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Database: UniProt
Entry: A0A1Q5KT35_9ACTN
LinkDB: A0A1Q5KT35_9ACTN
Original site: A0A1Q5KT35_9ACTN 
ID   A0A1Q5KT35_9ACTN        Unreviewed;       409 AA.
AC   A0A1Q5KT35;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OKJ84764.1};
GN   ORFNames=AMK32_12335 {ECO:0000313|EMBL:OKJ84764.1};
OS   Streptomyces sp. CB01883.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ84764.1, ECO:0000313|Proteomes:UP000186398};
RN   [1] {ECO:0000313|EMBL:OKJ84764.1, ECO:0000313|Proteomes:UP000186398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01883 {ECO:0000313|EMBL:OKJ84764.1,
RC   ECO:0000313|Proteomes:UP000186398};
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   -!- 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:OKJ84764.1}.
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DR   EMBL; LIWA01000002; OKJ84764.1; -; Genomic_DNA.
DR   RefSeq; WP_073891312.1; NZ_LIWA01000002.1.
DR   AlphaFoldDB; A0A1Q5KT35; -.
DR   OrthoDB; 9806257at2; -.
DR   Proteomes; UP000186398; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000186398}.
FT   DOMAIN          8..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          385..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  41990 MW;  43FA61E2696C38C9 CRC64;
     MTKRLTCDVV VVGAGMVGAA CALYAARAGL DVRVVDRGAV AGGTTGAGEG NLLVSDKEPG
     PELELALLSA GLWTELAEEL GRAIEYEPKG GLVVASTPDA LSALAAFAAG QRAAGVTAEP
     VAPDELLTLE PHLAPGLAGG VLYPQDAQVM PALAAAHLLR ASGAAVHTGH TVTDVLRAAD
     GPVRGVRTDR GDIHASAVVN AAGTWAADLA SLAGVRLPVL PRRGFVLVTE PLPRMVRHKV
     YAADYVADVA SDSAALRASP VVEGTAAGPV LIGATRERVG FDRSLSLPAV RALAAGAIGL
     FPFLARVHAQ RTYAGFRPYL PDHLPAIGPD PRAPGLFHAC GHEGAGIGLA PGTGQLIAHA
     LTGGVTGQDI APFRPERFED ARFEDDGYED DAFKDDAFKD EFDDGGEAR
//
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