FGD1_RHOJR
ID FGD1_RHOJR Reviewed; 335 AA.
AC Q0RVH7;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=F420-dependent glucose-6-phosphate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_02123};
DE Short=FGD 1 {ECO:0000255|HAMAP-Rule:MF_02123};
DE Short=G6PD 1 {ECO:0000255|HAMAP-Rule:MF_02123};
DE EC=1.1.98.2 {ECO:0000255|HAMAP-Rule:MF_02123};
GN Name=fgd1 {ECO:0000255|HAMAP-Rule:MF_02123};
GN OrderedLocusNames=RHA1_ro11062;
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; ABH00709.1; -; Genomic_DNA.
DR RefSeq; WP_011600337.1; NC_008271.1.
DR PDB; 5LXE; X-ray; 1.47 A; A/B=1-335.
DR PDBsum; 5LXE; -.
DR AlphaFoldDB; Q0RVH7; -.
DR SMR; Q0RVH7; -.
DR STRING; 101510.RHA1_ro11062; -.
DR EnsemblBacteria; ABH00709; ABH00709; RHA1_ro11062.
DR KEGG; rha:RHA1_ro11062; -.
DR PATRIC; fig|101510.16.peg.8893; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_4_0_11; -.
DR OMA; AESACHW; -.
DR BRENDA; 1.1.98.2; 3445.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..335
FT /note="F420-dependent glucose-6-phosphate dehydrogenase 1"
FT /id="PRO_0000413601"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 38
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 75
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 106..107
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02123"
FT BINDING 111
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"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5LXE"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 124..143
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5LXE"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:5LXE"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:5LXE"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:5LXE"
SQ SEQUENCE 335 AA; 36947 MW; D6CA7FA7E9F9EBE9 CRC64;
MVIKFGYKAS AEQFGPRELV ELGVLAEAHG MDSATVSDHF QPWRHEGGHA PFSLAWMTAV
GERTSRLQLG TSVMTPTFRY NPAVVAQAFA TMGCLYPGRI MLGVGTGEAL NEIATGFAGE
WPEFKERFAR LREAVALMRE LWLGDRVDFE GNYYKTVGAS IYDVPEGGIP VYIAAGGPVV
ARYAGRSGDG FICTSGKGME LYTEKLMPAV AEGAEKADRD VAEIDKMIEI KISYDTDPEL
ALENTRFWAP LSLTPEQKHS IDDPIEMERA ADALPIEQVA KRWIVASDPD EAVAQIRPYL
DAGLNHLVFH APGHDQKRFL ELFQRDLAPR LRGLA
