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Database: UniProt
Entry: U2N715_9CLOT
LinkDB: U2N715_9CLOT
Original site: U2N715_9CLOT 
ID   U2N715_9CLOT            Unreviewed;       816 AA.
AC   U2N715;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase family protein {ECO:0000313|EMBL:ERK31312.1};
GN   ORFNames=CINTURNW_1759 {ECO:0000313|EMBL:ERK31312.1};
OS   Clostridium intestinale URNW.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK31312.1, ECO:0000313|Proteomes:UP000016721};
RN   [1] {ECO:0000313|EMBL:ERK31312.1, ECO:0000313|Proteomes:UP000016721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URNW {ECO:0000313|EMBL:ERK31312.1,
RC   ECO:0000313|Proteomes:UP000016721};
RX   PubMed=24136853;
RA   Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT   Clostridium intestinale Strain URNW.";
RL   Genome Announc. 1:e00871-13(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERK31312.1}.
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DR   EMBL; APJA01000012; ERK31312.1; -; Genomic_DNA.
DR   RefSeq; WP_021801762.1; NZ_KI273145.1.
DR   AlphaFoldDB; U2N715; -.
DR   STRING; 1294142.CINTURNW_1759; -.
DR   PATRIC; fig|1294142.3.peg.1791; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   eggNOG; COG2210; Bacteria.
DR   HOGENOM; CLU_003291_3_1_9; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000016721; Unassembled WGS sequence.
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:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016721}.
FT   DOMAIN          463..550
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   816 AA;  89157 MW;  BF0024DE1B0FC420 CRC64;
     MKKVIIVGGV AGGASAATRL RRLDENLEII MFERGEYVSF ANCGLPYYIG GEIKEREKLL
     VQTPKSINDR FNVDVRVNSD VVSIDTDRKV VKVNSLEKGE YEESYDYLIL SPGAKPIKPP
     IKGIGSSKIY TLRNVPDTDK IKRVVDEKGI KSAVIIGGGF IGIEMAENLK ERGLDVTLIE
     AAPHILAPFD SEMVTIAEKE LNDRDVSLIL NNGVDSFKDN NDLIEVHLKD GSFVESDIVI
     LAIGVAPDTS FIRNTNIELG ARGHIIVDEY MRTSASDVYA VGDAILVKDY VSGEDVAIPL
     AGPANRQGRI AADNIAGRKV AYKGTQGTSI LKIFDLVGAS TGNNERTLKR LGIDYKTAYI
     HPMSHASYYP GAKQISIKLI FNKEGKVLGA QAFGYEGVDK FIDVIASVIK LNGTVEDLVE
     LELAYAPPFL SAKSPQNMVG FVAENYLNGT TDIISVNELS VYNSENSTLL DIRETIEVES
     GSIEGSINIP LNSLRNRLNE LPKDKEIIVY CAVGLRGHTA SRILTQNGFK VKNLSGGYKT
     YIQSKYIAKK ISKQSNLNTD IKKEEVAVDI NSIELDACGL CCPGPLMQVK AKIDTLNTGD
     VLKVKASDPG FYEDIKSWCK NTGNELMSLD KSCGIIYAEI KKKSKSNVEN VDILESSVKL
     DNSQTMVVFS GDLDKAIASF IIANGAAAMG KKVTMFFTFW GLNILRKNEN IQVKKNIIEK
     AFGFMMPRGS EKLSLSKMNM GGIGAKMIRG IMQKKNVQSL EELMKAAMDN GVNIVACTMS
     MDIMGIKEEE LIDGVNFGGV GYYLGEASES NINLFI
//
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