ID A0A1P8U5L9_9MICO Unreviewed; 563 AA.
AC A0A1P8U5L9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:APZ33409.1};
GN ORFNames=BOH66_03290 {ECO:0000313|EMBL:APZ33409.1};
OS Microbacterium aurum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=36805 {ECO:0000313|EMBL:APZ33409.1, ECO:0000313|Proteomes:UP000187185};
RN [1] {ECO:0000313|EMBL:APZ33409.1, ECO:0000313|Proteomes:UP000187185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 15219 {ECO:0000313|EMBL:APZ33409.1,
RC ECO:0000313|Proteomes:UP000187185};
RA Jung Y., Shin J.-H., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "Complete genome sequence of Microbacterium aurum KACC 15219.";
RL Submitted (DEC-2016) 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; CP018762; APZ33409.1; -; Genomic_DNA.
DR RefSeq; WP_076689261.1; NZ_JAFBCQ010000001.1.
DR AlphaFoldDB; A0A1P8U5L9; -.
DR STRING; 36805.BOH66_03290; -.
DR KEGG; maur:BOH66_03290; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000187185; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
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 InterPro; IPR001307; Thiosulphate_STrfase_CS.
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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000187185}.
FT DOMAIN 461..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 563 AA; 58833 MW; 883D5D12400F5978 CRC64;
MRIVIVGGVA GGMSCAARAR RLDETAEIIV LERGEHVSYA NCGLPYFVGG EISDPAKLLV
QTPQSLHAAL NLDVRTRHDV TGLDPEQRVV TVDTPDGTMR IGYDALVLSP GAQAARPPIP
GLDSPRVRTL RTVDDALALR EQVEAGARRA VVLGAGFIGI EAAEALARQG LDVSVVELAE
HVLPPLEPEL AALVSDELRL LGIELRTSIG AAGIQQGAEH DLVALSDGTL LPAELIVLSV
GVRPDTAVFE AAGVACERGA IVVDEHGRTS IPGVWAVGDA TVSVDAVTGV RRPVALAGPA
NRAGRLVADD ILRPGASRPI PHPVGTAIVR IGSLTAALTG VNRSALDAAG IGYRTIHLHP
NQHAGYFPGA TQLHLILHLR ETDGLLLGAQ AVGAEGVDKR IDVLATAIRA GMVVDELIDL
DLAYSPPYGQ AKDPVNLAGM IGENVRTGTL ALWYAQDVDH VLADAFVLDT RSRAEFATGH
LPGALNVPHT ELRDRLDEVR TAAAGRPVRV MCASGVRSAI AHRVLAQAGF DSASLSGGIL
TLRAALGDRA AELLRFEGAM QDA
//
