ID A0A3T0Y1Q7_9MICC Unreviewed; 472 AA.
AC A0A3T0Y1Q7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:BBE21575.1};
GN ORFNames=MN0502_04580 {ECO:0000313|EMBL:BBE21575.1};
OS Arthrobacter sp. MN05-02.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1571833 {ECO:0000313|EMBL:BBE21575.1, ECO:0000313|Proteomes:UP000283134};
RN [1] {ECO:0000313|EMBL:BBE21575.1, ECO:0000313|Proteomes:UP000283134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN05-02 {ECO:0000313|EMBL:BBE21575.1,
RC ECO:0000313|Proteomes:UP000283134};
RA Ii KM., Kono N., Paulino-Lima IG., Tomita M., Rothschild LJ., Arakawa K.;
RT "Complete genome sequence of Arthrobacter sp. Strain MN05-02, a UV-
RT resistant bacteria from Sonoran Desert.";
RL Submitted (MAY-2018) 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}.
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DR EMBL; AP018697; BBE21575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0Y1Q7; -.
DR Proteomes; UP000283134; 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:UP000283134}.
FT DOMAIN 8..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 358..463
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 146..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 183..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 472 AA; 49386 MW; CAE51A02166FCB1C CRC64;
MSEARTIDVI VIGAGAVGEN VAGRVVQKGL SAVLVESDLV GGECSYWACM PSKALLRPGT
VLRAARGVPG AREAVTGTLD AGQVLDRRTS FTSNWDDSSQ EEWVASAGIS LERGWAKLSG
EREVAITHGD GSTTTYRARH AVVLATGSTP TIPPIDGLAD LDYWTTREAT SAKEVPASLA
VLGGGVAGVE LAQAFARLGA EVTVIARSGI LGNYPPEASG LVLDALRGEG LTVLTDTATS
SVHKEGGLFV LDIGEGRSVT AEKLLVSTGR HPHTSGIGLE SIGLDPEKLT RDDTGRVPDA
GGWLYAVGDV GGIVQLTHQG KYEARMTGDA IAARAQGTLG DHAADWSPYT STADRSAVPQ
VVFTDPEIAM VGRTLEQARK DGVNASETSL EIAVAGSSLH SDDYSGWAQI VVDEDRKVLV
GVTFAGPDVS EMLHSATIAV VGEVPLDRLW HAVPAYPTVS EVWLRLLEKY GM
//
