ID A0A0R2PMG1_9MICO Unreviewed; 554 AA.
AC A0A0R2PMG1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KRO39253.1};
GN ORFNames=ABR66_04890 {ECO:0000313|EMBL:KRO39253.1};
OS Microbacteriaceae bacterium BACL25 MAG-120322-bin65.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae.
OX NCBI_TaxID=1655574 {ECO:0000313|EMBL:KRO39253.1, ECO:0000313|Proteomes:UP000053725};
RN [1] {ECO:0000313|EMBL:KRO39253.1, ECO:0000313|Proteomes:UP000053725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL25 MAG-120322-bin65 {ECO:0000313|EMBL:KRO39253.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KRO39253.1}.
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DR EMBL; LIAY01000046; KRO39253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PMG1; -.
DR Proteomes; UP000053725; 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; 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 461..543
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 554 AA; 58369 MW; C5AEAF3031253039 CRC64;
MSPQRETVQK VVIIGGVAGG MSAATRLRRI NESAEITVIE RGSAVSFANC GLPYHVGKVI
EDRSSLVLQH PAGLKSRFNI DVHIHTEATA IHPSEKTVSV TNLTTGESRD IAYDALVLSP
GSTPFRPPIP GVDTAHVLWS LEDMDRLIEA AEGAKTAVVV GGGFIGVELA ENLHHRGISV
TLVEALPQLM ATLDVEMAWP LVERARHQGL DVRVSTQVSA ITGSGVSLSD GSDISADLVV
VAVGARPNTE LAIQAGLDMG DSGGVAVDEQ QRTSDPHIWA VGDVAQKARA DGHSLVPLAG
LANRHGRLAA DSIMGRPAQA VRAHGTSIVG FFGLAAASTG YTERVLAQKN RAMRIIHTHP
FNHAGYYPGA SQMAMKLIVD PATDAILGAQ VVGDDGVDKR IDVIATAMAA GITASGLMDL
ELSYAPQFAS AKDPINMLGY VNENRALGEV SIQWHEVESY LEQGWQLLDV RTMGEYSQGA
IPGSQLITLD ELRGHVEGLR GSKVIVTCRV GQRGHTAASI LAQAGIEVAN LDGGYLTWQL
GTAASAQPAL SSTH
//