FGD_RHOH1
ID FGD_RHOH1 Reviewed; 337 AA.
AC E4W8Y2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=REQ_39220;
OS Rhodococcus hoagii (strain 103S) (Rhodococcus equi).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=685727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103S;
RX PubMed=20941392; DOI=10.1371/journal.pgen.1001145;
RA Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C.,
RA Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R., Hapeshi A.,
RA Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A., Sanders M.,
RA Scortti M.M., Prescott J.F., Fogarty U., Meijer W.G., Parkhill J.,
RA Bentley S.D., Vazquez-Boland J.A.;
RT "The genome of a pathogenic rhodococcus: cooptive virulence underpinned by
RT key gene acquisitions.";
RL PLoS Genet. 6:E1001145-E1001145(2010).
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; FN563149; CBH49907.1; -; Genomic_DNA.
DR RefSeq; WP_005517853.1; NZ_VEFT01000001.1.
DR AlphaFoldDB; E4W8Y2; -.
DR SMR; E4W8Y2; -.
DR STRING; 685727.REQ_39220; -.
DR EnsemblBacteria; CBH49907; CBH49907; REQ_39220.
DR GeneID; 57579562; -.
DR KEGG; req:REQ_39220; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; WRHKGGH; -.
DR OrthoDB; 1434838at2; -.
DR Proteomes; UP000006892; 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..337
FT /note="F420-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000413599"
FT ACT_SITE 41
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT ACT_SITE 110
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 40
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 77
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 108..109
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 113
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 178..179
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 181..182
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
SQ SEQUENCE 337 AA; 37118 MW; 4AA11BADE3CC6742 CRC64;
MVQGLKLGLK ASAEQFGPRD LVELGVMAEE HGLDSVTVSD HFQPWRHNGG HAPFSIAWMT
AVGERTQRLQ LGTSVMTPTF RYNPAVVAQA FATMGCLYPG RVMLGVGTGE ALNEIATGFK
GEWPEFKERF ARLRESVQLM RDLWTGDRVD FEGEYYSTKG ASIYDVPEGG IPVYIAAGGP
VVARYAGRAG EGFICTSGKG MDLYTEKLIP AVKEGAEKAA RNFADIDRMI EIKISYDTDP
AAALENTRFW APLSLTAEQK HSIDDPIEME AAADALPIEQ VAKRWIVSSD PDEAVEMIKP
YLDAGLNHLV FHAPGHDQKR FLDLFERDLA PRLRALA
