ID A0A0K2GB65_NITMO Unreviewed; 514 AA.
AC A0A0K2GB65;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=zwf1 {ECO:0000313|EMBL:ALA58114.1};
GN Synonyms=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN ORFNames=NITMOv2_1694 {ECO:0000313|EMBL:ALA58114.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA58114.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA58114.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA58114.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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; CP011801; ALA58114.1; -; Genomic_DNA.
DR RefSeq; WP_053379320.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GB65; -.
DR STRING; 42253.NITMOv2_1694; -.
DR KEGG; nmv:NITMOv2_1694; -.
DR PATRIC; fig|42253.5.peg.1665; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000069205; 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}; Reference proteome {ECO:0000313|Proteomes:UP000069205}.
FT DOMAIN 26..211
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 213..512
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 29..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 514 AA; 57796 MW; 7DF88B7BFC6D343D CRC64;
MASNSQRIEI SPAQETLPPV EPCTLVIFGG SGDLARRRLI PALYNLLLDG LLPSDYAVLG
LGRTPMSDEE FRAAVRDGVV KHSRQALIED TWNAFSRHLF YLAGENDNPQ TYLRLKARAE
ELERSLQLPG NRIFYLSIPP SSFAPVCEGL AQAGLAGARG ARSPYARIIV EKPVGRDLTS
ARAINEVTGR VFDESQIFRI DHYLGKETVQ NLMVVRFANS IFEPIWNHKY IDHVQITVSE
AEGVGTRAAY YEEAGALRDM VQNHLLQLLC LVAMEPPYSL DPDVVRNAKM EVLRCLRPIT
AKDVERFTVR AQYTEGTIHG TPVPGYRREK GVKPDSTTET YVAVKCFVEN WRWSGVPFYL
RTGKALPLRA SEVAVQFKEI PQILFNANPK GPLAPNVLAL RIQPEEGLSL RIVSRVPGTR
AQTHPVEMNF KYGEVFGRPS PEAYERLLLD VMAGDASRFM RRDAVEASWA WITQILQAWE
ELGQRWLPEY PAGTWGPVEA DRLIQNDGRS WRVL
//
