ID F4LNI6_TREBD Unreviewed; 858 AA.
AC F4LNI6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:AEE15840.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:AEE15840.1};
GN OrderedLocusNames=Trebr_0393 {ECO:0000313|EMBL:AEE15840.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE15840.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002696; AEE15840.1; -; Genomic_DNA.
DR RefSeq; WP_013757559.1; NC_015500.1.
DR AlphaFoldDB; F4LNI6; -.
DR STRING; 906968.Trebr_0393; -.
DR KEGG; tbe:Trebr_0393; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR eggNOG; COG2210; Bacteria.
DR HOGENOM; CLU_003291_3_0_12; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000006546; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:AEE15840.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546}.
FT DOMAIN 472..560
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 673..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 92254 MW; 54C069F3B037C5A2 CRC64;
MADKTLIIGG VAGGATAAAR LRRRNESMQI IMFERGEYIS YANCGLPYYI GGVIHNRDAL
LLQTPQAMLK KFNVDVRTSN EVTAIRPAEK KVTVRNLKTG AVYDESYDNL IIATGSSPVK
PPIPGIESPG IFTLWTVPDT DRIRNFIEEK KPARAAVVGG GFIGLEMAEN LKSAGLSVSL
IEMQEQVMAP LDREMAEILH VHLERNGVEL ILGDGVKRFR PEAGGTVVEL ASGRTVVADM
VVLAIGVRPN SQLAKDAGLA LNAKGGIVVD EYLRTSEKDI YAVGDVIEVT DYVSGGKTMI
PLAGPANKQA RILADNLSGD RKTYGGTIGT AIAKVFELNA ASAGLNEKQL AAAGKKKDAD
YHTVLINQKS HAGYYPGATT LTLKLLFEKN GTILGAQVVG SDGVDKRIDT IATVMRLRGT
VHDLAELELA YAPPFSSAKD PVNMLGFVAE NVLDTLVTCI EWRDAEALLR SGSDDFTVLD
VMEDSERTVF AVPGSYHIPL GQLRERLSEL DPSKLIVPYC AVGVRSYNAA RILMQNGFKR
VAMISGGTSF YKATHRESDA VSEDAAYSAA VGALSETAAH SATVGAASDT EYSADRSIKI
LDCSGLQCPG PIMKVYEALC DMEDSQILQV SATDMGFTAD AAAWCRRTGN TFVRSERRGG
EYVVYIRKGG DCCDPHDRGT PRKQESAPSQ GAAQSPETAL SPAQGKTIIV FSGDLDRVLA
SFIIANGAAA MGRPVTMFFT FWGLNVLRKT RTGKIKKPFM DKMFASMMPK GSAKLKLSKL
NMAGMGTAMM KKVMNDKNVD SLETLIRHAL DNGVKLIACT MSMDIMGITK EELIDGVEFA
GVASYLGDAE ESNVNLFI
//
