ID A0JSP4_ARTS2 Unreviewed; 488 AA.
AC A0JSP4;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase dimerization region {ECO:0000313|EMBL:ABK02064.1};
GN OrderedLocusNames=Arth_0665 {ECO:0000313|EMBL:ABK02064.1};
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK02064.1, ECO:0000313|Proteomes:UP000000754};
RN [1] {ECO:0000313|Proteomes:UP000000754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK02064.1; -; Genomic_DNA.
DR RefSeq; WP_011690532.1; NC_008541.1.
DR AlphaFoldDB; A0JSP4; -.
DR STRING; 290399.Arth_0665; -.
DR KEGG; art:Arth_0665; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_3_11; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000000754; 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; 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:UP000000754}.
FT DOMAIN 9..335
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 374..479
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 148..150
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 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 331..334
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 488 AA; 51003 MW; 80827E470B5C82F5 CRC64;
MTARVEREFD VIVIGAGAVG ENVADRVVQG GLTAVLIEAE LVGGECSYWA CMPSKALLRP
GTALHGAQTV PGAEEAVTRT LDASAVLKRR DYFTSNWQDD GQVKWVEDTG IELIRGRGRL
TGPRAVEVAG RDGVTYLLSA RHAVVLSTGS APTAPPVAGL AGLDYWTTRE ATSARSVPQS
LAVLGAGVAG TELAQAFARL GSAVTLVARG GLLSMYPKDA ASLVLAGLRA DGVDVRLNTG
TEKVSRNGDG SYTVALADGD SIRAERLLVA TGRHPALDGL GLEAVGLGAA DGRVPPLRTD
TTGLVEGMDY AGQGDGGDWL YAVGDAAGKV MLTHQGKYSA RATGDAIAAR AKGELQGSPE
PWTRFAQTAN DHAVPNVVFT DPELASVGRS VEQARKDGYN VSSVELPISV AGSSLHSEHY
EGWAQLVVDE DRKVLLGATF AGPDVAELLH AATIAVVGEV PLNRLWHAVP SYPTVSEVWL
RLLEEYGL
//
