ID A0A1X9MI59_9BACI Unreviewed; 485 AA.
AC A0A1X9MI59;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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_3 {ECO:0000313|EMBL:ARK31291.1};
GN Synonyms=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN ORFNames=BkAM31D_16310 {ECO:0000313|EMBL:ARK31291.1};
OS Halalkalibacter krulwichiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK31291.1, ECO:0000313|Proteomes:UP000193006};
RN [1] {ECO:0000313|EMBL:ARK31291.1, ECO:0000313|Proteomes:UP000193006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM31D {ECO:0000313|EMBL:ARK31291.1,
RC ECO:0000313|Proteomes:UP000193006};
RA Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL Submitted (APR-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}.
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DR EMBL; CP020814; ARK31291.1; -; Genomic_DNA.
DR RefSeq; WP_066160645.1; NZ_CP020814.1.
DR AlphaFoldDB; A0A1X9MI59; -.
DR STRING; 199441.BkAM31D_16310; -.
DR KEGG; bkw:BkAM31D_16310; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000193006; 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:ARK31291.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193006}.
FT DOMAIN 7..189
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 192..485
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 10..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 485 AA; 55454 MW; F55BA54F1EB35AF3 CRC64;
MEAMTFVLFG ATGDLAKRKI FPALYNLFLD QKLPLPISII GVGRGDLSDT DFQNYVEDSL
KTFSRRSLND NSNFEVFIRA FRYCHVDASK AEGYKGLLEL VKQREEELNI PENRMFYLSV
APEFFNVIAF NIKESGLGST KGWKRLIIEK PFGHDLKSAQ ELNDKLSKAF DEEEIFRIDH
YLGKPMVQNL EVLGFANPVL QALWNNQYIA NVQITASETV GVEERAGYYD QTGAIRDMFQ
NHMLQMLMMT AMQLPKQISA EEIRNEKRKV IESLRPLKKE DVVNHVIRGQ YGPGEIHSKP
VVGYTGEAEV APSSLNDTFV AVRLCVDDDF WRGVPFYIRT GKRMAEKSTR IVIEFKNTSK
DLYRTQEKET APNLLVIEIN PNESVSLQLN SKNPLNNGKI EPVNVDFSAK QADVPEAYEL
LIYDAMRGDS TFFAHWKEVE LSWKWVQPIL EAFEENTIPL QLYTSGSMGP DASHQLLAEE
GYKWW
//
