FGD_NAKMY
ID FGD_NAKMY Reviewed; 339 AA.
AC C8XBB4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=F420-dependent glucose-6-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02123};
DE Short=FGD {ECO:0000255|HAMAP-Rule:MF_02123};
DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_02123};
DE EC=1.1.98.2 {ECO:0000255|HAMAP-Rule:MF_02123};
GN Name=fgd {ECO:0000255|HAMAP-Rule:MF_02123}; OrderedLocusNames=Namu_0967;
OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC Bacteria; Actinobacteria; Nakamurellales; Nakamurellaceae; Nakamurella.
OX NCBI_TaxID=479431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nakamurella multipartita DSM 44233.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-
CC phosphate (G6P) to 6-phosphogluconolactone. {ECO:0000255|HAMAP-
CC Rule:MF_02123}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + H(+) + oxidized coenzyme F420-(gamma-
CC L-Glu)(n) = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420-
CC (gamma-L-Glu)(n); Xref=Rhea:RHEA:27294, Rhea:RHEA-COMP:12939,
CC Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57955,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC EC=1.1.98.2; Evidence={ECO:0000255|HAMAP-Rule:MF_02123};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02123}.
CC -!- SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_02123}.
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DR EMBL; CP001737; ACV77376.1; -; Genomic_DNA.
DR RefSeq; WP_015746290.1; NC_013235.1.
DR AlphaFoldDB; C8XBB4; -.
DR SMR; C8XBB4; -.
DR STRING; 479431.Namu_0967; -.
DR EnsemblBacteria; ACV77376; ACV77376; Namu_0967.
DR KEGG; nml:Namu_0967; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; WRHKGGH; -.
DR OrthoDB; 1434838at2; -.
DR Proteomes; UP000002218; Chromosome.
DR GO; GO:0070967; F:coenzyme F420 binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052749; F:glucose-6-phosphate dehydrogenase (coenzyme F420) activity; IEA:UniProtKB-EC.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.30; -; 1.
DR HAMAP; MF_02123; F420_G6P_DH; 1.
DR InterPro; IPR019944; F420-dep_G6P_DH.
DR InterPro; IPR019945; F420_G6P_DH-rel.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
DR TIGRFAMs; TIGR03554; F420_G6P_DH; 1.
DR TIGRFAMs; TIGR03557; F420_G6P_family; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Oxidoreductase; Reference proteome.
FT CHAIN 1..339
FT /note="F420-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000413597"
FT ACT_SITE 42
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT ACT_SITE 111
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 41
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 78
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 109..110
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 114
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 177..178
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 180..181
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
SQ SEQUENCE 339 AA; 37533 MW; DF31FCC674D02AF3 CRC64;
MTPPPIRFGY KASAEQFGPS ELADLAVAAE EHGFDSVFIS DHLQPWRHDG GHAPASLPWL
GAVGARTQRV ILGTSVLTPT IRYHPGVIAQ AFATLGSMYP GRIVLGVGTG ESLNEVPLGL
AWPEQKERFA RLKESVNLIH ELWTGERVTF EGEYYRTDKA TIYDRPADPV PIYIGASGPA
ATRLAGRIAD GFITTSGKAP SLYTDTLLPA LRDGVEKAGR RLDELDTLME MKVSFDTDRE
RAMQDTRFWA ALALKPEQKA GVEDPLEMQR LADELPIEQA ASRWIVSDDP DEHVEKIRTY
LDLGFRHLVF HAPGHDQQRF LALYGEQILP RLRALVGQG
