ID A0A1Q5HCD6_9ACTN Unreviewed; 557 AA.
AC A0A1Q5HCD6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OKJ42499.1};
GN ORFNames=AMK22_06450 {ECO:0000313|EMBL:OKJ42499.1};
OS Streptomyces sp. CB01580.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703933 {ECO:0000313|EMBL:OKJ42499.1, ECO:0000313|Proteomes:UP000186318};
RN [1] {ECO:0000313|EMBL:OKJ42499.1, ECO:0000313|Proteomes:UP000186318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01580 {ECO:0000313|EMBL:OKJ42499.1,
RC ECO:0000313|Proteomes:UP000186318};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:OKJ42499.1}.
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DR EMBL; LIXJ01000003; OKJ42499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5HCD6; -.
DR STRING; 1703933.AMK22_06450; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000186318; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap 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; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186318}.
FT DOMAIN 38..400
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..532
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 557 AA; 59996 MW; 1C9CABE7D0AAF4C6 CRC64;
MITMPARKPR RNAAATRRTP LLLDRAALKR RLADDTYDVL VIGGGITGAY AVLDAVSRGL
RAALIEKDDF ASGTSSKSSK MVHGGLRYIE QGNVNLVRHS LLERHRFRKN APHLVHRLPF
LFPILEKEGI FDARLAKGFE GLLWTYDLVG GWRIGKLHQR LTVPEVLAQA PTLRAENLKG
GLMYFDARTD DARLVLTIVR TAAALGATVL NGAKAEGLLM QMGKVSGARV TADGDTLDIR
ARAVVNATGV WTDELDAKAD EGHRPQVRPA KGVHIVVPWD KVRINCTVTV PIPGRARRAT
CTRWGNSVVL GTTDEDYQGS ADDVHCTRRE MDFLLEGANT AFEGKLTPDD VVGSIGGLRP
LVGGKEGATL DMRRDHHITV GRTGMVTVTG GKLTTSRHMG ELVIDKVMTV LGRRAKSRTA
DLPLLGGAGY DSEAVAASGG IAAHLGERFG TEARFVGDLI QDDPSLAEPV VAGLPYTKAE
VVYAARAELA RSVDDVLSRR TRARLFARDA SADAAEAVGA ILGRELNLTE AEVERSVAEY
LAAVRHEKSV LLEGAAA
//
