FGD_MYCLB
ID FGD_MYCLB Reviewed; 336 AA.
AC B8ZU74;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=MLBr00269;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(2009).
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. {ECO:0000255|HAMAP-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; FM211192; CAR70362.1; -; Genomic_DNA.
DR RefSeq; WP_010907639.1; NC_011896.1.
DR AlphaFoldDB; B8ZU74; -.
DR SMR; B8ZU74; -.
DR EnsemblBacteria; CAR70362; CAR70362; MLBr00269.
DR KEGG; mlb:MLBr00269; -.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; WRHKGGH; -.
DR OrthoDB; 1434838at2; -.
DR Proteomes; UP000006900; 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_0000413595"
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; 37199 MW; 12DAA450AEC93DCB CRC64;
MAELRLGYKA SAEQFAPREL VELGVAAEAH GMDSATVSDH FQPWRHQGGH ASFSLSWMTA
VGERTNRILL GTSVLTPTFR YNPAVIGQAF ATMGCLYPNR VFLGVGTGEA LNEVATGYQG
AWPEFKERFA RLRESVRLMR ELWRGDRVDF DGDYYQLKGA SIYDVPEGGV PIYIAAGGPE
VAKYAGRAGE GFVCTSGKGE ELYTEKLIPA VLEGAAVAGR DADDIDKMIE IKMSYDPDPE
QALSNIRFWA PLSLAAEQKH SIDDPIEMEK VADALPIEQV AKRWIVVSDP DEAVARVGQY
VTWGLNHLVF HAPGHNQRRF LELFEKDLAP RLRRLG
