ID W5Y667_9CORY Unreviewed; 545 AA.
AC W5Y667;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AHI21988.1};
GN ORFNames=B843_02985 {ECO:0000313|EMBL:AHI21988.1};
OS Corynebacterium vitaeruminis DSM 20294.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI21988.1, ECO:0000313|Proteomes:UP000019222};
RN [1] {ECO:0000313|EMBL:AHI21988.1, ECO:0000313|Proteomes:UP000019222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL Submitted (FEB-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; CP004353; AHI21988.1; -; Genomic_DNA.
DR RefSeq; WP_025252042.1; NZ_CP004353.1.
DR AlphaFoldDB; W5Y667; -.
DR STRING; 1224164.B843_02985; -.
DR KEGG; cvt:B843_02985; -.
DR PATRIC; fig|1224164.3.peg.591; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_11; -.
DR Proteomes; UP000019222; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
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 InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019222}.
FT DOMAIN 453..533
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 545 AA; 57738 MW; 68C698F28BA59D51 CRC64;
MATTVIVGGV AGGMSTAARL RRNDENREII VFEASGYVSF ANCGLPYHVG GVIPERSSLL
LQTPESLGAR FRIDVRTRHL VTEIDTVNNT VTVENLESGE TFTQAYDELV LSPGARPFVP
PIPGIERALT LRTVEDVDRI IAALDDSVKN VALIGGGFIG LELAENLIHR GLGVTVIERG
PQILAPFDEE MAAIVAGHLE KNKVVIHTNA DTTEIGEDSL TLADGTVIPA DVVIAAIGVR
PDTRLAEAAG LEIGPRGGIK VDEQQRTSVP NVFALGDAAE KTDINSGAAA LIPLAQTANR
HGRLVADIIT GRDTKALPVL GTAIVGLFGL AASATGWNER NARRAGRNVR VIHIHPVNHA
GYYPGATQLN LKLVIDADTD AILGAQAVGF EGADKRIDVI ATAMRGGLTA SDLADLELAY
SPQYGSAKDP INLAGMVADN LAQGEKSVQW HELSDDMQLI DVRTVGEYER GHIPGAVNIP
VDDLRENLDK IDASRPVVVS CQVGLRGHVA TRILSGLGMD VANLDGGYLT YTHGQAARKF
AHADQ
//
