ID A0A143YTS0_9LACT Unreviewed; 835 AA.
AC A0A143YTS0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pyridine nucleotide disulphide reductase class-i signature {ECO:0000313|EMBL:CZQ95645.1};
GN ORFNames=TR210_1323 {ECO:0000313|EMBL:CZQ95645.1};
OS Trichococcus ilyis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ95645.1, ECO:0000313|Proteomes:UP000076878};
RN [1] {ECO:0000313|EMBL:CZQ95645.1, ECO:0000313|Proteomes:UP000076878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ95645.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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}.
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DR EMBL; FJNB01000008; CZQ95645.1; -; Genomic_DNA.
DR RefSeq; WP_068622737.1; NZ_FNYT01000007.1.
DR AlphaFoldDB; A0A143YTS0; -.
DR STRING; 640938.TR210_1323; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000076878; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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 464..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 835 AA; 89836 MW; 8DB043CDDDD6D3FE CRC64;
MKRKIVIIGG VAGGATAAAR LRRLNEEDEI VIFEKGEYIS FANCGLPYHI GGTIQERDNL
LLETVGGMAK KFNIGIKNFS EVVKINRAEK TITVKHVLTG ATTEESYDKL IISTGARPIK
PAIAGIEEAE NVFTLRNIPD MDKIKAYINE HQVKRATVIG GGFIGLEMME NLWELGIQVS
LVEMSDQVMA PIDFEMAQSV HAHIDMHNVN LILNDGVKAF EDKGSKVRLN SGKVLNTDMT
ILSIGVTPEN ELATAAGLKT GVRGAIVVND QLQTSDPDIF AVGDVIEVTD FVNGKPTVVP
LAWPANRQGR LVADHLNGMD VRYKGTMGTS VAKVFELTVA AAGNNEKTLN GSGTDYKVVH
IHPNSHAGYY PGASPLDIKL LFGLDGKILG VQAVGMEGVE KRVDVIATAM KLGATVYDLP
DLELAYAPPY SSAKDPANIA GYVASNILEG KIDTFQWHEV DGLIAKGAFL LDVREEFELA
TGALGNAYTI PLAQIRERMS ELPKDKTIHV FCQVGHRGYN AARILMQNGF SVKNLDGGYK
TYKQAKTTLT YEEDVPEAAV HVEPVHAKPA AQPASNTIQV DACGLQCPGP ILKVKENIDK
MVDGQELIIE ASDFGFLADI AAWTKNTGNT LLSKEIDGKI VRAHVAKGKA GAVKSATPAG
FNEAALAAQA AQAPILQETK DGATMVVFSG DLDKALASFI IANGAAAYGK QVTMFFTFWG
LNVIKRPEKV SVAKRGMERM FDIMLPSHAG KLPISKMNMS GVGSKMIQAV MKQKNVDSLP
AMIAQAQKMG VKMVACTMSM DIMGIKEEEI IEGVDFGGVA AYIGDTMDAN LNLFI
//