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Database: UniProt
Entry: A0A0R2PMG1_9MICO
LinkDB: A0A0R2PMG1_9MICO
Original site: A0A0R2PMG1_9MICO 
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
//
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