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Database: UniProt
Entry: A0A2C1KC63_9BACI
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ID   A0A2C1KC63_9BACI        Unreviewed;       492 AA.
AC   A0A2C1KC63;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=COD11_12045 {ECO:0000313|EMBL:PGT83777.1};
OS   Bacillus sp. AFS040349.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT83777.1, ECO:0000313|Proteomes:UP000222674};
RN   [1] {ECO:0000313|EMBL:PGT83777.1, ECO:0000313|Proteomes:UP000222674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS040349 {ECO:0000313|EMBL:PGT83777.1,
RC   ECO:0000313|Proteomes:UP000222674};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-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|ARBA:ARBA00009975, ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PGT83777.1}.
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DR   EMBL; NUMC01000050; PGT83777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1KC63; -.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000222674; 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:UP000222674}.
FT   DOMAIN          11..189
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          192..489
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         14..21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         87..88
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                   ECO:0000256|PROSITE-ProRule:PRU10005"
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   492 AA;  56178 MW;  550DA3572E60CA19 CRC64;
     MTQEHPKSII VIFGATGDLA KRKLFPSIYR LVQNEKIGKN FAVVGVARRP WTTDEFRSNV
     SDSIQTSMKE SKDLEEFTSH FYYHPFDVTN PSSYLELNGL LTELDGTYQT EGNRIFYLAM
     APEFFGTIAQ NLKKEGLTDT NGWSRLVIEK PFGHDLPSAR KLNQEIREAF NENQIYRIDH
     YLGKEMVQNI EVIRFANALF EPLWNNRYIS NIQVTSSEIL GVEDRGRYYE NSGALRDMVQ
     NHMLQMVALL AMEPPIKLTT DEIRSEKVKV LRALRAVAED EVSQYFVRGQ YGAGQLEDKQ
     LVAYRDENNV DDNSQTETYV AGKLLIDNFR WAGVPFYIRT GKRMAAKSTK IVVQFKDIPM
     NLYYKKGETV PPNLLIIHIQ PEEGITLQLN AKKDEDESGI SKPVKLDLSN NFLDGINTPE
     AYEKLIYDCM RGDATNFTHW DEVALSWSFV DPISEAWTKG KAAIASYPSG SMGPKEADDL
     LKEDGNQWWP VN
//
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