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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//