ID A0A069RAF8_PEPLI Unreviewed; 489 AA.
AC A0A069RAF8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00966};
DE Short=G6PD {ECO:0000256|HAMAP-Rule:MF_00966};
DE EC=1.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00966};
GN Name=zwf {ECO:0000256|HAMAP-Rule:MF_00966,
GN ECO:0000313|EMBL:KDR93793.1};
GN ORFNames=CLIT_23c00650 {ECO:0000313|EMBL:KDR93793.1};
OS Peptoclostridium litorale DSM 5388.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1121324 {ECO:0000313|EMBL:KDR93793.1, ECO:0000313|Proteomes:UP000027946};
RN [1] {ECO:0000313|EMBL:KDR93793.1, ECO:0000313|Proteomes:UP000027946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W6 {ECO:0000313|EMBL:KDR93793.1,
RC ECO:0000313|Proteomes:UP000027946};
RA Poehlein A., Jagirdar A., Khonsari B., Chibani C.M.,
RA Gutierrez Gutierrez D.A., Davydova E., Alghaithi H.S., Nair K.P.,
RA Dhamotharan K., Chandran L., G W., Daniel R.;
RT "Genome sequence of Clostridium litorale W6, DSM 5388.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00966};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|ARBA:ARBA00004937, ECO:0000256|HAMAP-Rule:MF_00966}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00966}.
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:KDR93793.1}.
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; JJMM01000026; KDR93793.1; -; Genomic_DNA.
DR RefSeq; WP_038267600.1; NZ_JJMM01000026.1.
DR AlphaFoldDB; A0A069RAF8; -.
DR STRING; 1121324.CLIT_23c00650; -.
DR eggNOG; COG0364; Bacteria.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000027946; Unassembled WGS sequence.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526, ECO:0000256|HAMAP-
KW Rule:MF_00966}; NADP {ECO:0000256|HAMAP-Rule:MF_00966};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966,
KW ECO:0000313|EMBL:KDR93793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027946}.
FT DOMAIN 5..188
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 191..487
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 8..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 84..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 489 AA; 55928 MW; 35A64718CE3ADDC9 CRC64;
MCLIVLFGGS GDLSRKKLMP SLYNLQCQGK LSEDCHVFAI GRRERNEKEY IKALKEGAFS
NSRLGGDERA WKSLSSRIYY RNFDFGDGAA YERLEAEMSK LENEKGLSGS RIYYMAVSPD
YFTLITDSIG KAGMNKGAKG SYRRLVIEKP FGRSLESARL LNCEISRVFP EKDIYRIDHY
LAKEMIQNIM GIRFSNAIFE PLWSRDNIDN IQISVCEKDG VQGRGGYYDG AGALRDMVQN
HIMQMISLIC MEPPISLEAD EIRDEKVKVI KHIEKIKGGN LKERMVLGQY SAGNVDGGDV
AGYRDEEGVP SDSATETFAA LKLEVANRRW KGVPVYIRTG KRMSRKLAQI VVQFKTFCQI
HGFEPYKEPM PNLLVIRVQP KDGVFFQFNM KKPGSTEEIV TQQMDYCRSC EYSENTPQAY
ERLFEDVIKG DASLFTRWDE IEGSWKIIDE ILSGCTREEQ NMQFYEAGSM GPDESEELLQ
REGRRWWNI
//
