ID A0A1I6V4W5_9BACI Unreviewed; 556 AA.
AC A0A1I6V4W5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase {ECO:0000313|EMBL:SFT08647.1};
GN ORFNames=SAMN05421668_14411 {ECO:0000313|EMBL:SFT08647.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFT08647.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFT08647.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFT08647.1,
RC ECO:0000313|Proteomes:UP000199139};
RA de Groot N.N.;
RL Submitted (OCT-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 class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; FPAI01000044; SFT08647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6V4W5; -.
DR STRING; 306541.SAMN05421668_14411; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000199139; 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; 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 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857}.
FT DOMAIN 466..552
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 556 AA; 61213 MW; 6C3C0EE8096DD094 CRC64;
MKIVVIGSVA AGTSVAAKAR RNTEEAEIFV YDQGKDISYS VCGIPYHIGE EVEELSALTP
RNAAWFKKRY NVSVFTEHKV TRIDPANKQL EVTDLVSGEK KQDNYDGLVF ATGASPFTPP
PFNQKEYDNV FQVRTIQDAR DIGAYSSKQP KKALIIGAGF IGLEMTEQLI HKGLEVTIVQ
LEDQVMPPMD ADMTFHIEEH MRAKGVNLIL GDTVKIIEGK TSVERVITTN GITIEPDIVI
LSAGVRPNTE LAKEMGVKLG DSRAIAVNNK MQTNLPDVYA VGDVAESFSV ITGKPIYRPL
GSTANKMGRI AGDVITGGDL EHRGVLGTGI FRIFELHVGQ TGLTEKEAKK EGYDVEVLYN
IKPDHAEYLG GKELTIKALA DKKTGRILGA QVIGKAGVDK RIDVIATAIT FKAKAEDLFH
LDLAYAPPFA TTKDPILYTG MVLDNALKRN PLITPADLIN RLDWNEKVQI IDTRSKKDFE
KSHVKGAIHI PLAELRERNV ELDKNVTTVT YCNKGVTGNA AQNVLINYGF KKVYNLSGGN
KNFQNHIKMI EKNYSK
//
