ID S4XF41_9CORY Unreviewed; 563 AA.
AC S4XF41;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AGP31757.1};
GN ORFNames=A606_10590 {ECO:0000313|EMBL:AGP31757.1};
OS Corynebacterium terpenotabidum Y-11.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1200352 {ECO:0000313|EMBL:AGP31757.1, ECO:0000313|Proteomes:UP000014809};
RN [1] {ECO:0000313|EMBL:AGP31757.1, ECO:0000313|Proteomes:UP000014809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y-11 {ECO:0000313|EMBL:AGP31757.1,
RC ECO:0000313|Proteomes:UP000014809};
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Szczepanowski R., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium terpenotabidum Y-11 (=DSM
RT 44721).";
RL Submitted (JUN-2012) 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; CP003696; AGP31757.1; -; Genomic_DNA.
DR RefSeq; WP_020442106.1; NC_021663.1.
DR AlphaFoldDB; S4XF41; -.
DR STRING; 1200352.A606_10590; -.
DR KEGG; cter:A606_10590; -.
DR PATRIC; fig|1200352.3.peg.2161; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_11; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000014809; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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: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; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000014809}.
FT DOMAIN 473..560
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 563 AA; 59237 MW; D6AE6550A93DEBDE CRC64;
MTDQTHSPRH TVIVGGVAGG MSAATRLRRR DEHARITVLE KSGHVSFANC GLPYYIGGVI
EGRENLLLQT PASLHERFNL DVHVNTEVTA IDRAAHELTV TDLTTGQQRT IGYDTLVLSP
GAAPFIPPVP GIERALALRT VEDTDRIHDA VAGLAPGAPV VVAGGGFIGI EVAENLAHRG
LDVTVVEFGP QIMGPLDPEI AGIVERRLVD NGVHVLTGTG VATVEDVTVT LTDGTSRPAD
LVIAAAGVRP ATGFAAEAGL ETLAGGALVV DATWRTSDPD IFAVGDAVAT PDALTGEPVV
VPLAQTANRD GRLVADIISG DDVSLPRTWG TSVMGVFGLQ VASTGWTEKR LVAAGVPHQV
IATHPASHAG YYPGAAGLSM KLLVGTGDFR GEDLRDRILG AQVVGEEGAD KRLDILATAM
QSGRRASELL DLELAYAPQF SSAKDPVNML GYIADNLRTG RTELVTWNQI DELAQDAVLL
DVRTPGEFAA GSLPGAVNIP LDELRGRLGE VRELCGEAPV VVFCQVGQRG HVAESVLRGE
GLTRVYNLTG GYRTWSDGQR TLR
//
