ID A0A1C9WPS9_9MICC Unreviewed; 454 AA.
AC A0A1C9WPS9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AOT03267.1};
GN ORFNames=ASPU41_07865 {ECO:0000313|EMBL:AOT03267.1};
OS Arthrobacter sp. U41.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1849032 {ECO:0000313|EMBL:AOT03267.1, ECO:0000313|Proteomes:UP000095776};
RN [1] {ECO:0000313|EMBL:AOT03267.1, ECO:0000313|Proteomes:UP000095776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U41 {ECO:0000313|EMBL:AOT03267.1,
RC ECO:0000313|Proteomes:UP000095776};
RA Fomenkov A., Akimov V.N., Vasilyeva L.V., Andersen D., Vincze T.,
RA Roberts R.J.;
RT "Complete Genome and Methylome Analysis of Psychrotrophic Bacterial
RT Isolates from Antarctic Lake Untersee.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP015732; AOT03267.1; -; Genomic_DNA.
DR RefSeq; WP_069950452.1; NZ_CP015732.1.
DR AlphaFoldDB; A0A1C9WPS9; -.
DR STRING; 1849032.ASPU41_07865; -.
DR KEGG; aru:ASPU41_07865; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000095776; Chromosome.
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; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000095776}.
FT DOMAIN 5..314
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..443
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 135..137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 172..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 454 AA; 48616 MW; C1ECCD80DC79EA98 CRC64;
MEEHFDVAVL GMGPGGEVAA SRLLKAHKKV AVIERELIGG ECAYWACVPS KTLLRPPEAK
TAAARSAGVT GAELDWAAAS DYRDYMIRHL DDKAQIDGYK GQGATVIKAE ARITGPGTLQ
AGGRTIHADH IIIATGSEAV MPELEGAENV TIWTNRETFT TTTLPRRAVV IGGSAVGTET
ATFLARFGVD VTLVHRGKAL MEREEPRVGE LTRLYLEEAG VNVRLASHAV RARREGDSSS
LELDDGTSVG TDVVIFATGR RPRSKDLGFE AAGVKLDPKG AVVIDEQCRA GEGVWAGGDV
TAVMPFTHVA KYQGRIVADA ILGHARPATY DGIPRVVFGD PEIAAAGITQ AQADEQGLST
AFAELDLAES LTRPWTYEQE PRGHLGLLTD TNTGTLIGAW AVSPLAGEWI HQASLAIRAR
IPLAVLHDQV AQFPSYSEAF HMALDNLKYR KELL
//
