ID C4L109_EXISA Unreviewed; 821 AA.
AC C4L109;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACQ70972.1};
GN OrderedLocusNames=EAT1b_2049 {ECO:0000313|EMBL:ACQ70972.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ70972.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ70972.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC {ECO:0000256|ARBA:ARBA00008984}.
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DR EMBL; CP001615; ACQ70972.1; -; Genomic_DNA.
DR RefSeq; WP_015880531.1; NC_012673.1.
DR AlphaFoldDB; C4L109; -.
DR STRING; 360911.EAT1b_2049; -.
DR KEGG; eat:EAT1b_2049; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR eggNOG; COG2210; Bacteria.
DR HOGENOM; CLU_003291_3_1_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000000716; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01524; RHOD_Pyr_redox; 1.
DR Gene3D; 3.40.1260.10; DsrEFH-like; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.30.110.40; TusA-like domain; 1.
DR InterPro; IPR032836; DsrE2-like.
DR InterPro; IPR027396; DsrEFH-like.
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; IPR001455; TusA-like.
DR InterPro; IPR036868; TusA-like_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 1.
DR Pfam; PF13686; DrsE_2; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF01206; TusA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF75169; DsrEFH-like; 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 SUPFAM; SSF64307; SirA-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS01148; UPF0033; 1.
PE 3: Inferred from homology;
FT DOMAIN 465..552
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 821 AA; 88824 MW; 74032C5A7D064A0F CRC64;
MSKKIVIVGG VAGGASAAAR LRRLNEENHI VMFDRGEYIS FANCGLPYYI GDVIQDRQKL
LVQTVEGMNK RFQLDIRNLT EVVKINRDEK TVTVKHVQTG ETYDESYDVL ILSPGAKPIR
PNIPGIDEAE DIFTLRNIPD TDKIRGYVDD KAPKHATVIG GGFIGIEMAE NLRERGVEVT
LVEMADQVMT PLDREMVAPI HEHMRLHGVE LQLSDGVSSF SEKGKKVHLT SGRVIDTDMV
IMSIGVTPES TIAREAGLET GTRGAIRVNE KMMTSDPSIY AIGDAVEVLD YVFHEPTVVP
LAWPANRQGR LVADIINGRD VKYNGTMGTG IAKVFDMTVA STGWNEKRLK AAGKTYEAVH
VHPGSHAGYY PGSTPVSLKL LFHPTTGEIY GAQGVGINGV DKRIDVIATA MKGGLTVLDL
PDLELSYAPP FSSAKDPVNM IGYVASNVVL GDNEVVHWDE IDELVENGAT LLDVRDESEH
ELGKIPGSIN VPLNSLRENL DNYDRNETIY VTCQVGLRGY LASRILRQNG FKVKNLSGGY
KTWSQINRDF EALEEANTSN ETAATVVEEE PTQMTNAPIG EAVVLDTCGL QCPGPILEVN
KKVAELGEGE TLRVLASDPG FFADIEAWAK KTGNKLVSKQ FVNGRVEAIL QKGQGPAVPQ
AGAPAGDGAS MVVFSGDLDR ALASLIIAQG AAAMGKDVTM FFTFWGLNVI RKPDAPEVKK
QGLEKMFGMM MPGHAGELPL SNMNFGGVGQ KMMKKVMSDK NVPSVEEMIK SAQEAGVKMV
ACTMSMDVMG IKEEELIDGV DLGGVAAYLG AAEGGNLNLF I
//
