FGD2_RHOJR
ID FGD2_RHOJR Reviewed; 337 AA.
AC Q0RV73;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=F420-dependent glucose-6-phosphate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_02123};
DE Short=FGD 2 {ECO:0000255|HAMAP-Rule:MF_02123};
DE Short=G6PD 2 {ECO:0000255|HAMAP-Rule:MF_02123};
DE EC=1.1.98.2 {ECO:0000255|HAMAP-Rule:MF_02123};
GN Name=fgd2 {ECO:0000255|HAMAP-Rule:MF_02123};
GN OrderedLocusNames=RHA1_ro11166;
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL3.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000434; ABH00813.1; -; Genomic_DNA.
DR RefSeq; WP_011600440.1; NC_008271.1.
DR AlphaFoldDB; Q0RV73; -.
DR SMR; Q0RV73; -.
DR STRING; 101510.RHA1_ro11166; -.
DR EnsemblBacteria; ABH00813; ABH00813; RHA1_ro11166.
DR KEGG; rha:RHA1_ro11166; -.
DR PATRIC; fig|101510.16.peg.8986; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; KADGFIC; -.
DR Proteomes; UP000008710; Plasmid pRHL3.
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; Plasmid; Reference proteome.
FT CHAIN 1..337
FT /note="F420-dependent glucose-6-phosphate dehydrogenase 2"
FT /id="PRO_0000413602"
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; 37281 MW; 361B7F7530C2FDBC CRC64;
MTQQLKLGYK ASAEQFGPRE LVELAVLAEK HGMDSATVSD HFQPWRHNGG HAPFSLSWMT
AVGERTKRLQ LGTSVLTPTF RYNPAVIAQA FATMGCLYPG RIMLGAGTGE ALNEIATGYT
GQWPEFRERY ARLRESVQLM RDLWTGERTD FKGEYYSTTG ASIYDVPECG IPVYIAAGGP
VVARYAGRAG DGFICTSGKG MELYTDKLMP AVSEGATKAE RDVTSIDKMI EIKISYDTDP
EAALENTRFW APLSLTQEQK HSIEDPIEME AAADALPIEQ VAKRWIVSSD PDDAVAQVKQ
YIDAGLNHLV FHAPGHDQKR FLELFDRDLA PRLRALG
