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Database: UniProt
Entry: A0A2U2Z9M2_9ACTN
LinkDB: A0A2U2Z9M2_9ACTN
Original site: A0A2U2Z9M2_9ACTN 
ID   A0A2U2Z9M2_9ACTN        Unreviewed;       466 AA.
AC   A0A2U2Z9M2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:PWI08998.1};
GN   ORFNames=DIZ27_19620 {ECO:0000313|EMBL:PWI08998.1};
OS   Streptomyces sp. NWU339.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI08998.1, ECO:0000313|Proteomes:UP000245372};
RN   [1] {ECO:0000313|EMBL:PWI08998.1, ECO:0000313|Proteomes:UP000245372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NWU339 {ECO:0000313|EMBL:PWI08998.1,
RC   ECO:0000313|Proteomes:UP000245372};
RA   Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT   "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT   South African rhizosphere soils.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:PWI08998.1}.
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DR   EMBL; QFRK01000015; PWI08998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2Z9M2; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000245372; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43429:SF1; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245372}.
FT   DOMAIN          2..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          332..434
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   466 AA;  49504 MW;  5D71201CBA448810 CRC64;
     MVVIGGDAAG MAAASRARRL KGPDELEIVA FERGRFTSFS ACGIPYWVGG DITDRDTLIA
     RTPEEHRARD IDLRLRTEVT EIDPDRGRVR ARDVESGAES WTSYDKLVIA TGARPIRPEL
     PGMDAPGVHG VQTLDDGQAL LDTLARTDGR RAVVVGAGYI GVEMAEAMIN RGYEVTVVNR
     GREPMATLDP DMGLLVHKAM EGLGITMVND TEVTGLVTGD DGRVRAVATA DARYPADVVV
     LGIGVRPETD LARAAGLPLG EHGGLLTDRS MRVRGHENVW AGGDCVEVLD LISGQERHIP
     LGTHANKHGQ IIGSNVGGDY ATFPGVVGTA VSKVCDLEIA RTGLREKDAH RAGLRFEAVT
     IESTSRAGYY PNASPMTVKM LAELRTGRLL GVQIVGREGA GKRVDIAAVA LTAGMTVEQM
     TMLDLGYAPP FSPTWDPVLV AARKATARIR ATAGGPTPPA GPTRSR
//
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