlphaFoldDB; A0A0F8CLC8; -.
DR OrthoDB; 23890at2157; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000053331; 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; 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:UP000053331}.
FT DOMAIN 165..301
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 301 AA; 32408 MW; C16B6CB4DFBE94A9 CRC64;
MELGVIGLGR MGQIVVNRSL DAGHDVVAFD LSAEATATAA EAGATAADSV EDLCDRLGAE
KRIWLMVPAG DAVDATLADL EPHLDADDVV VDGGNSQFQA SVRRAEETDA AYLDCGTSGG
PASAEEGFSL MVGGPEWAYE AMVPVFDAVA TGPDGHDRMG ESGSGHYVKM VHNGVEYALM
QAYGEGFELL TEGRYDLDME TVARTWNNGA VIRSWLLELC EEAFREEGSD LGDVADHVAG
GSTGTWTVQE ALEQEVPVPL IYQALAERFD SRNEGRFSRR LANRLRYGFG RHEVARRSDE
Q
//
