ID A0A101FLN6_9BACT Unreviewed; 565 AA.
AC A0A101FLN6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KUK39313.1};
GN ORFNames=XD68_1130 {ECO:0000313|EMBL:KUK39313.1};
OS Synergistales bacterium 54_24.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK39313.1, ECO:0000313|Proteomes:UP000054050};
RN [1] {ECO:0000313|Proteomes:UP000054050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:KUK39313.1}.
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DR EMBL; LGFQ01000049; KUK39313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FLN6; -.
DR STRING; 1635272.XD68_1130; -.
DR Proteomes; UP000054050; 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; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 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; 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 3: Inferred from homology;
FT DOMAIN 476..564
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 565 AA; 61216 MW; 445E251B08507A8B CRC64;
MGKRVVIIGG VACGGKVASR LRRLEPEAEI LMLEKGEHIS YAACGLPFYV GGTVSDYKDL
INTSIGVVRD ASYFKAVKDV DVLTSHMATS INRELKNVEA TDLRTGERKL FSYDYLVIAT
GASPIIPPIP GNQLESVFRL WTLDDAMKLR SAIDSGRVKR AAIVGGGLVG LEAAEAMAMR
GIETTVVDLL GWPLPAMLDE EFGAKLKGLM ASKGVMFYGS EKVTEIVGNG CEVAALRTDK
KEIPVEAVLL AVGVKPNARL ATEVGLKVGQ KGGILVDEHM RTSDPYIYAG GDVIETRHLI
TNEPTYQPMG SSANRQGRVI ADNIAGIPST FKGVAGTAIM RFFDFTVART GLSEELAESK
GFDPVSVMIV DPDKPHFMPG SAWISAKVVA DRRTRRLLGA QFFGPGQVDK RLDAFVAAMT
GKLTVDDLAD ADFGYAPPYS TALDPLTHAA NAVRNKMDGM LISYSPSEFK NKLDSDGEDV
LLLDVRTPAE VKEQGRLPYE NQVNIPLGQL RDRANELPTD KEIVTFCKVS VRGWDAYNIL
KGKGFERVAL LEGGIVGWPY EIDRP
//
