ID A0A0F5VXZ4_9ACTN Unreviewed; 461 AA.
AC A0A0F5VXZ4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KKD06210.1};
GN ORFNames=TN53_20440 {ECO:0000313|EMBL:KKD06210.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD06210.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD06210.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD06210.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (JAN-2015) 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:KKD06210.1}.
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DR EMBL; JXTE01000031; KKD06210.1; -; Genomic_DNA.
DR RefSeq; WP_046260008.1; NZ_JXTE01000031.1.
DR AlphaFoldDB; A0A0F5VXZ4; -.
DR PATRIC; fig|1415558.3.peg.4092; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000033641; 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; COENZYME A DISULFIDE REDUCTASE; 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:UP000033641}.
FT DOMAIN 9..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..443
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 461 AA; 48828 MW; 520CAB7D02D8AAAD CRC64;
MNISAANERL VVIGGDAAGM SAASQARRLK GPGELEIVAF ERGHFTSYSA CGIPYWVGGD
VEERDQLIAR TPEEHRARDI DLRLRTEVTE IDVAGQRVRA RDVDSGAESW TSYDKLVIAT
GARPIRPEMP GADAPGVHGV QTLDDGQALL DTLTRTRGRK AVVVGAGYIG VEMAEALINR
GYEVTVVNRG SEPMSTLDAD MGRLVHEAME GMGITMVNDA EATKVLTGED GRVRAVATQD
AEYPADVVVL GIGVRPETSL AKAAGLPVGH HDGLLTDLAM RVRGHENIWA GGDCVEVLDL
VSGQERHIAL GTHANKHGQV IGANVGGGYA TFPGVVGTAV SKVCDLEIAR TGLREKDARR
AGLQFETVTV ESTSRAGYYP GASPMTVKML AERRTGRLLG VQIVGREGAG KRVDIAAVAL
TAGMTVERMT ALDLGYAPPF SPVWDPVLVA ARKAALKVRA S
//
