ID G6PD_ZYMMO Reviewed; 485 AA.
AC P21907; Q5NQL3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966};
GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=ZMO0367;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=2254282; DOI=10.1128/jb.172.12.7227-7240.1990;
RA Barnell W.O., Yi K.C., Conway T.;
RT "Sequence and genetic organization of a Zymomonas mobilis gene cluster that
RT encodes several enzymes of glucose metabolism.";
RL J. Bacteriol. 172:7227-7240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00966}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR EMBL; M60615; AAA27692.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29865.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88991.1; -; Genomic_DNA.
DR PIR; B37855; B37855.
DR RefSeq; WP_011240288.1; NZ_CP035711.1.
DR PDB; 7XHL; X-ray; 3.25 A; A/B/C/D/E/F/G/H=1-485.
DR PDB; 7XHP; X-ray; 2.78 A; A/B/C/D/E/F/G/H=1-485.
DR PDBsum; 7XHL; -.
DR PDBsum; 7XHP; -.
DR AlphaFoldDB; P21907; -.
DR SMR; P21907; -.
DR STRING; 264203.ZMO0367; -.
DR GeneID; 79904429; -.
DR KEGG; zmo:ZMO0367; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_5; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001173; 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glucose metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..485
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068138"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 89..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:7XHL"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:7XHL"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7XHL"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:7XHL"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7XHL"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:7XHL"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:7XHL"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:7XHL"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 199..211
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 220..225
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:7XHL"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7XHL"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 354..358
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 416..425
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:7XHP"
FT HELIX 435..454
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:7XHP"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:7XHL"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:7XHP"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:7XHP"
SQ SEQUENCE 485 AA; 53859 MW; C326FC605ED92430 CRC64;
MTNTVSTMIL FGSTGDLSQR MLLPSLYGLD ADGLLADDLR IVCTSRSEYD TDGFRDFAEK
ALDRFVASDR LNDDAKAKFL NKLFYATVDI TDPTQFGKLA DLCGPVEKGI AIYLSTAPSL
FEGAIAGLKQ AGLAGPTSRL ALEKPLGQDL ASSDHINDAV LKVFSEKQVY RIDHYLGKET
VQNLLTLRFG NALFEPLWNS KGIDHVQISV AETVGLEGRI GYFDGSGSLR DMVQSHILQL
VALVAMEPPA HMEANAVRDE KVKVFRALRP INNDTVFTHT VTGQYGAGVS GGKEVAGYID
ELGQPSDTET FVAIKAHVDN WRWQGVPFYI RTGKRLPARR SEIVVQFKPV PHSIFSSSGG
ILQPNKLRIV LQPDETIQIS MMVKEPGLDR NGAHMREVWL DLSLTDVFKD RKRRIAYERL
MLDLIEGDAT LFVRRDEVEA QWVWIDGIRE GWKANSMKPK TYVSGTWGPS TAIALAERDG
VTWYD
//
