ID R6FC81_9FIRM Unreviewed; 565 AA.
AC R6FC81;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=BN538_01961 {ECO:0000313|EMBL:CDA99692.1};
OS Lachnospiraceae bacterium CAG:215.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1262985 {ECO:0000313|EMBL:CDA99692.1, ECO:0000313|Proteomes:UP000018007};
RN [1] {ECO:0000313|EMBL:CDA99692.1, ECO:0000313|Proteomes:UP000018007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:215 {ECO:0000313|Proteomes:UP000018007};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:CDA99692.1}.
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DR EMBL; CBCV010000272; CDA99692.1; -; Genomic_DNA.
DR AlphaFoldDB; R6FC81; -.
DR Proteomes; UP000018007; Unassembled WGS sequence.
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: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;
FT DOMAIN 465..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 565 AA; 62360 MW; A3FF4B2A806D65E5 CRC64;
MKVVIVGGVA GGATAAARIR RLDEEAEIVV FERTGYISYA NCGLPYYIGG TIEDAEELTL
QTPESFWKRF RVQMKVHHEV TAIHPERKTV SVKNLENAEE FEESYDKLLL SPGAKPVLPK
ISGIGNEKLF TLRTVEDTFK IKKYIEEKKP KSVILAGGGF ISLELAENLR ESGMVVTIVQ
RPKQLMNPFD PDMASFIHNE MRQHGVKLYL GHTVEKVEEN EQSINVLLKD GTALQADMVV
MALGATPDTK LAKAAGLELG IKESILVDER METSVADIYA VGDAVQVKHS VTGADVLISL
AGPANRQGRI AADNICGGKS IYHGSQGSSV IKIFRLTGAT TGINERTAKK AGINVDKVIL
SPMSHAGYYP GGKMMTMKVI FEKESYRLLG AQIIGYDGVD KRIDVLATAI HMKMKATDLK
GLDLAYAPPY SSAKDPVNMA GYMIDNISKG ILKQFHIEDI EKVVQKENIV RLDVRTPEEY
AHGHIDGFRN IPVDELRERL NEIDTDKPIY VICQSGLRSY IASRILSGKG LECYNFAGGF
RFYDAVIREQ SLIETSLPCG MDQRK
//