ID B0RGJ4_CLAMS Unreviewed; 487 AA.
AC B0RGJ4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CAQ02400.1};
GN OrderedLocusNames=CMS2313 {ECO:0000313|EMBL:CAQ02400.1};
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02400.1, ECO:0000313|Proteomes:UP000001318};
RN [1] {ECO:0000313|EMBL:CAQ02400.1, ECO:0000313|Proteomes:UP000001318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC {ECO:0000313|Proteomes:UP000001318};
RX PubMed=18192393; DOI=10.1128/JB.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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 ECO:0000256|RuleBase:RU003691}.
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DR EMBL; AM849034; CAQ02400.1; -; Genomic_DNA.
DR RefSeq; WP_012299600.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0RGJ4; -.
DR STRING; 31964.CMS2313; -.
DR KEGG; cms:CMS2313; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_11; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000001318; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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 InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 25..344
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 365..467
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 62..67
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 487 AA; 51042 MW; DA22DCF6CEEB8368 CRC64;
MPESTDHADP ATDAQPGAAT EPERYDVAVI GAGPAGTAAA LRAAELGASV VVLEAGRVGG
TCVNTGCVPT RVLAKTARLV REVRSAGENG IGVGDPTPHW PSIVARVHEQ VDRVRSLKDE
AERFRAAGVT LIHEGRARFV DDRTLVLDSG RRITAGSIIV CVGGHSRRLP VPGAELATVP
EDVLALPGIP RRLAVIGAGN TGAQLVTVFR SFGSEVTLLD VAPRVLTASD EAISEAVADA
FTAQGVRVHT GIDTVTGLTK TGDGSITLLW RDGDRPQSSS FDAVIMATGW PADVEDLGLE
HAGLEVERSA IPVDRYLRTR VPHILAVGDA NGKDMLVQAA QSEGEAAAEN AVLGVNRRIP
LQLLPAGGFT DPDYAGVGLT QAEARERDSA CVVARVPFAE VDRAVIDDRE AGFLLLIADR
RRELILGAHA VGENAVEVIQ SVTTAMAAGV DVATLAHVRF AYPTYSAIIG IAARRLLQED
DRAGELD
//
