ID A0Q376_CLONN Unreviewed; 477 AA.
AC A0Q376;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ABK62113.1};
GN OrderedLocusNames=NT01CX_0612 {ECO:0000313|EMBL:ABK62113.1};
OS Clostridium novyi (strain NT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK62113.1, ECO:0000313|Proteomes:UP000008220};
RN [1] {ECO:0000313|EMBL:ABK62113.1, ECO:0000313|Proteomes:UP000008220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT {ECO:0000313|EMBL:ABK62113.1,
RC ECO:0000313|Proteomes:UP000008220};
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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DR EMBL; CP000382; ABK62113.1; -; Genomic_DNA.
DR RefSeq; WP_011723057.1; NC_008593.1.
DR AlphaFoldDB; A0Q376; -.
DR STRING; 386415.NT01CX_0612; -.
DR KEGG; cno:NT01CX_0612; -.
DR PATRIC; fig|386415.7.peg.2115; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_3_1_9; -.
DR Proteomes; UP000008220; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1.
DR PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008220}.
FT DOMAIN 3..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 397..450
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 477 AA; 51755 MW; E34676B4C0E00936 CRC64;
MFDVTIVGAG VIGCSIAREL SKYNLKVCVL EKGPDVATGT SKANSGIVHG GHDATPGTLK
AKLNVRGNEM FDKLVEELDF PFKRNGSLVL CFDESEKEGL QKLLEKGQKN GVPNLEIIGK
ERILEMEPNV NDDVVGALYV PTGGIVCPYE MTIAMAENAY TNGVEFKFET EVKNVVKKEN
GFTLETSKGN VETNLVINAA GLFSDDLNNM VSKNKIEIIA RKGEYCLFDK TAGAMATKTL
FQLPTKMGKG VLVTPTVDGN LLIGPNAVDV EDKTDVDTTQ EGIDDILNRA KKTFKQIPMR
QVITSFSGLR SHDTVNDFII GEAEDVPGFI NVAGIESPGL SSAPAIAEMV EGIVVEKLSP
AKNDKFNPIR EGIPKFREMT NEERKELIAK DPSYGKIVCR CETVTEGEIL NAIRRPLGAK
DLDGIKRRTR AGMGKCQSGF CSTKIVALLS KELGIPETEV TKFGGKSNLL IGEDKEI
//
