ID M4U527_9GAMM Unreviewed; 566 AA.
AC M4U527;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase family protein {ECO:0000313|EMBL:AGH80721.1};
GN ORFNames=PCNPT3_03895 {ECO:0000313|EMBL:AGH80721.1};
OS Psychromonas sp. CNPT3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80721.1, ECO:0000313|Proteomes:UP000010320};
RN [1] {ECO:0000313|EMBL:AGH80721.1, ECO:0000313|Proteomes:UP000010320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80721.1,
RC ECO:0000313|Proteomes:UP000010320};
RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA Yayanos A.A., Bartlett D.H.;
RT "The complete genome sequence of the deep-sea bacterium Psychromonas
RT CNPT2.";
RL Submitted (MAR-2013) 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; CP004404; AGH80721.1; -; Genomic_DNA.
DR RefSeq; WP_015464602.1; NC_020802.1.
DR AlphaFoldDB; M4U527; -.
DR STRING; 314282.PCNPT3_03895; -.
DR KEGG; psy:PCNPT3_03895; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000010320; 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:UP000010320}.
FT DOMAIN 464..545
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 566 AA; 62218 MW; 730DA899C563E6C2 CRC64;
MNKKILIVGG VAGGASTAAR CRRHSEEDTI IMFEKGPHVS FSNCCLPYHL SGVVATAEEL
VLMSPKQFAD QYNIDARVAS EVVSIDRAAK TILVKNVETG EEYNEHYDKL ILSPGAKPIV
PPIPGIEKVN TFSIRNVVDI DRLNKFIKKG DTKNISVIGG GFIGVETAEN LKEAGYNVTL
IEAMPQIMKP FDYDMVQILH KELHDHGVNL IVNDKVERFS ENKIILSSGK EVDTDVVVMA
IGVRPETDLA KQAGLDLGKT GAMKVNQNYQ TNDADIYAVG DVIEVYSYLY NDYFQLPLAG
PAQKQARAVA DHINGMAIDN RGYIGSSVIK VFDYNAASTG LNEGMIKALG LNLCYNTVNI
IPNDKVGLMP FGAVAHFKLV YEVPTGRILG AQAIGKGNID KRIDVIATVI KFGGTIYDLK
DLELCYAPPF GTAKDIVNFA GYVATNLMNS DFKQVHGSNI RPLVESGACI VDVREESEFA
QSHIKGAINI PLSEIRQRTD ELPKDKPLYL HCRSGQRSYN AVLALQNMGF TDVYNVSGGF
MGLCFYEYFN DKTLKRTPIV TDYNFD
//
