ID A0A0N7I396_9MICO Unreviewed; 546 AA.
AC A0A0N7I396;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ALJ18703.1};
GN ORFNames=AOA12_01760 {ECO:0000313|EMBL:ALJ18703.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ18703.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ18703.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ18703.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-2015) 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; CP012697; ALJ18703.1; -; Genomic_DNA.
DR RefSeq; WP_054679289.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0N7I396; -.
DR STRING; 1714373.AOA12_01760; -.
DR KEGG; mio:AOA12_01760; -.
DR PATRIC; fig|1714373.3.peg.379; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000059097; Chromosome.
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: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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000059097}.
FT DOMAIN 454..540
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 546 AA; 56893 MW; E34E537EFE791F1A CRC64;
MRIVIVGGVA GGMSCAARAR RLDESAEIIV IERGAHPSFA NCGLPYFVGG EITDERALLV
QTPASLRAAL NLDVRPHSEV VAVDTVARTV TVAAADGTYT LDYDALVLSP GASAVRPPIP
GIDAPHVQTL RTVEDAVALR DRVTAGTRAV VLGAGFIGVE AAEALAQRGV EVALVELAAH
PLPPVEPELA SLVADELRRL GIDVRTGIAA SAVDGDAVVL EDGTRLPADV VVLSVGVRPD
TAVFEDAGIA CERGAIVVDE HGRTSADRVW AAGDATLSVD AVTGIRRPVA LAGPANRAGR
LIADDILGTG RRVPPPVGTA IVRVGELTAA LTGANRASLR AAGIAFETIH LHPNQHAGYF
PGVARLSMVV HFGADDGRLL GAQIVGTEGV DKRIDVIATA MRFGAVVDDL IDLDLAYSPP
YGQAKDAVNL TGLVGQNVRT GTLRLWYADD LEAVRAEALV LDVRRADEVA KRALPDALHI
PHTELRERLD EVRAAAAGRP VRVLCQSGVR SAIAHRVLTQ AGFDSASLSG GMLTLHATLG
DHPFPP
//
