ID C2ER82_9LACO Unreviewed; 483 AA.
AC C2ER82;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 71.
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:EEJ70971.1};
GN ORFNames=HMPREF0548_2178 {ECO:0000313|EMBL:EEJ70971.1};
OS Lactobacillus ultunensis DSM 16047.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ70971.1, ECO:0000313|Proteomes:UP000005583};
RN [1] {ECO:0000313|EMBL:EEJ70971.1, ECO:0000313|Proteomes:UP000005583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ70971.1,
RC ECO:0000313|Proteomes:UP000005583};
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:EEJ70971.1}.
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DR EMBL; ACGU01000113; EEJ70971.1; -; Genomic_DNA.
DR RefSeq; WP_007126923.1; NZ_GG693256.1.
DR AlphaFoldDB; C2ER82; -.
DR STRING; 525365.HMPREF0548_2178; -.
DR PATRIC; fig|525365.8.peg.1027; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_9; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000005583; 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}.
FT DOMAIN 9..188
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 190..480
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 46
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 149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 337
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"
SQ SEQUENCE 483 AA; 55677 MW; 2DD63C005F6A3970 CRC64;
MKNIPVVMII FGGSGDLAHR KLYPALFNLY EQGLIHDNFA VIGTARRPWS HEYLREQVGD
AVHETHDQVN ENDLKDFASH FYYQSHDVTN VEHYVTLKKL AQELDDRYCA HGNRLFYMAM
APRFFGTIAT HINDQHLTGS GFNRIVVEKP FGHDLASAEE LNKEITASFD EDDIFRIDHY
LGKEMVQNIM PMRFSNPLIK NIWSSEYIKN IQVTLAERLG VEARGGYYDT SGALRDMVQN
HIFQIITLLA MPEPKDIAST SIHQAKQDLL NSLIIPSPED VKKDFVRGQY LGSDTTFAYK
QEPNVDPNSM TETFVAGKVK FKKGPIAGVP IYFRTGKEFK EKKNRIDIVL KHINNPYGQA
HSNNITIEID PTSKIYITIN GKKIDVPGIR REDLTYAFSK EEMAKVPDGY ERLLHDVFVN
DSTNFTHWSE LKRYWEFIDA VEEAWQIENK SDNPNVVQYL PYRMGPKEAN NIFESPTEHW
IYE
//
