ID R5XCL4_9FIRM Unreviewed; 565 AA.
AC R5XCL4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=BN568_02431 {ECO:0000313|EMBL:CDA06171.1};
OS Blautia sp. CAG:257.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1262756 {ECO:0000313|EMBL:CDA06171.1, ECO:0000313|Proteomes:UP000018056};
RN [1] {ECO:0000313|EMBL:CDA06171.1, ECO:0000313|Proteomes:UP000018056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:257 {ECO:0000313|Proteomes:UP000018056};
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:CDA06171.1}.
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DR EMBL; CBBB010000232; CDA06171.1; -; Genomic_DNA.
DR AlphaFoldDB; R5XCL4; -.
DR STRING; 1262756.BN568_02431; -.
DR Proteomes; UP000018056; 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; 3.50.50.60; 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:UP000018056}.
FT DOMAIN 465..545
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 565 AA; 61886 MW; 45658534D94F32A6 CRC64;
MKVVIIGGVA GGATAAARIR RLDEKAEIIV FEKSGYVSYA NCGLPYYIGG VIQNKEELTL
QTPESFWKRF QITMKVRHEV TGIFPERKTV AVKNLDTGES FEEVYDKLLI STGAKPVWPK
LPGTDLDNLF TLRTVEDTLK IREFVEKKQP KSAVLAGGGY IGLELAENLR ELGLDVTIVQ
RPKQLMNPLD GDMAAFVHAK MRSRGVKLML GHTVEGFEKG EKGTRVLLKD EQPLEADMVI
LAIGVAPDSH LAKEAGLELG IKGSIVVNDR METSAPDIFA AGDAVEVKHY ITGEKALISL
AGPANKQGRI AADNICGGDS RYPGSLGSSV IKVFDMTAAS AGINERTAKQ TGIDYDKVYL
SPASHASYYP GGKVMTMKVI FEKKTYKLLG AQIIGYDGVD KRIDVLATAM YAGITALQLK
ELDLSYAPPY SSAKDPVNMA GFMIENIAEG RLKQFFTEEV ENLPRDGSVI LLDARTPGEY
ARGHIEGFIN IPVDELRDRL SELDKKKKVY IICQSGLRSY IAYRILAQEG FDCRNFSGGF
RLYETVTGDR MAAGEALPCG MEINR
//
