ID A0A1W5ZR25_9BACI Unreviewed; 557 AA.
AC A0A1W5ZR25;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:ARI75739.1};
GN ORFNames=HM131_02360 {ECO:0000313|EMBL:ARI75739.1};
OS Halobacillus mangrovi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=402384 {ECO:0000313|EMBL:ARI75739.1, ECO:0000313|Proteomes:UP000192527};
RN [1] {ECO:0000313|EMBL:ARI75739.1, ECO:0000313|Proteomes:UP000192527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTB 131 {ECO:0000313|EMBL:ARI75739.1,
RC ECO:0000313|Proteomes:UP000192527};
RA Lee S.-J., Park M.-K., Kim J.-Y., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F.,
RA Lee D.-W.;
RT "The whole genome sequencing and assembly of Halobacillus mangrovi
RT strain.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP020772; ARI75739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5ZR25; -.
DR STRING; 402384.HM131_02360; -.
DR KEGG; hmn:HM131_02360; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000192527; 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;
FT DOMAIN 465..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 557 AA; 60524 MW; 62E8CE2F3D4D36F3 CRC64;
MAKKIIIVGG VAGGATAAAR LRRLSEEDEI IMIEKGEYIS FANCGLPYYI GDVITNRDSL
LVQTVEGMSK KFNLEIRNLS EAIGIDRENR TLAIKDLRTG DVYNESFDRL ILSPGARPIV
PPFEGLQEAN HVFTLRSVPD TDQIKAWVDN KQPEKAVVIG GGFIGLEMAE NLVHRGVEVT
LVELGNQVMA PLDYEMASLV HKELVDKGVQ LILEDGVKSF EDEGKTIVLD SGTKLSSDLT
ILAIGVRPEN ELAVQAGLEV GKRGGIIVNE HLQTEDPDIY AIGDAIEVKD YIQHVPTMVP
LAWPANRQGR LVADHIHGKG VSYKGTLGTS VAKVFDLTVA ATGNNEKVLS RLGIASEVVH
IHPASNATYY PGGQPLALKL IFEPETGKLF GAQAVGYEGV EKRIDVIATA IKGGLNVADL
ADLELAYAPP YSSAKDPVNM AGYVASNIVD GEVNIVHYHE IDRIIEQGGL LVDVREPEER
EIGFIPGSIN IPLGDLRNRI EELPKDQTIY ITCQAGLRGY LATRILNHNG YESSNLSGGY
KTYQAGKCVW KENVVQS
//
