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Database: UniProt
Entry: D9VLG0_9ACTN
LinkDB: D9VLG0_9ACTN
Original site: D9VLG0_9ACTN 
ID   D9VLG0_9ACTN            Unreviewed;       327 AA.
AC   D9VLG0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Glucose-6-phosphate dehydrogenase, F420-dependent {ECO:0000313|EMBL:EFL12966.1};
GN   ORFNames=SSNG_00218 {ECO:0000313|EMBL:EFL12966.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL12966.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL12966.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL12966.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657750; EFL12966.1; -; Genomic_DNA.
DR   RefSeq; WP_007261916.1; NZ_GG657750.1.
DR   AlphaFoldDB; D9VLG0; -.
DR   STRING; 253839.SSNG_00218; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_4_0_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd01097; Tetrahydromethanopterin_reductase; 1.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR   InterPro; IPR019945; F420_G6P_DH-rel.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
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   4: Predicted;
FT   DOMAIN          10..290
FT                   /note="Luciferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00296"
SQ   SEQUENCE   327 AA;  35225 MW;  1D488876C3393480 CRC64;
     MTSYGYFLAS EEFTPAELLD QARQAEAAGF TSLAISDHFH PWNDAQGNSP FVWSVIGALS
     QTVDLPITTL VTCPTVRMHP CITAQAAATS SVLTGGRFRF GVGSGEALNE HVHGDPWPPF
     DERADMLREA VQVMRELFGG ERVTHRGRHY TVENARLYTC PDSPPPVYVS GFGPKAAALA
     AEIGDGYVLM GPDRELVDAF RGAGGTGKPV IGGLKVCWHE NRDEAVDTVH RLWPSEQLPG
     ELAQILPTPA HFEQATQLVT RAQVAESTPC GDDPAEHIAA IERYAEAGFD EVYVGQIGPD
     QSAFFDAYRT TVLPALSRGS AESAEAA
//
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