ID A0A173LP31_9ACTN Unreviewed; 523 AA.
AC A0A173LP31;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BJL86_1696 {ECO:0000313|EMBL:ANI92472.1};
OS Dietzia timorensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=499555 {ECO:0000313|EMBL:ANI92472.1, ECO:0000313|Proteomes:UP000186104};
RN [1] {ECO:0000313|EMBL:ANI92472.1, ECO:0000313|Proteomes:UP000186104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ID05-A0528 {ECO:0000313|EMBL:ANI92472.1,
RC ECO:0000313|Proteomes:UP000186104};
RA Wu X.;
RT "Complete genome sequence of a saline-alkali tolerant type strain Dietzia
RT timorensis ID05-A0528T.";
RL Submitted (JUN-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; CP015961; ANI92472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A173LP31; -.
DR STRING; 499555.BJL86_1696; -.
DR KEGG; dtm:BJL86_1696; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000186104; 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}.
FT DOMAIN 41..224
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 226..521
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 523 AA; 58168 MW; 972FD60C3420C990 CRC64;
MGPVSSEGHV HEDVADEAWT NPLRDPRDRR LPRIAGPCGI VIFGVTGDLS RKKLIPAIYD
LANRGLLPPG FALIGFGRRK WGNDEFAEFA KQCAKERSRT KFREDVWERL AEGLRFVTGT
FDGDEGFDSL AETLDELGSA GKTAGNIAFY LSIPPDDFPV VCRQLDRTGV AEPGNDSWRR
VVIEKPFGHD LDSARELNDV VAAVFPEESV FRIDHYLGKE TVQNIMALRF ANQLFEPVWN
SNYVDHVQIT MAEDIGLGGR AGYYDGIGAA RDVIQNHLIQ LMALVAMEEP INFSAAALRE
EKIKVLESAA LAEPIEDTTA RGVYGAGWQG SEKVLGLHEE EGYDPNSTTE TYAAITLEVH
NRRWGGVPFY LRTGKRLGRR VTEIAVVFAR APHLPFDSTM TEELGSNALV IRVQPDEGVT
LRFGSKTPGT TMEVRDVSMD FDYGESFTVD SPEAYERLIL DVLLGAPSLF PESREVELSW
MLLDPVLDEW ASRGRPETYA AGTWGPSSAD KMLQRDGRSW RRP
//
