ID K6WT58_9MICO Unreviewed; 339 AA.
AC K6WT58;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=fdg {ECO:0000313|EMBL:GAB97021.1};
GN Synonyms=fgd {ECO:0000256|HAMAP-Rule:MF_02123};
GN ORFNames=KILIM_054_00310 {ECO:0000313|EMBL:GAB97021.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB97021.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB97021.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB97021.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:GAB97021.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAHD01000054; GAB97021.1; -; Genomic_DNA.
DR RefSeq; WP_006593553.1; NZ_BAHD01000054.1.
DR AlphaFoldDB; K6WT58; -.
DR STRING; 1184609.KILIM_054_00310; -.
DR eggNOG; COG2141; Bacteria.
DR OrthoDB; 180193at2; -.
DR Proteomes; UP000008366; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008366}.
FT DOMAIN 8..307
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 177..178
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02123"
SQ SEQUENCE 339 AA; 37409 MW; 38D3DD1AE8AE028F CRC64;
MSVRIGYKAS SEQFAPAQLA GFAIRAEELG FDSAFIADHF QPWRHTGGHA PASIPWLAHV
AARTQRIVLG TSVMTPTFRY NPAVIAQAFA TMACLTPGRI VLGVGTGEAL NEMAVGSVEG
DWPEFKERFA RLREAVEVMR GLWAGERFSF AGEYYRTEEA TIYDLPDEPV PVYIAAGGPM
VARYAGRYGD GFICTSGKGR ELYEDKLLPA VAEGLEKKGR AHGSIDRMIE IKISYDRDPV
RALENTRFWA PLSLSPEQKH SLHDPAQMEA AADELPIEQV AKRWIVASSG PEAIEAMREY
VDLGFTHLVV HGPGHDQERF LTQFAEDVLP GLREFGQEG
//
