FGD_AMYMU
ID FGD_AMYMU Reviewed; 333 AA.
AC D8I5S8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=AMED_3381;
OS Amycolatopsis mediterranei (strain U-32).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=749927;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-32;
RX PubMed=20567260; DOI=10.1038/cr.2010.87;
RA Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F.,
RA Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N., Zhang Z.,
RA Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S., Ding X.,
RA Zhao G.P.;
RT "Complete genome sequence of the rifamycin SV-producing Amycolatopsis
RT mediterranei U32 revealed its genetic characteristics in phylogeny and
RT metabolism.";
RL Cell Res. 20:1096-1108(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; CP002000; ADJ45167.1; -; Genomic_DNA.
DR RefSeq; WP_013225239.1; NC_014318.1.
DR RefSeq; YP_003765569.1; NC_014318.1.
DR AlphaFoldDB; D8I5S8; -.
DR SMR; D8I5S8; -.
DR STRING; 749927.AMED_3381; -.
DR EnsemblBacteria; ADJ45167; ADJ45167; AMED_3381.
DR KEGG; amd:AMED_3381; -.
DR PATRIC; fig|749927.5.peg.3492; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; WRHKGGH; -.
DR Proteomes; UP000000328; 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..333
FT /note="F420-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000413584"
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 174..175
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 177..178
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
SQ SEQUENCE 333 AA; 37156 MW; 2EE8526E7186727E CRC64;
MLKVGYKASA EQFGPRDLVE YAVRAEEVGL DSVWVSDHFL PWRHEGGHAP WALAWMPAVA
ERTKRVQIGT SVLTPTFRYN PAVIAQAFAT MSLLSNGRVI LGVGSGEALN EIAVSGREWP
EFKERFARLR ESIKLIRELW TSDNVNFKGD YYELVDAKIY DRPEQPVPVY IAAGGPVVAK
YAGRAGDGFI CTSGKGMELY TDKLMPAVKE GAEAAEKTVE DVDRTIEIKL SYDRDHEKAL
ENTRFWAPLS LSAEQKHSVS SAEEMERLAD ELPIDQVAKR WIVASDPDEA VAQIKPYLDA
GLNHLVFHGP GHDQERFLTQ FSEDVLPKLR ALG
