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Database: UniProt
Entry: G2NHG9_STREK
LinkDB: G2NHG9_STREK
Original site: G2NHG9_STREK 
ID   G2NHG9_STREK            Unreviewed;       430 AA.
AC   G2NHG9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:AEN09953.1};
GN   ORFNames=SACTE_2051 {ECO:0000313|EMBL:AEN09953.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09953.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN09953.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN09953.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; CP002993; AEN09953.1; -; Genomic_DNA.
DR   RefSeq; WP_014045939.1; NC_015953.1.
DR   AlphaFoldDB; G2NHG9; -.
DR   STRING; 862751.SACTE_2051; -.
DR   KEGG; ssx:SACTE_2051; -.
DR   PATRIC; fig|862751.12.peg.2134; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_018354_10_0_11; -.
DR   OrthoDB; 9775082at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397}.
FT   DOMAIN          12..180
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   430 AA;  44613 MW;  25720E78D52BBCE1 CRC64;
     MTAAPASFQT GFTLSPGVLV DAADAADVRE AVRRAADRRL SVAVHATGHG LPGPVEGGML
     IATHRMDGVT VDPERHTARV AAGTPWGRVI EAAAVHGLAP LNGSSPGVGA VSYTLGGGLG
     ILAREFGYAA DHVRSLDVVT ADGVAREVTP TGEPDLFWGL RGGGHRLGVV TGLEIGLVPV
     ARLYGGAVAY DGEHAAEVVR GYLEWTRTLP DTCTSSLSAM TYPDLPQVPE AVRGRYLVSV
     RIAYTGGAAD GEALVAPLRT TAPVASDSLR EMPYTESHTI HSDPPFPHAY YGDSAVLRDL
     DAVAAARVLE LTGPQAPMMT VVQLNHLGGA LAAPPAAAGA VPYREAGFLL RLLSPLGGTD
     VAAVRSLYGE VTGLLAPHLM GRALNFSFGG GDRTDGFHAP RTRERLAGLV SRYDPASLFG
     GPYGVSRDAR
//
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