FGD_MYCS2
ID FGD_MYCS2 Reviewed; 336 AA.
AC A0QQJ4; I7G2C9; O68447;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=F420-dependent glucose-6-phosphate dehydrogenase;
DE Short=FGD;
DE Short=G6PD;
DE EC=1.1.98.2;
GN Name=fgd; Synonyms=fgd1; OrderedLocusNames=MSMEG_0777, MSMEI_0761;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=9555906; DOI=10.1128/jb.180.8.2212-2219.1998;
RA Purwantini E., Daniels L.;
RT "Molecular analysis of the gene encoding F420-dependent glucose-6-phosphate
RT dehydrogenase from Mycobacterium smegmatis.";
RL J. Bacteriol. 180:2212-2219(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP PROTEIN SEQUENCE OF 2-27, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 607 / DSM 43465 / mc(2)6 / NCTC 7017 / NRRL B-692;
RX PubMed=8631674; DOI=10.1128/jb.178.10.2861-2866.1996;
RA Purwantini E., Daniels L.;
RT "Purification of a novel coenzyme F420-dependent glucose-6-phosphate
RT dehydrogenase from Mycobacterium smegmatis.";
RL J. Bacteriol. 178:2861-2866(1996).
RN [6]
RP STEREOSPECIFICITY.
RC STRAIN=ATCC 607 / DSM 43465 / mc(2)6 / NCTC 7017 / NRRL B-692;
RX PubMed=8706724; DOI=10.1111/j.1432-1033.1996.0093u.x;
RA Klein A.R., Berk H., Purwantini E., Daniels L., Thauer R.K.;
RT "Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent
RT glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis and F420-
RT dependent alcohol dehydrogenase from Methanoculleus thermophilicus.";
RL Eur. J. Biochem. 239:93-97(1996).
RN [7]
RP ROLE IN RESISTANCE TO OXIDATIVE STRESS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=20075070; DOI=10.1074/jbc.m109.074310;
RA Hasan M.R., Rahman M., Jaques S., Purwantini E., Daniels L.;
RT "Glucose 6-phosphate accumulation in mycobacteria: implications for a novel
RT F420-dependent anti-oxidant defense system.";
RL J. Biol. Chem. 285:19135-19144(2010).
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. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420
CC as an electron acceptor. Exhibits nearly no activity with D-mannose-6-
CC phosphate or D-fructose-6-phosphate as substrate.
CC {ECO:0000269|PubMed:20075070, ECO:0000269|PubMed:8631674}.
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:0000269|PubMed:8631674,
CC ECO:0000269|PubMed:9555906};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.004 mM for coenzyme F420 (at pH 7 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:8631674};
CC KM=1.6 mM for D-glucose 6-phosphate (at pH 7 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:8631674};
CC pH dependence:
CC Optimum pHs are 5.5 and 8.0. {ECO:0000269|PubMed:8631674};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:8631674};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8631674}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are more sensitive than
CC the wild-type to oxidative stress induced by plumbagin and menadione.
CC They display decreased ability to consume G6P and reduce plumbagin and
CC menadione when exposed to these agents. {ECO:0000269|PubMed:20075070}.
CC -!- MISCELLANEOUS: Exhibits Si-face stereospecificity with respect to C5 of
CC coenzyme F420.
CC -!- SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK75077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF041061; AAC38338.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK75077.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP37241.1; -; Genomic_DNA.
DR RefSeq; WP_003892203.1; NZ_SIJM01000036.1.
DR RefSeq; YP_885182.1; NC_008596.1.
DR AlphaFoldDB; A0QQJ4; -.
DR SMR; A0QQJ4; -.
DR STRING; 246196.MSMEI_0761; -.
DR PRIDE; A0QQJ4; -.
DR EnsemblBacteria; ABK75077; ABK75077; MSMEG_0777.
DR EnsemblBacteria; AFP37241; AFP37241; MSMEI_0761.
DR GeneID; 66738952; -.
DR KEGG; msg:MSMEI_0761; -.
DR KEGG; msm:MSMEG_0777; -.
DR PATRIC; fig|246196.19.peg.772; -.
DR eggNOG; COG2141; Bacteria.
DR OrthoDB; 1434838at2; -.
DR BRENDA; 1.1.98.2; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0070967; F:coenzyme F420 binding; IDA:UniProtKB.
DR GO; GO:0052749; F:glucose-6-phosphate dehydrogenase (coenzyme F420) activity; IEA:UniProtKB-EC.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8631674"
FT CHAIN 2..336
FT /note="F420-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000413596"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000250"
FT BINDING 177..178
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000250"
FT BINDING 180..181
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 37176 MW; F1C1A24353E2BF98 CRC64;
MAELKLGYKA SAEQFAPREL VELAVLAESA GMDSATVSDH FQPWRHEGGH APFSLAWMTA
VGERTKNLVL GTSVLTPTFR YNPAVIAQAF ATMGCLYPGR IFLGVGTGEA LNEIATGYAG
EWPEFKERFA RLRESVRLMR ELWLGDRVDF DGEYYRTKGA SIYDVPEGGI PVYIAAGGPV
VAKYAGRAGD GFICTSGKGE ELYAEKLIPA VKEGAAAADR DADAIDRMIE IKISYDTDPE
LALENTRFWA PLSLTAEQKH SIDDPIEMEK AADALPIEQV AKRWIVASDP DEAVEKVGQY
VKWGLNHLVF HAPGHDQRRF LELFKRDLEP RLRKLA
