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Database: UniProt
Entry: V5WF96_9SPIO
LinkDB: V5WF96_9SPIO
Original site: V5WF96_9SPIO 
ID   V5WF96_9SPIO            Unreviewed;       851 AA.
AC   V5WF96;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Putative CoA-disulfide reductase {ECO:0000313|EMBL:AHC14219.1};
DE            EC=1.8.1.14 {ECO:0000313|EMBL:AHC14219.1};
GN   ORFNames=L21SP2_0797 {ECO:0000313|EMBL:AHC14219.1};
OS   Salinispira pacifica.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Salinispira.
OX   NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC14219.1, ECO:0000313|Proteomes:UP000018680};
RN   [1] {ECO:0000313|EMBL:AHC14219.1, ECO:0000313|Proteomes:UP000018680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC14219.1,
RC   ECO:0000313|Proteomes:UP000018680};
RX   PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA   Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA   Klenk H.P., Fardeau M.L., Spring S.;
RT   "Complete genome sequence and description of Salinispira pacifica gen.
RT   nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT   mat.";
RL   Stand. Genomic Sci. 10:7-7(2015).
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; CP006939; AHC14219.1; -; Genomic_DNA.
DR   RefSeq; WP_024267150.1; NC_023035.1.
DR   AlphaFoldDB; V5WF96; -.
DR   STRING; 1307761.L21SP2_0797; -.
DR   KEGG; slr:L21SP2_0797; -.
DR   PATRIC; fig|1307761.3.peg.798; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   eggNOG; COG2210; Bacteria.
DR   HOGENOM; CLU_003291_3_0_12; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000018680; Chromosome.
DR   GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 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; 2.
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;
KW   Oxidoreductase {ECO:0000313|EMBL:AHC14219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018680}.
FT   DOMAIN          471..559
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   851 AA;  93010 MW;  21A74181E9D17B2D CRC64;
     MKVLIIGGVA GGATTAARLR RIQEDAEIVI FERGGYISYA NCGLPYYIGD VIQDRDRLFV
     QTPESFRENL NIDVRIRSEV TSIDPESKHI SVKNLETGEE YRESYDKLVL SPGAEPVKPP
     IPGIQSEGIF TLRSVPETDA IKTFVEEHNP RKAVIVGAGF IGLEMAENLH EKGLYVTIVE
     MAQQVMNVVD YEMAAQVHQH LKTKDVEFYL QDGVSNFSRQ KGADGQERII ITLQSGRTIE
     TDMVILSIGV RPESRLARDC GIETGETGGI KVNSHLETSE KDIYAVGDAI EFINPITKQP
     TITYLAGPAN KQGRICADNI VFGNQKEYRG SISTAIAKVF DITVASTGAS EKTLNKHRIP
     YHSIITHGSS HAGYYPNAMP VTIKTLFSKD EGRVLGAQII GYEGVDKRID MIAAVIRQEG
     SVQDLMELEH AYAPPYSSAK DPVNIAGFVA ENILTGRSRH IHWNEVAAGC NPDEMQLVDV
     RTPEEYQLGS IDGAVNIPVY EVRSRLGELD RNKTIIVFCG VGLRAYQAER ILRQNGFEDV
     FNLSGGYKTY EYAAQKQSNE DIFENDTIWK DDNIYQVDPD RKSAQPGSAP VSDSVMASAA
     GIKKMEIDAR GLQCPGPIMA LKKSVDSASE GQIIRETATD PGFYKDVKSW CNMTGNTLVS
     LEQDGANIVA EVRKAAARDS AAQNGTAGRS GSNAGNESTM VVFSDSLDQA LANFVIANGA
     ASAGKKVTLF FTFWGLSVIK KSRKTRGVKK DFMGKMFSLM LPRGSKKLGL SKMNMAGMGA
     GMMRRRMKKL NIDSLETMID QARENGVRMV ACQMSMDVMG VKAEELIDGV EIGGVASYLE
     AASSAGVNLF I
//
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