FGD_INTC7
ID FGD_INTC7 Reviewed; 334 AA.
AC E6SFR5;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=Intca_2335;
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS 12989 / 7 KIP).
OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP;
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL Stand. Genomic Sci. 3:294-303(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; CP002343; ADU48844.1; -; Genomic_DNA.
DR RefSeq; WP_013493158.1; NC_014830.1.
DR AlphaFoldDB; E6SFR5; -.
DR SMR; E6SFR5; -.
DR STRING; 710696.Intca_2335; -.
DR EnsemblBacteria; ADU48844; ADU48844; Intca_2335.
DR KEGG; ica:Intca_2335; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; WRHKGGH; -.
DR OrthoDB; 1434838at2; -.
DR Proteomes; UP000008914; 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; Reference proteome.
FT CHAIN 1..334
FT /note="F420-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000413587"
FT ACT_SITE 38
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 37
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 74
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 105..106
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 110
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 176..177
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 179..180
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
SQ SEQUENCE 334 AA; 37084 MW; A809252CF99563D1 CRC64;
MLKVGWKASA EQFGPRELVD HTVRAEQLGF DSVFISDHFQ PWRHRAGHAP FAMSWLAAAG
ERTERVTLGT SVMTPTFRYN PAVVAQAFGT LGALNPGRII LGIGTGEALN EVAVGAAGSP
WPEFKERFAR LREAVTLMRR LWTEERVTFE GDYYRTHDAT IYDRPAEPIP VYVAAGGPLV
ARYAGRSGDG FICTSGKGRE LYADQLLPAV DEGLSRSSRT RDDIDRMIEI KLSYDRDPGA
ALHNVRFWAP LSLTAEQKHG VHDPVEMERL ADELSDEQVA KRWIVTSDPG EAVEQIRQYV
DLGFNHLVVH APGDDQARFL DQFSADVLPG LRGL
