ID A0A1K1SL08_9PSEU Unreviewed; 334 AA.
AC A0A1K1SL08;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04489730_6008 {ECO:0000313|EMBL:SFW85001.1};
OS Amycolatopsis australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW85001.1, ECO:0000313|Proteomes:UP000182740};
RN [1] {ECO:0000313|EMBL:SFW85001.1, ECO:0000313|Proteomes:UP000182740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW85001.1,
RC ECO:0000313|Proteomes:UP000182740};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FPJG01000006; SFW85001.1; -; Genomic_DNA.
DR RefSeq; WP_072479411.1; NZ_FPJG01000006.1.
DR AlphaFoldDB; A0A1K1SL08; -.
DR STRING; 546364.SAMN04489730_6008; -.
DR OrthoDB; 180193at2; -.
DR Proteomes; UP000182740; 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}.
FT DOMAIN 10..304
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 38
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 75
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 106..107
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 111
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 175..176
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 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
SQ SEQUENCE 334 AA; 37138 MW; 7A127FB5FA9BD178 CRC64;
MALKVGYKAS AEQFGPRELV EYAVRAEEVG LDSVWVSDHF LPWRHEGGHA PFALAWMPAV
AERTKRVQIG TSVLTPTFRY NPAVIAQAFA TMSLLSNGRV ILGVGTGEAL NEIAVSGREW
PEFKERFARL RESIKLMREL WTSDDVNFDG DYYKLVNAKI YDRPEQPVPV YVAAGGPVVA
KYAGRSGDGF ICTSGKGMDL YTEKLIPAVK EGAEAASRDA EGIDRTIEIK MSYDRDPEQA
LENTRFWAPL SLSAEQKHSV SSAEEMERLA DELPIEQVAK RWIVASDPDE AVAQIKPYLD
AGLNHLVFHG PGHDQERFLT QFSEDVLPKL RALA
//
