G6PD_BORBU
ID G6PD_BORBU Reviewed; 478 AA.
AC O51581;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966};
GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=BB_0636;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00966}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR EMBL; AE000783; AAB91531.1; -; Genomic_DNA.
DR PIR; C70179; C70179.
DR RefSeq; NP_212770.1; NC_001318.1.
DR RefSeq; WP_002656376.1; NC_001318.1.
DR AlphaFoldDB; O51581; -.
DR SMR; O51581; -.
DR STRING; 224326.BB_0636; -.
DR PRIDE; O51581; -.
DR EnsemblBacteria; AAB91531; AAB91531; BB_0636.
DR GeneID; 56567446; -.
DR KEGG; bbu:BB_0636; -.
DR PATRIC; fig|224326.49.peg.1027; -.
DR HOGENOM; CLU_013524_5_0_12; -.
DR OMA; VEICVYE; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001807; 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 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 PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..478
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068111"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 86..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 478 AA; 56113 MW; 4DDBCE2861161C8A CRC64;
MKERSVSNFD IVIFGVTGNL SRKKLIPSLF NLFKNKCISN FRVIGFSRKI FTDKEFRLYI
KDSLWQEETD SLIEIFLNFF VYVFGDFNEK ESYKNLFKFL DRSRETIYYL STSPAFYGPI
INHLKKYFLS EKLTLSKIVL EKPFGSSLET AKKLNSLLYS AFKEDQIYRI DHYLGKETVQ
NIFTFRFGNS IFENIWNNRY VDFVQITVAE ELGLDGRVEY YDSVGALKDM VQNHILQLLS
LVAMESPIKF DSEFIHDEKV KVLKSLRKIS KEDIKNYIVK GQYIGSQVQG VFKKGYKDET
EFLGNSNTET YLAMKVFINN WRWSGVPFYL RTGKGLARKF SEIYIQFKKP SFTLFNNSSV
DFSNALIFRI QPRDGIEIKF NTKKPGYNYE IQTANMEFSY HGAFKRLFDE AYERLLLDAF
LGDGTLYATS DEIESSWEFV SDIANKWADI EICNYFYGSE GPKEIDSILE KDHFWRKI
