ID A0A239H1U7_9FIRM Unreviewed; 825 AA.
AC A0A239H1U7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:SNS75151.1};
GN ORFNames=SAMN05446037_101969 {ECO:0000313|EMBL:SNS75151.1};
OS Anaerovirgula multivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Anaerovirgula.
OX NCBI_TaxID=312168 {ECO:0000313|EMBL:SNS75151.1, ECO:0000313|Proteomes:UP000198304};
RN [1] {ECO:0000313|EMBL:SNS75151.1, ECO:0000313|Proteomes:UP000198304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCA {ECO:0000313|EMBL:SNS75151.1,
RC ECO:0000313|Proteomes:UP000198304};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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 sulfur carrier protein TusA family.
CC {ECO:0000256|ARBA:ARBA00008984}.
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DR EMBL; FZOJ01000019; SNS75151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239H1U7; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000198304; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01524; RHOD_Pyr_redox; 1.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000198304}.
FT DOMAIN 465..552
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 825 AA; 89832 MW; 9EE01DA82D243B0F CRC64;
MAKKILIVGG VAGGATTAAR LRRLDEKAEI VLFERGEYIS FANCGLPYYI GGIIEERDAL
LVQTPEDMSR KFNIDIRVFN EVTKINREDK SVTVKNLKTE ELYQESYDYI VLSPGANPIF
PPIPGINEAD NLFTLRSIPD TDRIKDYVDN RKPKAAIVIG GGFIGIEMAE NLHYRGIEVT
LVEMANQIMA PIDYEMAAIL HNHLRDKGVQ LILEDGVKAF EDSGKKVLLQ SGKAVSIDLI
ILAIGVKPEN QLAKEAGLAL GEKGGILTNP YLETSDPAIY AIGDAIEIND YINGNPAMIP
LAGPANKQGR IAANNIIGKR ETYSGTLGTA VAKIFDMTVA STGNNERTLK QLGVNYQAIH
LHPGSHAGYY PGAFPISMKL LFESNSGKIL GAQAVGHKGV EKRIDVIATA IKGNLTAVDL
KELELSYAPP FSSAKDPVNM LGFVAANILE GLTDTFQWYE IKDILQADAL LIDVRDEIER
DLGYIDGSIN IPLGELRNRL PEIPKNKTIY VYCQVGIRGY IAARILMQEG YKVKNLDGGY
KTYQSIYAAN SGGNCLVEVD DSGVAKIHCN PNEDIKADLH INACGLQCPG PIIQVYKALE
EMQSGEVLEV KATDPGFMKD IASWCSKTGN TLIKSQMDGK TCKALIQKGS TLGAKHVVSS
SQESIINANK DAATMVVFSG DLDKALASFI IASGAASMGK KVTLFFTFWG LNILRKDSSP
KVRKDFLEKM FGWMMPKGPK KLPISKMNMG GMGPKMIQHV MKRKNVDSLE TLIKNAMDMD
VNIVACAMSM DIMGIKAEEL IDGVEIGGVA TYLGETQDAN LNLFI
//
