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Database: UniProt
Entry: A0A2I7N2W5_9NEIS
LinkDB: A0A2I7N2W5_9NEIS
Original site: A0A2I7N2W5_9NEIS 
ID   A0A2I7N2W5_9NEIS        Unreviewed;       565 AA.
AC   A0A2I7N2W5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AUR50793.1};
GN   ORFNames=CUN60_00270 {ECO:0000313|EMBL:AUR50793.1};
OS   Aquella oligotrophica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Aquella.
OX   NCBI_TaxID=2067065 {ECO:0000313|EMBL:AUR50793.1, ECO:0000313|Proteomes:UP000236655};
RN   [1] {ECO:0000313|Proteomes:UP000236655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100970 {ECO:0000313|Proteomes:UP000236655};
RA   Chan K.G., Lee L.S.;
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP024847; AUR50793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I7N2W5; -.
DR   KEGG; nba:CUN60_00270; -.
DR   OrthoDB; 9769238at2; -.
DR   Proteomes; UP000236655; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00158; RHOD; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000236655}.
FT   DOMAIN          463..547
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   565 AA;  61782 MW;  2DA96F57D2250E74 CRC64;
     MARKILIIGG VAGGASAAAR LRRLSEDDQI IMFERGEHVS FSNCSLPYFL GGHISSSDKL
     VLMSPEKFLK QYNIIARTKN EVTAINRQDK IITIKDLNSG ELYTESYDKL ILSPGAKPIV
     PPIPGIEKIN LFTVRNVTDI NNLHNAIQDK SKKIAVIGGG FIGVEVAENL KEAGYDVSLI
     EAMPQILRTF DYDMVQILHK EILDHGINLL VNDKVAGFDT NTVLLGSGKK VAADIVIMAI
     GVSPETHLAK EAGLEIGKTG AIATSPMCQT NDPDIYAIGD AIEVDGKLFD DKWKLALAWP
     AQIQARGVAD HINGQDFLNP GYIGSSCIKV FNLNAASTGL TEGFIQATKM DIDYETVIIT
     PNDKVSLMPD NSTMFFKLIF DKNTRKVLGA QAIGKGNADK RIDVIATAIK FGATIDDLTE
     IELCYAPPYS SAKDVVNMAG YVAANIADKS FSQVSPNEVR NLVESGAYIV DVRETPELEK
     GKIIGSYHIP LSELRSRYQE IPKDRPVYLH CRSGQRSYNG ALALQNLGYS NVVNVAGGFL
     GLSYYEYFND KTLNRNPILT AYNFN
//
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