G6PD_KLULA
ID G6PD_KLULA Reviewed; 497 AA.
AC P48828;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN Name=ZWF; OrderedLocusNames=KLLA0D19855g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RA Wesolowski-Louvel M., Tanguy-Rougeau C., Fukuhara H.;
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. The main function of this enzyme is
CC to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC and nucleic acid synthesis (By similarity).
CC {ECO:0000250|UniProtKB:P11413}.
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;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X70373; CAA49834.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH01040.1; -; Genomic_DNA.
DR PIR; S31337; S31337.
DR RefSeq; XP_453944.1; XM_453944.1.
DR PDB; 7E6H; X-ray; 2.70 A; A=1-497.
DR PDB; 7E6I; X-ray; 2.39 A; A=1-497.
DR PDBsum; 7E6H; -.
DR PDBsum; 7E6I; -.
DR AlphaFoldDB; P48828; -.
DR SMR; P48828; -.
DR STRING; 28985.XP_453944.1; -.
DR PRIDE; P48828; -.
DR EnsemblFungi; CAH01040; CAH01040; KLLA0_D19855g.
DR GeneID; 2893289; -.
DR KEGG; kla:KLLA0_D19855g; -.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; P48828; -.
DR OMA; VEICVYE; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glucose metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..497
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068104"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 15..22
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 183..187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 68..73
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:7E6H"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 326..330
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:7E6H"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 393..401
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:7E6I"
FT HELIX 433..451
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:7E6I"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7E6H"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:7E6I"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:7E6I"
SQ SEQUENCE 497 AA; 56574 MW; C6EC57AD6B6E9F1F CRC64;
MATQFDENTV ITIFGASGDL SKKKTFPALF GLYREGYLNP TTKIIGYARS KLSNEDLREK
VKPFLKKPNG AKDDAKVNEF LSMVSYHAGP YDSDEGYLEL KKIIEEFEAE KKVDEPHRLF
YLALPPSIFI DVCSKLKENL YTESGIQRVI VEKPFGHDLQ SATELQEKLA PLFSEDELFR
IDHYLGKEMV KNLLLMRFGN TFLNAAWNKE NIQSVQVVFK EPFGTEGRGG YFDSIGIIRD
VMQNHLLQVL TLLTMERPVS FDPESVRDEK VKVLKAFSPI DHDDILIGQY GRSVDGSKPS
YLDDETVKED SKCVTFAAIG FKIANERWDG VPIVMRAGKA LNEGKVEIRI QFRRVASGMF
TDIPNNELVI RIQPNEAIYL KCNAKTPGLA NENQTTELDL TYSERYKNYW IPEAYESLIR
DALLGDHSNF VRDDELDVSW KLFTPLLNYL EGPDGPQPKI YPYGCRSPDG LVEFLADHGY
TFSKPGSYQW PVTTPKM
