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Database: UniProt
Entry: R5D328_9BACT
LinkDB: R5D328_9BACT
Original site: R5D328_9BACT 
ID   R5D328_9BACT            Unreviewed;       818 AA.
AC   R5D328;
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=BN567_01491 {ECO:0000313|EMBL:CCX70281.1};
OS   Prevotella sp. CAG:255.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262923 {ECO:0000313|EMBL:CCX70281.1, ECO:0000313|Proteomes:UP000017913};
RN   [1] {ECO:0000313|EMBL:CCX70281.1, ECO:0000313|Proteomes:UP000017913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:255 {ECO:0000313|Proteomes:UP000017913};
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   -!- 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:CCX70281.1}.
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DR   EMBL; CAWV010000165; CCX70281.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5D328; -.
DR   Proteomes; UP000017913; 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: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          463..546
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   818 AA;  88295 MW;  3985EF6D186087C5 CRC64;
     MRHIIIGGVA GGATAAARIR RADEKAEIIL VEKGPHISYA NCGLPYYIGG TIADKNKLFV
     QTPESFGRRF NVDVRVNTEA ISIDTKAKTV TLRRPDGSVI DEHYDRLLLS PGSSPVRPPF
     PGIDTEGIFT LRNVEDTFRI KDYLTQHSVK SAVVVGGGFI GLEMAENLSH AGARVSIVEM
     APQVMAPVDF SIASHVHREL LSQGVSLHLN TAVERFEKDN GRIRVFFKSG KSIVTDLVLL
     SIGVSPNTSL AKSAGIELGA RGIKVDKYLE TSAKDVYAVG DAIEYPHPEY SEPWLNYLAG
     PANRQGRIVA DNMVFGNTTE YEGAIGTSIA KVFDVVVGST GLPAKRLKQL GIKYQSSTTT
     SMSHAEYYPG AFFITTKLTF NPEDGTLYGA QCVGHEGVDK RIDQLAIIIK HKGTIYDLIR
     LEQAYAPPFS SAKDPIAIAG YTAANIISGK MPVIYWRDID GLDRSKVQII DTRTPSEFSL
     GTISGAVNIP VDDIRERMGE IDKSKPVVTF CAVGLRGYIA ARILIANGYD VRNLSGGYKT
     YQLATQDLQC ADGNDDSDDS SCSCSCTPGS QCSDSRATLT VDACGLQCPG PILKLKQATD
     DMQPGETIEV KATDPGFPSD AKAWCKSTGN AFLSVSCTDG CHTVLIRKQQ SDDKPAAACA
     PAGKNKTLIC FSDNLDRAIA TFILANGAAA TGSKVSIFFT FWGLNVIKKK HGPAVKKTLT
     EKMFAHMLPK SSDSLALSKM NMMGMGSKMI RGIMKKKNID SLESLIRQAM DNGVEFIACQ
     MTMDMMGIKK EELLDGVTVG GVASYMQKAE EAGVNLFI
//
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