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
//