ID M1WM50_PSEP2 Unreviewed; 494 AA.
AC M1WM50;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:CCH48990.1};
GN OrderedLocusNames=BN4_11755 {ECO:0000313|EMBL:CCH48990.1};
OS Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS (Desulfovibrio piezophilus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH48990.1, ECO:0000313|Proteomes:UP000011724};
RN [1] {ECO:0000313|EMBL:CCH48990.1, ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA Ollivier B., Dolla A.;
RT "The first genomic and proteomic characterization of a deep-sea sulfate
RT reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT piezophilus.";
RL PLoS ONE 8:e55130-e55130(2013).
RN [2] {ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}.
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DR EMBL; FO203427; CCH48990.1; -; Genomic_DNA.
DR RefSeq; WP_015415034.1; NC_020409.1.
DR AlphaFoldDB; M1WM50; -.
DR STRING; 1322246.BN4_11755; -.
DR KEGG; dpi:BN4_11755; -.
DR PATRIC; fig|879567.3.peg.1844; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_7; -.
DR OrthoDB; 9802739at2; -.
DR BioCyc; DPIE1322246:BN4_RS08810-MONOMER; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000011724; Chromosome.
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:CCH48990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011724}.
FT DOMAIN 22..201
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 203..490
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 98..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 494 AA; 56195 MW; 8A29F8C0D73041C5 CRC64;
MADTNGIETC DYNTPKDPCA IVIFGATGDL AARKILPSLY ALLCSGRLPD PSIIIGVSRS
GLSHEEYRER TRQALVESNA DMKCWEDFAP RLFYRSVDVN DVGTFTNLAG FIKDKESEFQ
TGGNRLFHLS VPPVAYEAIA QSLAHVGLAH EKDNWSRLVV EKPFGYDLES SRKLAAALKE
GFKEKQIFRI DHYLAKETVQ NMLMFRFANS IFEPVWNRQF IQSVHITAAE SLGVEHRAGF
YDHTGVLRDM FQNHMMQLLS LVAMEPPSIY EANRIRDEKA KIYRSLRPFP MDSLDENLVL
GQYAAGMIKE KSVPSYVSEP GVSPNSTTPT FASMKAYIDN WRWQGVPFYI TSGKRMSTKR
TDIEVKFKEV PHSMFRNILG EHITANRLTL SIHPKEEVML SFQAKTPGPG MCLRNVTMNF
DYAMGHPLRL TAYEKVLLDV LMGDHTLFWR QDSVDLCWSY LTPMLKECEC EEQAERLHLY
KAGTDGPKKA RGDW
//
