ID A0A136PXL0_9ACTN Unreviewed; 459 AA.
AC A0A136PXL0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KXK63087.1};
GN ORFNames=AWW66_04670 {ECO:0000313|EMBL:KXK63087.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK63087.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK63087.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK63087.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) 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:KXK63087.1}.
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DR EMBL; LRQV01000009; KXK63087.1; -; Genomic_DNA.
DR RefSeq; WP_067360247.1; NZ_LRQV01000009.1.
DR AlphaFoldDB; A0A136PXL0; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000070620; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070620}.
FT DOMAIN 4..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 459 AA; 48396 MW; C87675DD346A63BC CRC64;
MAERLIVIGG DAAGMSAASQ ARRRRGRNDL EIVAFERGHF TSYSACGIPY WIGGLVPERD
QLIARAPQTF RDEYDIDVRL QHEVTAIDLG RREVVARDLA GGGEVRAGFD TLVYAVGATP
RLPDWARSGV AGVFGVQTLD DGAALRDWLE AEPRPRRAVV VGGGYIGVEM AEALVQRGLD
VTLVERGEQP MSTVDDDMAV LVAAAMRGVG IEIRTGVEVT GLTEQDGRVS AVVTDDGPLP
ADVVVLGLGV RPNTALAEAA GLPLGPSGGV QVDRRMRVLG VPGVWAAGDC VETLHRVSGL
PVHVPLGTHA NKQGRVAGIN IGGGYATFPG VIGTAVTKVC ELEVGRTGLR ERDAHAAGFE
FVSVVIESTN RAGYYPGARP MTVKLIAERP SGRLLGAQIV GWSEAAKRID ALAVALWNGM
TVDDMTALDL GYAPPYAPVW DPVLVAARTA VDALAAHSR
//
