ID C0W3G3_9ACTO Unreviewed; 527 AA.
AC C0W3G3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
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 ECO:0000313|EMBL:EEH66726.1};
GN ORFNames=HMPREF0058_0407 {ECO:0000313|EMBL:EEH66726.1};
OS Actinomyces urogenitalis DSM 15434.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=525246 {ECO:0000313|EMBL:EEH66726.1, ECO:0000313|Proteomes:UP000004778};
RN [1] {ECO:0000313|EMBL:EEH66726.1, ECO:0000313|Proteomes:UP000004778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15434 {ECO:0000313|EMBL:EEH66726.1,
RC ECO:0000313|Proteomes:UP000004778};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EEH66726.1}.
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DR EMBL; ACFH01000020; EEH66726.1; -; Genomic_DNA.
DR RefSeq; WP_006549711.1; NZ_DS999576.1.
DR AlphaFoldDB; C0W3G3; -.
DR STRING; 103621.GCA_001067145_00599; -.
DR GeneID; 81707524; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_11; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000004778; 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:UP000004778}.
FT DOMAIN 40..224
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 226..525
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 527 AA; 58170 MW; E5636D98B1C540A4 CRC64;
MDTADSAHAT SSSQAAAGSN PLLDPRDLRL PRIADPCVMV MFGITGDLAR HKLLPAIYDL
ANRGLLSPSF SLVGVGRRDW SDEDMRAYVR GSVGAHARTP WHESIWEQLA EGMRFVTFSS
FEDDEAYERL TGVVAELDAS RGTSGNRAFY LSIPPGWFPA VTQRVAASGL VDDAPGSWRR
VVIEKPFGHD RDSARELDSL VGRIVRPDDV FRVDHYLGKE TVQNILALRF ANTMFEPLWN
QGYVDHVQIT MAEDIGIGSR AGYYDTIGAA RDVIQNHLLQ LLALTAMEEP SSMDAAAVRA
EKEKVLDCVR LTRHGVLDLD ATTARGRYVG GFQGGVAVPG YTEEQGVPQD STTETFAAIR
LEIANRRWAG VPFYLRAGKR LARRVTEVAV VFKQPPFLPF DPSATAGVGA NTIVLRIQPD
EGITMRLASK VPGTHMELRD VLMDFGYGAS FNEESPEAYE RLILDALLGD APLFPHQREV
DLSWRILDPV IEHWAAAGVP DSYRPGSWGP DSAHDLLTRD GRTWRRS
//
