ID A0A0Q8PZV4_9ACTN Unreviewed; 457 AA.
AC A0A0Q8PZV4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KRB78927.1};
GN ORFNames=ASE01_23630 {ECO:0000313|EMBL:KRB78927.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB78927.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB78927.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78927.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB78927.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78927.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:KRB78927.1}.
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DR EMBL; LMIA01000004; KRB78927.1; -; Genomic_DNA.
DR RefSeq; WP_056748790.1; NZ_LMIA01000004.1.
DR AlphaFoldDB; A0A0Q8PZV4; -.
DR STRING; 1736488.ASE01_23630; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000050886; 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 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 PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000050886}.
FT DOMAIN 5..291
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 344..443
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 457 AA; 46869 MW; 1F59A9C12C52824B CRC64;
MTTVRIVVVG ANAAGMSAAH TVLRAARSAG RGVRVTAVEA SGHTSYSACG IPYWIAGDVS
SGDDLVARTA QQHRDAGIDL RLGTRAVGLD VSRRVLTCEG ETPGEVEYDE LVLATGATAI
VPDWARAAGG ALVPGVHPVK DLDDGEAWIE QLSAEPRRAV VVGAGYIGVE MAEALLRRGL
STTLLTRGRV MGGLDDDMGD RVAAGIREAG VDLRTETTVK RLETSEGRVS GVVTADGDVL
PADVVVLAIG VEPATALGSD AGLPVGEAGG YLPDAGGRIA AGVWAAGDCC EVEHRLTGQP
AFLPLGTHAN KLGRVVGDNL LGGDRRFGGA LGTAITRFVV DEVHVEISRT GLSSREADEA
GHDVVALVTE GSTISGYMPD AAPIATKVIA DRTTRALLGV QVVGGPGAGK RIDAAAAALW
GAMSVDDLAG MDLSYAPPFA TAWDALQIAA RRLAERI
//
