ID A0A0H3IZZ9_CLOPA Unreviewed; 821 AA.
AC A0A0H3IZZ9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KRU13371.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:AJA50617.1, ECO:0000313|EMBL:KRU13371.1};
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:AJA50617.1};
GN Name=cdr {ECO:0000313|EMBL:AJA50617.1};
GN ORFNames=CLPA_c05290 {ECO:0000313|EMBL:AJA50617.1}, CP6013_02619
GN {ECO:0000313|EMBL:KRU13371.1};
OS Clostridium pasteurianum DSM 525 = ATCC 6013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA50617.1, ECO:0000313|Proteomes:UP000030905};
RN [1] {ECO:0000313|EMBL:AJA50617.1, ECO:0000313|Proteomes:UP000030905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 525 {ECO:0000313|EMBL:AJA50617.1}, and DSM 525 / ATCC 6013
RC {ECO:0000313|Proteomes:UP000030905};
RX PubMed=25700415;
RA Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT Clostridium pasteurianum DSM 525.";
RL Genome Announc. 3:e01591-e01514(2015).
RN [2] {ECO:0000313|EMBL:KRU13371.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU13371.1};
RA Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KRU13371.1, ECO:0000313|Proteomes:UP000028042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU13371.1,
RC ECO:0000313|Proteomes:UP000028042};
RX PubMed=25103768;
RA Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Genome Announc. 2:0-0(0).
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; CP009268; AJA50617.1; -; Genomic_DNA.
DR EMBL; JPGY02000001; KRU13371.1; -; Genomic_DNA.
DR RefSeq; WP_004455218.1; NZ_JPGY02000001.1.
DR AlphaFoldDB; A0A0H3IZZ9; -.
DR GeneID; 76625012; -.
DR KEGG; cpae:CPAST_c05290; -.
DR KEGG; cpat:CLPA_c05290; -.
DR PATRIC; fig|1262449.3.peg.425; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR eggNOG; COG2210; Bacteria.
DR Proteomes; UP000028042; Unassembled WGS sequence.
DR Proteomes; UP000030905; 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 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:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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 Oxidoreductase {ECO:0000313|EMBL:AJA50617.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030905}.
FT DOMAIN 464..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 821 AA; 90035 MW; E407BFC5BACD2641 CRC64;
MKKKILIIGG VAGGASAAAR LRRLDEDAEI IMFEKGEYIS FANCGLPYYI GETIKDRKKL
IVQTPENMVK RFNVDVKPNS EVIGVDTNRK FVKVNSKDKG IYEENYDYLI LSPGAKPMKP
NIEGIDSKKI ITLRNIPDTD KIKNYVDNND IKNTVVIGGG FIGVEMAENL VQRGINVTLV
EAAPHILAPF DTDMTVIAEK ELESNGVNLI LGDGVKSFKD TENSLEILLS SNTKLTTDLV
ILAIGVVPDT DFIKGSQIKL GKRGHILVDK NMKTNIENIY AVGDAVEIKD FVNGQSTAIP
LAGPANKQGR IAADNIAGLN KSFNGSQGTA IIKIFGLTAA NTGNNERTLK RLDIPYKVIY
VHPVSHASYY PGASPISIKL IFNEKGTILG AQAMGYEGVD KRIDVIASVM RLHGTIYDLT
ELELNYAPPF SSAKDPVNMA GFTAENVLTG KSEVITPTEL YYYDLSNSIL VDVRSKLEFN
NGHIDGAINI PVDNLRERLS ELDKNKEIIV YCQVGLRGYV AERILKQKGF KVKNLTGGYK
TASMLNYKPK EINFTEQKEL DSESMKEVAA TDGNYNCNKV LDTCGLCCPG PLMEVKKSVD
ELKNGETLKV TASDPGFYED IKSWCNTTNN TLINLTKDNA NITALIKKNC ETLEKTSSNI
SVPPANTNKT MVVFSGDLDK AIASFIIANG AASMGKKVTM FFTFWGLNVL RKSEKVSVKK
SFIEKMFGIM MPRGSKKLKL SNMNMLGMGA KMIRGIMKNK NVSSLEDLME TAIANGVEIV
ACQMSMDVMG IQKEELIDDI KIGGVGYYLG EAENSNVNLF I
//
