ID A0A1A1YJM5_9MYCO Unreviewed; 336 AA.
AC A0A1A1YJM5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=F420-dependent glucose-6-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02123};
DE Short=FGD {ECO:0000256|HAMAP-Rule:MF_02123};
DE Short=G6PD {ECO:0000256|HAMAP-Rule:MF_02123};
DE EC=1.1.98.2 {ECO:0000256|HAMAP-Rule:MF_02123};
GN Name=fgd {ECO:0000256|HAMAP-Rule:MF_02123};
GN ORFNames=A5724_21265 {ECO:0000313|EMBL:OBF31515.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF31515.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_02123};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02123}.
CC -!- SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate
CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_02123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBF31515.1}.
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DR EMBL; LZHZ01000048; OBF31515.1; -; Genomic_DNA.
DR RefSeq; WP_067805250.1; NZ_LZHZ01000048.1.
DR AlphaFoldDB; A0A1A1YJM5; -.
DR STRING; 1834117.A5724_21265; -.
DR OrthoDB; 180193at2; -.
DR Proteomes; UP000092025; Unassembled WGS sequence.
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 CDD; cd01097; Tetrahydromethanopterin_reductase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 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 NCBIfam; TIGR03554; F420_G6P_DH; 1.
DR NCBIfam; TIGR03557; F420_G6P_family; 1.
DR PANTHER; PTHR43244; -; 1.
DR PANTHER; PTHR43244:SF1; 5,10-METHYLENETETRAHYDROMETHANOPTERIN REDUCTASE; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_02123}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02123};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT DOMAIN 11..307
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 39
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 76
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 107..108
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 112
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 177..178
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 180..181
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
SQ SEQUENCE 336 AA; 37500 MW; A337C7DD58727CCD CRC64;
MAELKLGYKA SAEQFAPREL VELAVAAEEH GMDSATVSDH FQPWRHEGGH APWSLAWMAA
VGERTKRLIL GTSVLTPTFR YNPAVIAQAF ATMGCLYPDR IFLGVGTGEA LNEIATGYEG
EWPEFKERYA RLRESVKLMR ELWLGDRVDF DGEYYRTKGA SIYDVPEGGI PIYIAAGGPQ
VAKYAGRAGD GFICTSGKGE ELYKDKLIPA MREGAEAAGK NPDDVDAMIE IKISYDTDPE
LALENTRFWA PLSLTAEQKH SIDDPIEMEK AADALPIEQV AKRWIVASDP DEAVAKVKDY
VDWGLNHLVF HAPGHDQRRF LELFQRDLEP RLRRLG
//
