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Database: UniProt
Entry: F8J6T6_HYPSM
LinkDB: F8J6T6_HYPSM
Original site: F8J6T6_HYPSM 
ID   F8J6T6_HYPSM            Unreviewed;       447 AA.
AC   F8J6T6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:CCB63479.1};
GN   OrderedLocusNames=HYPMC_0245 {ECO:0000313|EMBL:CCB63479.1};
OS   Hyphomicrobium sp. (strain MC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB63479.1, 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|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000362-1};
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312}.
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DR   EMBL; FQ859181; CCB63479.1; -; Genomic_DNA.
DR   RefSeq; WP_013945892.1; NC_015717.1.
DR   AlphaFoldDB; F8J6T6; -.
DR   STRING; 717785.HYPMC_0245; -.
DR   KEGG; hmc:HYPMC_0245; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_024722_3_0_5; -.
DR   Proteomes; UP000000494; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR   PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000362; FNR; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000362-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000362-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000494}.
FT   DOMAIN          11..172
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         85
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         156..159
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         200..201
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         354
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         361..363
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         361
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ   SEQUENCE   447 AA;  48439 MW;  C6B0814B9D44B70F CRC64;
     MLQQNAASGL KIAIVGAGPA GFYAAEALAA ACPDCEITLI ERLPTPYGLI RSGVAPDHQT
     TKSIQNTFER IARLDNIRFV GNVEIGGDVS LDELRRFYDG VVLACGAPLD APLGIPGDNL
     PEVYGAAQFV GWYNGHPDFA ELNPRLDGGG VVVIGNGNVA IDIARVLSKS PDELANSDIA
     HHALQRLSVA DLSDVHIVGR RGPVEAKFTT AELQELGELQ TTVALADAAE LPETIGEEFS
     LRDRRLKNKN LECFKAFAQA DSMSRARRLR FQFNARPVQV LGDDRVEAVR FERTRVVGEA
     VEGTGEIFEI PCSLVVYAIG YRPSPMLGVN LRGTDNRLQS DAGRVAPGLY VVGWLKRGPS
     GKIGTNRIDG EEIAKKIIAE VDASGRTGFS GLEKLFQERS LRWTDFDDWK AIEAAEVAAA
     LMGAPRRKFV RVDHMLEVCR KIPATPA
//
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