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Database: UniProt
Entry: A0A0K8J655_9FIRM
LinkDB: A0A0K8J655_9FIRM
Original site: A0A0K8J655_9FIRM 
ID   A0A0K8J655_9FIRM        Unreviewed;       566 AA.
AC   A0A0K8J655;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN   ORFNames=SD1D_1272 {ECO:0000313|EMBL:CUH92818.1};
OS   Herbinix luporum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Herbinix.
OX   NCBI_TaxID=1679721 {ECO:0000313|EMBL:CUH92818.1, ECO:0000313|Proteomes:UP000196053};
RN   [1] {ECO:0000313|Proteomes:UP000196053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD1D {ECO:0000313|Proteomes:UP000196053};
RA   Wibberg D.;
RL   Submitted (SEP-2015) 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; LN879430; CUH92818.1; -; Genomic_DNA.
DR   RefSeq; WP_058258157.1; NZ_LN879430.1.
DR   AlphaFoldDB; A0A0K8J655; -.
DR   KEGG; hsd:SD1D_1272; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000196053; Chromosome i.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00158; RHOD; 1.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000196053}.
FT   DOMAIN          469..545
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   566 AA;  62674 MW;  5EB69791036DF671 CRC64;
     MGRKILIVGG VAGGASAAAR LRRNNEDDQI IMFERGPHIS FSNCSLPYHL SGIVKEADNL
     VLMKPELFLK QYNIEARINS EVIAINRDDK TVTVRKTDTD EEYTESYDKL ILSPGARPIA
     PKLPGMEKVN IFTVRNVVDI DNLNKFIKNM KTKDVAVIGG GFIGVEVAEN LRLGGYNVTL
     IEASNQILRP YDYDMVQIFH KVMLDNKVNL ILGDKVEKFE EDKVILASGK TIRAGAVVMA
     VGVSPEINLA KESGLKIGKT GAIKVDKNYL TDDTDIYAIG DAIEVYNALT HTMTKLSLAG
     PALKQARAVA DHINNKTTVN KGYIGSTAIK VFDYNGATTG LNESLIKDLN MNINYDIVRL
     ILSDKVGLMP DAAPMHFKLL FEVPTGRILG AQAIGKGDVT KRIDIIATAI KFAGTVYDLK
     DLELSYAPPF STAKDIVNYA GYIGSNLLNG DYKQVNVDKV RELVENNNII IDVREVHEFE
     KGHIKGAINI PLSQLRNRID EIPKDKPIYL HCRTGQRSYN AVLALQHMGY DKVYNITGSF
     LGVCLYEYYN DIVSGRESIV TEYNFK
//
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