ID C7NHJ2_KYTSD Unreviewed; 515 AA.
AC C7NHJ2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Ksed_13180 {ECO:0000313|EMBL:ACV06349.1};
OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS (Micrococcus sedentarius).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06349.1, ECO:0000313|Proteomes:UP000006666};
RN [1] {ECO:0000313|EMBL:ACV06349.1, ECO:0000313|Proteomes:UP000006666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC {ECO:0000313|Proteomes:UP000006666};
RX PubMed=21304632; DOI=10.4056/sigs.761;
RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL Stand. Genomic Sci. 1:12-20(2009).
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; CP001686; ACV06349.1; -; Genomic_DNA.
DR RefSeq; WP_015779294.1; NC_013169.1.
DR AlphaFoldDB; C7NHJ2; -.
DR STRING; 478801.Ksed_13180; -.
DR KEGG; kse:Ksed_13180; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_11; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000006666; 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 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 31..214
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 216..513
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 515 AA; 57164 MW; D1A401640F8B3AA8 CRC64;
MSPARVTADH NPLRADDDKR LPRIAGPSAL VLFGVTGDLA RKKLLPAIYD LANRGLLPSG
FSLVGFARRD WDGQDFDAEV RKAVMEHCRT PFDEDVWKQL QQGTRFVAGT FDDEGAYDEL
RGVLEELDEL RGTGGNRAFY LSIPPRFFAE VCQQLQAAGL STPEEGSWRR VVIEKPFGHD
EKSARELNAI VEEVFPPDSI FRIDHYLGKE TVQNILALRF ANQMFEPIWN ANYVDHVQIT
MAEDIGIGGR AGYYDGVGAA RDVIQNHLLQ LMALTAMEEP TSFDARHLRM EKEKVLASTS
LAGSVDDAAV RGQYAAGWQG NEKVGGYLQE EGVADGSVTE TYAALKLAVD TRRWAGVPFY
LRAGKRLGKR VSEIAVVFKR APHLPFSHTA TEELGQNAIV IRVQPDEGVT MRFGSKVPGP
QMEVRDVTMD FGYGNAFTES SPEAYERLIL DVLLGEPPLF PRHEEVELSW RILDPVTARW
ASPQAERPEQ YAAGTWGPAA SDAMMAADGR SWRLP
//
