ID A0A1Y3TXQ8_9FIRM Unreviewed; 561 AA.
AC A0A1Y3TXQ8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OUN39617.1};
GN ORFNames=B5G28_04665 {ECO:0000313|EMBL:OUN39617.1};
OS Faecalibacterium sp. An77.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=1965655 {ECO:0000313|EMBL:OUN39617.1, ECO:0000313|Proteomes:UP000196357};
RN [1] {ECO:0000313|Proteomes:UP000196357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An77 {ECO:0000313|Proteomes:UP000196357};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUN39617.1}.
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DR EMBL; NFHK01000008; OUN39617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3TXQ8; -.
DR Proteomes; UP000196357; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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;
FT DOMAIN 460..541
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 561 AA; 60777 MW; 4B7E8660D8D16E41 CRC64;
MKYVLVGGNT GGAGAAARLR RLDEQAEILL LEKGAHVSYS NCSLPYRLSE TVDQTEKLVL
NTPESLHGAY NIETRANSQV LSIDRAGKKV RVKDLATGRA YDEAYDTLIL SPGANAVVPR
IQGIENANLF TVKTVEDVSR FYGFLKDKGV RKVSVIGGGF IGVEVAVNLR EAGYQVALVE
AMPQILKPYD YDMVQILQKA MIDHGVDLVV GDSVVAFQQS NVQLNSGRVI EGDAVVMAVG
VRPDTALAAE AGLEMNPRGA IKVDPNYRTS DPSIYAVGDA VEVFNPLTRK PAMVQLAGPA
QKQARQAADH IYGLPVRNTG FIGSSCIQVF EWNAASTGLT AAQCEQEGIP YEVAYVLPKD
RVGIMPGSTQ LHYKLIFEVP TGRVLGAQAI SKGDAVKRID VAATLIKLGG TVDDLRDLEL
CYAPPFSAPK DAANYAGLVA GNLLAHRFRQ VHVDQVRDLV ESGAYILDVR PAAVYHQGHL
KTSVNIPLAQ LRSRLDEIPT DRPVYVHCQI GQSSYNAVLA LQGHGFTNVY NVSGGFLGIC
AYEYFNDVTQ KREPIVTNYL F
//
