ID A0A0B2ADD0_9MICO Unreviewed; 552 AA.
AC A0A0B2ADD0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KHK99817.1};
GN ORFNames=LK09_00265 {ECO:0000313|EMBL:KHK99817.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK99817.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK99817.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK99817.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) 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:KHK99817.1}.
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DR EMBL; JTDK01000001; KHK99817.1; -; Genomic_DNA.
DR RefSeq; WP_039394072.1; NZ_JTDK01000001.1.
DR AlphaFoldDB; A0A0B2ADD0; -.
DR STRING; 1348253.LK09_00265; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000031030; Unassembled WGS sequence.
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:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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:UP000031030}.
FT DOMAIN 457..543
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 552 AA; 57147 MW; F4CAB47ADAA82FEA CRC64;
MKTVIVGGVA GGMSAATRLR RLDEDAQIVV FERGAYVSYA NCGLPYYVGG VIRDRDALLL
QTPESLAARF RLDVRVEHEV TGIDADGRTV TVLDRTTGAT STETYDELIL AVGASARTGG
GGIPSRTLRT VDDVDAIDAL IAGAGEAPHA LVVGGGFIGL EAVENLVRRG VRTTLVQRGA
HILSPLDSEM ASPVDAELRR HGVDVRTSTT IARIDDGVVR LDDGTRLQPD FLVDAAGVVP
NVDLALLAGV PLGPTGGIAV DAQGRTGIPH ISAVGDGVEK IDALSGAESL VTMAGLANRH
GRSVADVLAG RHESHTPALG TSIVKVFDVV AAKTGWSERE LVAAGRAHRV IHTHPASHAT
YYPGAQTMSM KLLVDPATDA ILGAQVVGGE GVDKRIDVIA VAMAGGISAS GLSRLELAYA
PQFGSAKDPV NQLGYVADNL RTGTTRAIQW HELDAAQDAG ATVLDVRSPA EHAAGGIPGA
VNIPVDELRD RLTEIPDGPV VVHCAVGQRG HTAARILSQR GFDVVNLDGG YRTWVAGAAA
AGRAPQASRA AA
//
