ID Q24QK3_DESHY Unreviewed; 521 AA.
AC Q24QK3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN OrderedLocusNames=DSY3900 {ECO:0000313|EMBL:BAE85689.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE85689.1, ECO:0000313|Proteomes:UP000001946};
RN [1] {ECO:0000313|EMBL:BAE85689.1, ECO:0000313|Proteomes:UP000001946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51 {ECO:0000313|EMBL:BAE85689.1,
RC ECO:0000313|Proteomes:UP000001946};
RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AP008230; BAE85689.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24QK3; -.
DR STRING; 138119.DSY3900; -.
DR KEGG; dsy:DSY3900; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR Proteomes; UP000001946; Chromosome.
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:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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; PR00469; PNDRDTASEII.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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:UP000001946}.
FT DOMAIN 403..490
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 521 AA; 57092 MW; 229EF3F2F18373C7 CRC64;
MVQTPEDMQA RFNIDVRIRS EVIRLDAANK KVLVRSQSRG TYEESYDALI LSPGAKALRP
NIPGIDSERI LTLRNIPDTD AIKGLVDQKG VQSAIIIGGG FVGVEMAENL REQGLNVTLV
EAAPHILAPF DTDMVVLAEK KLVAHGIRLI LNDGVKSFQD LENQVEVTLA SNRKLQGDLI
ILAIGVIPDT GFLKESGLEL GPKGHLIVNE HMATNLPHVY AAGDAVEVLD YITKTKTAIP
LAGPANKQGR IAADNIAGLN STYKGTQGTS IIKIFELTAA STGANERTLQ RANLPYHVIH
IHPVSHASYY PNAYPMTLKL IFGADGRIFG AQGIGRDGVD KRIDVISTVI RLGGTVEDLT
ELELAYAPPF SSAKDPVNMA GYVAQNVLTG QAHMLVWDDL NKIDEEYTFV DVRTKIEFAK
GHVEGAINIP VDDLRQRIQE LDPGKLIVVY CEVGLRGYFA ERILTQKGYR VLNLTGGYTT
YSVQGFDPNQ ALDDYKKDFN PYPCCADEDI IDPDTQRIKH Q
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