ID E3EE44_PAEPS Unreviewed; 554 AA.
AC E3EE44;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:ADO54524.1};
GN Name=ndh1 {ECO:0000313|EMBL:ADO54524.1};
GN ORFNames=PPSC2_02825 {ECO:0000313|EMBL:ADO54524.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO54524.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO54524.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO54524.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002213; ADO54524.1; -; Genomic_DNA.
DR RefSeq; WP_013369164.1; NC_014622.2.
DR AlphaFoldDB; E3EE44; -.
DR STRING; 1406.LK13_15640; -.
DR KEGG; ppm:PPSC2_02825; -.
DR PATRIC; fig|886882.15.peg.535; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000006868; Chromosome.
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; 3.50.50.60; 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; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT DOMAIN 465..545
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 554 AA; 60647 MW; BB8AD3E6B52EA413 CRC64;
MGRKIIIIGG VAGGASAAAR LRRWSEEDEI ILFERGEHVS FANCGLPYYI GGTIQAREKL
FLQTPQGIRD RFNIDVRVQK EVIQIDREHK LVHYRDMITG ETDEQPYDIV VLSPGAKPMI
PDIPGLHEAT NVFTLRNIHD TDLIKAYVDE RHPKHATVIG AGFVGLEMAE NLRERGLAVT
IMDKGQQLLN PLDPEMAKLV EQHVKLNGVE VRLEEGVAAF EEQGTQLRLT SGEMLQTDLV
ILAIGVVPEN ELAKQCGLEL GFRGAIQVNA QLQTSDPSIY AVGDAIQVKD RNHGFATMVS
LAWGANRQGR LAADHINGQA ISYDGALGTS VIKTFALTAA STGNNEKTLQ RLAVPYQAIH
IHPGSHAGYY PGASPISMKL LFHPETGMIY GAQAVGADGA DKRIDVIATA IRGHLNVREL
ADIELAYAPP YSSAKDPVNM AGYVASNIMD GLVQTIQWHE VDDFHRNGGL VIDVRDAVEL
QGGTIPGSMH IPLVEIRERM SEIPRDLEIA VSCQVGLRGY LAARILTQSG YRVRNVDGGY
KTYSVMAKRD HLLK
//
