ID A0A1I0LR98_9ACTN Unreviewed; 491 AA.
AC A0A1I0LR98;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=SAMN05421811_123112 {ECO:0000313|EMBL:SEU44675.1};
OS Nonomuraea wenchangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=568860 {ECO:0000313|EMBL:SEU44675.1, ECO:0000313|Proteomes:UP000199361};
RN [1] {ECO:0000313|EMBL:SEU44675.1, ECO:0000313|Proteomes:UP000199361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SEU44675.1,
RC ECO:0000313|Proteomes:UP000199361};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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; FOHX01000023; SEU44675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0LR98; -.
DR STRING; 568860.SAMN05421811_123112; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000199361; 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; 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:UP000199361}.
FT DOMAIN 16..191
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 193..487
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 94..95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 152
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 491 AA; 54764 MW; 18AF681020DE461D CRC64;
MSTPPAAGPV HTADLVVFGG TGDLSMRKLL PALYHCDRDG RLSPETRVIA MSRGGLADAD
FRGKVDAEVR DSVPVDDPAV WQRFLGRLHH VSVDVGAANH PGWHHLAELL APHEERDRVF
YLASPPRTFG PFCRELAEAG LVTPRSRVVL EKPLGHDLPS AQRINDEVGA IFDERQIFRI
DHYLGKETVQ NLLVLRFANA FLEPIWNSLW IDHVQITAAE TVGTPGRRGY YDHAGALRDM
VQNHLLQLLT LTAMEPPARN DREAIRDEKV KVLQALRPIV GTEADRFTVR GQYVGAGDLP
GYLDEPGSTP PTESSRRVET FTAIRAEIRN WRWAGVPFYL RTGKRMPYRR SEIVVQFKDV
PHSIFPGGSP NRLVLRLQPE EGIELHLMAK EPGAGEVTLK PVPMALSFGK TFTARVPEAY
ERLLTDVLAG NPTLFMRRDE VEAAWRWIDP ILDAWRATPA LPEPYPAGTT GPAGAHELLG
RSGRAWHEEE L
//
