ID A0A418KWH3_9ACTN Unreviewed; 342 AA.
AC A0A418KWH3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ECO:0000313|EMBL:RIQ34058.1};
GN ORFNames=DY240_04440 {ECO:0000313|EMBL:RIQ34058.1};
OS Jiangella rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Jiangella.
OX NCBI_TaxID=2293569 {ECO:0000313|EMBL:RIQ34058.1, ECO:0000313|Proteomes:UP000284057};
RN [1] {ECO:0000313|EMBL:RIQ34058.1, ECO:0000313|Proteomes:UP000284057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY265 {ECO:0000313|EMBL:RIQ34058.1,
RC ECO:0000313|Proteomes:UP000284057};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-
CC phosphate (G6P) to 6-phosphogluconolactone. {ECO:0000256|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: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:RIQ34058.1}.
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DR EMBL; QUAL01000037; RIQ34058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418KWH3; -.
DR OrthoDB; 180193at2; -.
DR Proteomes; UP000284057; 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};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02123,
KW ECO:0000313|EMBL:RIQ34058.1}.
FT DOMAIN 12..308
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT ACT_SITE 41
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT ACT_SITE 110
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 40
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 77
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 108..109
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 113
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 178..179
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 181..182
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
SQ SEQUENCE 342 AA; 37623 MW; 92D9CA0A7FD69BB2 CRC64;
MGRTLKLGYK ASAEQFGARD LVEYGVLAEQ AGMDSAVVSD HFQPWRHNGG HAPFSLAWMT
AVGERTSTIT LGTSVLTPTF RYNPAVIAQS FATMGCLYPG RIILGVGTGE ALNEIATGFR
GTWPEFKERF ARLRESVDLI RRLWSGERVD FDGEYYAAAG ASIYDVPKDG IPIYVAAGGP
VVARYAGRAA DGFICTSGKG MDLYTEKLVP AVKEGKEQSG QPDRDVDHLI EIKLSYDRDP
QAALENTRFW APLSLTPEQK HSVDDPIEME RLADELPLEQ VAKRWIVASD PQAVVDAVRP
YVEAGFNHLV FHAPGADQRR FFEQFEADLA APLRQLSSAL PD
//
