ID U2N6T6_9CLOT Unreviewed; 550 AA.
AC U2N6T6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase dimerization subunit {ECO:0000313|EMBL:ERK31232.1};
GN ORFNames=CINTURNW_1807 {ECO:0000313|EMBL:ERK31232.1};
OS Clostridium intestinale URNW.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK31232.1, ECO:0000313|Proteomes:UP000016721};
RN [1] {ECO:0000313|EMBL:ERK31232.1, ECO:0000313|Proteomes:UP000016721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URNW {ECO:0000313|EMBL:ERK31232.1,
RC ECO:0000313|Proteomes:UP000016721};
RX PubMed=24136853;
RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT Clostridium intestinale Strain URNW.";
RL Genome Announc. 1:e00871-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERK31232.1}.
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DR EMBL; APJA01000012; ERK31232.1; -; Genomic_DNA.
DR RefSeq; WP_021801810.1; NZ_KI273145.1.
DR AlphaFoldDB; U2N6T6; -.
DR STRING; 1294142.CINTURNW_1807; -.
DR PATRIC; fig|1294142.3.peg.1841; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000016721; 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 Reference proteome {ECO:0000313|Proteomes:UP000016721}.
FT DOMAIN 465..549
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 550 AA; 60765 MW; ADB54DD73F2F8DEC CRC64;
MKIAIIGAVA AGTSAAAKAR RNDETAEIKI FEMGEEISYS SCGLPYYIGN EIQNREQLVP
RDVKFFKSKY NVDILIRHKV LSVDVNAKEL KVENLSSGKV FIEKYDKLVI STGATPILPR
IEGIDKDNVF VLRDVISADK IKNYIEKSKP KKALVVGSGF IGLEMVENLK NIGIDVTVVE
MEDHLMKPLD KDVSLYLKDT LLKHEINVIL NDGVVKFEGD SVARRVFLKS GKHIETDMVL
VATGVRPNVE LAKNAGVEIG ETGAIKVNNK MQTNIEDIYA CGDCAESYSI VTGKHFYRPL
GSTSNKMGRI AGDQITGGDL EFRGIVGTGI FKIFDMAVAQ TGLTEVEAIN EGYDISVSHN
IKPDKPPYYH GEEMLIKAVA DKKTEKLLGV QIVGKAGVDK RIDVFVTAIT FGAKVSDLFH
LDLAYAPPFS TAKDPVMYTG MILTNDINSN RKLITPNKLQ EKIDNNEDII IIDTREPKQY
EVSHVDGAIN IPHKELRDKA NTLDKEKLTI TYCNKGVTGN ATQNILLNMA FKNVYNLSGG
NKNYSKILKK
//
