ID H8H0Y8_DEIGI Unreviewed; 493 AA.
AC H8H0Y8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:AFD27007.1};
GN Synonyms=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN OrderedLocusNames=DGo_PA0121 {ECO:0000313|EMBL:AFD27007.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG Plasmid P1 {ECO:0000313|EMBL:AFD27007.1,
OG ECO:0000313|Proteomes:UP000007575}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD27007.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD27007.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RC PLASMID=Plasmid P1 {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
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; CP002192; AFD27007.1; -; Genomic_DNA.
DR AlphaFoldDB; H8H0Y8; -.
DR KEGG; dgo:DGo_PA0121; -.
DR PATRIC; fig|745776.4.peg.3158; -.
DR HOGENOM; CLU_013524_5_0_0; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000007575; Plasmid P1.
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}; Plasmid {ECO:0000313|EMBL:AFD27007.1}.
FT DOMAIN 10..177
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 180..446
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT REGION 453..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 493 AA; 53089 MW; 8E82DCD72F239656 CRC64;
MTQPPSDALV FFGATGDLAY KQIFPALQAM VARGTLDIPV IGVAKSGWTR EQLVERARQS
VQEHGSIDEQ AFARLSDLLQ YIDGDYNDDA TFTQLRQALG GAQRPLHYLA IPPSLFGPVC
ERLAASGCTQ GARIVVEKPF GHDLESARAL NATLHGVFAE ADIFRIDHYL GKEAVQNLLY
LRFANGFLEP LLRRAGVREI QITMAETFGV AGRGRFYEEA GAIRDVVQNH MLQVLGLLTM
EAPANQGQEA VRDGVARVFK SVRSLTPADV VRGQYAGYTR EAQVAPDSQV ETYAALRFEV
DSWRWAGVPI YVRVGKELPV TCTAVTVVFR DPPQEVFADV APHTNFLRLQ LTPGVQVTLG
LNTKRPGAGM KGQSTELTLH RQEASGLAPY DRLLTDALAG DATLFAREDE VEEAWRIVQG
VLGDAAPLQP YAPGTWGPAG ADTLLAPGLG WMDPDPDRGT AVPALAPTPP SAPAPHGSAE
NPAPAAQASP VGE
//
