ID U5E9A4_NOCAS Unreviewed; 485 AA.
AC U5E9A4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:GAD83955.1};
GN ORFNames=NCAST_20_05250 {ECO:0000313|EMBL:GAD83955.1};
OS Nocardia asteroides NBRC 15531.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD83955.1, ECO:0000313|Proteomes:UP000017048};
RN [1] {ECO:0000313|EMBL:GAD83955.1, ECO:0000313|Proteomes:UP000017048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD83955.1,
RC ECO:0000313|Proteomes:UP000017048};
RX PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA Suzuki K., Fujita N., Gonoi T.;
RT "Genome based analysis of type-I polyketide synthase and nonribosomal
RT peptide synthetase gene clusters in seven strains of five representative
RT Nocardia species.";
RL BMC Genomics 15:323-323(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:GAD83955.1}.
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DR EMBL; BAFO02000020; GAD83955.1; -; Genomic_DNA.
DR RefSeq; WP_019049216.1; NZ_VBUS01000001.1.
DR AlphaFoldDB; U5E9A4; -.
DR STRING; 1824.SAMN05444423_1011260; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000017048; 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; 3.30.390.30; -; 1.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 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 FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000017048}.
FT DOMAIN 9..324
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 362..468
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 185..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 46..51
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 485 AA; 51479 MW; 2E4948CC7E91FCB5 CRC64;
MSDNETRSYD VVVIGAGPVG ENVADRTSAA GLRTVIVEAE LVGGECSYWA CEPSKAMLRP
ALLHREAARF PGVAGAVTGG LDAAAVLKHR DRMAAEWNDQ DQLAWLDSVR VDLVRGHGRL
DGPKRVTVRT PDGGTVRLLA RHAVALCTGT TAALPPLPDL DALRPWTSRE ATAARSVPDR
LAILGAGVVA VEMATAWQAL GARVTLIARE SRLLGRVEPF AADLVTERLR EAGVDLRLGT
TIETATRVGD EVHLALADGT ELVADELLLA TGRAPRTTDL GVDTVGLRPG GWLSTDDTLT
VTAVEGEWLY AVGDVNRRAL LTHQGKYQAR ITGAVIAARA RGQALDTGRW GAHTATADLD
AVPQVVFTDP EIASVGLTTA DAARIGRAVH VVDYEIGHVA GAIQHDPEYR GRARVLLDPD
RGVVVGATFA GPGVAELLHS ATIAITGEVP LQRLWHAVPS FPTIGEVWLR LLETYRDQQG
EEAVA
//
