FGD_MYCTO
ID FGD_MYCTO Reviewed; 336 AA.
AC P9WNE0; L0T6D5; P96253; Q7D9V4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=FGD1 {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=fgd1; Synonyms=fgd; OrderedLocusNames=MT0420;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-
CC phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in
CC resistance to oxidative stress, via its consumption of G6P that serves
CC as a source of reducing power to combat oxidative stress in
CC mycobacteria. More precisely, is likely involved in a F420-dependent
CC anti-oxidant mechanism that protects M.tuberculosis against oxidative
CC stress and bactericidal agents. {ECO:0000250|UniProtKB:P9WNE1,
CC ECO:0000255|HAMAP-Rule:MF_02123}.
CC -!- FUNCTION: Is essential for the bioreductive activation of the bicyclic
CC 4-nitroimidazole prodrug PA-824 (nitroimidazo-oxazine) developed for
CC anti-tuberculosis therapy against both replicating and persistent
CC bacteria. It does not interact directly with PA-824 but, rather,
CC provides reduced F420 to the deazaflavin-dependent nitroreductase Ddn,
CC which in turn activates PA-824. {ECO:0000250|UniProtKB:P9WNE1}.
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; AE000516; AAK44644.1; -; Genomic_DNA.
DR PIR; E70628; E70628.
DR RefSeq; WP_003898438.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNE0; -.
DR SMR; P9WNE0; -.
DR EnsemblBacteria; AAK44644; AAK44644; MT0420.
DR KEGG; mtc:MT0420; -.
DR PATRIC; fig|83331.31.peg.449; -.
DR HOGENOM; CLU_027853_4_0_11; -.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..336
FT /note="F420-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000427143"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 39
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 76
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 107..108
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 112
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 336 AA; 36989 MW; A25059725E3A60B3 CRC64;
MAELKLGYKA SAEQFAPREL VELAVAAEAH GMDSATVSDH FQPWRHQGGH APFSLSWMTA
VGERTNRLLL GTSVLTPTFR YNPAVIAQAF ATMGCLYPNR VFLGVGTGEA LNEIATGYEG
AWPEFKERFA RLRESVGLMR QLWSGDRVDF DGDYYRLKGA SIYDVPDGGV PVYIAAGGPA
VAKYAGRAGD GFICTSGKGE ELYTEKLMPA VREGAAAADR SVDGIDKMIE IKISYDPDPE
LALNNTRFWA PLSLTAEQKH SIDDPIEMEK AADALPIEQI AKRWIVASDP DEAVEKVGQY
VTWGLNHLVF HAPGHDQRRF LELFQSDLAP RLRRLG
