ID F8JH38_HYPSM Unreviewed; 486 AA.
AC F8JH38;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:CCB68082.1};
GN OrderedLocusNames=HYPMC_4874 {ECO:0000313|EMBL:CCB68082.1};
OS Hyphomicrobium sp. (strain MC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB68082.1, ECO:0000313|Proteomes:UP000000494};
RN [1] {ECO:0000313|Proteomes:UP000000494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA Genoscope.;
RT "The complete genome of Hyphomicrobium sp. MC1.";
RL Submitted (MAY-2011) 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; FQ859181; CCB68082.1; -; Genomic_DNA.
DR RefSeq; WP_013950472.1; NC_015717.1.
DR AlphaFoldDB; F8JH38; -.
DR STRING; 717785.HYPMC_4874; -.
DR KEGG; hmc:HYPMC_4874; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_5; -.
DR Proteomes; UP000000494; 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: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.
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:UP000000494}.
FT DOMAIN 18..334
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 354..461
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 151..153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 188..195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 486 AA; 51639 MW; 1BEA29AE0E7E92CB CRC64;
MPKDTVEPHP ETHTVNADFC VIGAGAGGVA VATTAAAFGQ RVVLIEKHKM GGDGLNYGSI
PANALLAAAK RAQDMRTASP FGIRGVEPLI DHAAVNRYVT DVIARIAPNT TVERFGGMGI
QVISAAAKFL NPTTVAAGEY RISARRFVIA TGSSPTIPPI PGLADVPYFT NETIFDNNAP
IPHLIVVGAG TTGIELAQAH RRLGSRVTVI DAADALGDED SELAVVLLTQ LAAEGIVFRE
GVRITRVSGT VGNITVEIAG NGESETERIE GSAILVAAGR KANVADLGLD NARIKVAGNA
IKVNESLMTT NKRVYAIGDA AGGLRFAHVA AEQADVVLRR SLFRQSAKTV GRSTPRVVFT
EPQFACVGLS EAEASTKYGR VNVLRWPYHE NDRAQIERKT EGHIKVITTK RGQILGAAIV
GAEAGEIIQM WSLAISQRLN IKAMTQWISP YPTFSEINKK AAIRYFATVP SNPFLRKVIA
LLAKLG
//
