ID D7E2R6_NOSA0 Unreviewed; 509 AA.
AC D7E2R6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Aazo_1091 {ECO:0000313|EMBL:ADI63443.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI63443.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI63443.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI63443.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
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|ARBA:ARBA00009975, 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; CP002059; ADI63443.1; -; Genomic_DNA.
DR RefSeq; WP_013190461.1; NC_014248.1.
DR AlphaFoldDB; D7E2R6; -.
DR STRING; 551115.Aazo_1091; -.
DR KEGG; naz:Aazo_1091; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_3; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001511; 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; IPR019796; G6P_DH_AS.
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.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00966}; Reference proteome {ECO:0000313|Proteomes:UP000001511}.
FT DOMAIN 25..206
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 208..507
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 254
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"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 509 AA; 58156 MW; F36AC8FC00995191 CRC64;
MVSLLENPLR VGLQQQGMPE PQIIVIFGAS GDLTWRKLVP ALFKLRRERR IPPETTIVGV
ARREWSHDYF REQMQKGMEE AHSNVELGEL WQDFSQGLFY CPGNIDDPES YQKLKNLLAK
LDEKRGTRGN RMFYLSVAPN FFPEAIKQLG AGGMLDDPYK HRLVIEKPFG RDLSSAQNLN
QVVQKYCKEN QVYRIDHYLG KETVQNLLVF RFANAIFEPL WNRQFVDHVQ ITVAETVGVE
DRAGYYESAG ALRDMLQNHL MQLYCLTAME APNAMDADSI RTEKVKVLQA TRLADVNNLS
RSAVRGQYSA GWMKGQQVAG YREEPGVNPN STIPTFVGMK FMVDNWRWQG VPFYLRTGKR
MPKKVSEIAI HFREVPSRMF PSAAQQKNAN VLALRIQPNE GISLRFDVKM PGGDFRTRSV
DMDFTYGSFG IEATSDAYDR LFLDCMMGDQ TLFTRADEVE AAWQVVTPAL SVWDGPADPT
TIPEYEAGTW EPAEAELLIN QDGRRWRRL
//
