ID A0A0Q5CR08_9MICO Unreviewed; 460 AA.
AC A0A0Q5CR08;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KQQ28629.1};
GN ORFNames=ASF54_08255 {ECO:0000313|EMBL:KQQ28629.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ28629.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ28629.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ28629.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ28629.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ28629.1,
RC ECO:0000313|Proteomes:UP000051456};
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:KQQ28629.1}.
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DR EMBL; LMNV01000002; KQQ28629.1; -; Genomic_DNA.
DR RefSeq; WP_055960789.1; NZ_LMNV01000002.1.
DR AlphaFoldDB; A0A0Q5CR08; -.
DR STRING; 1736329.ASF54_08255; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000051456; 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:UP000051456}.
FT DOMAIN 2..312
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 334..437
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 460 AA; 48491 MW; 702A28C7EB530727 CRC64;
MHLVAIGGSD AGISAALRAR ELDPSVDVTV VVADAYPNFS ICGIPYFFSR EVQPWQSLAH
RTHADLEATG MNLRLETFAT SIDVTGHRLA VRALDGTEST IDYDALMVGT GALPSHAGIE
GLDTLGPEDG VHVIHSMGDT FALDRFLETR NPQTAIIVGA GYVGLEMAEA FTVRGIRTTQ
IQRGPEVLST LDPELGALVH TELTDHGVTV LTDTTVNRID KTGDALTVSA THLGEPVTHT
ADVVLVVVGV RPNTDLLERA GATLGAGRAV EVDDTMRTGL PDVFAAGDGV TTHHRLLGTT
YLPLGTTAHK QGRVAGENAL GGTARFAGSV GTQVVKVFDL VASRTGLREH EAAAAGFAPV
STTAIADDHK RYYPGAQPIS IRVTGDSRDG RLLGAQLVGR LGTETAKRVD TYAVALHAGL
TVEQVSELDL SYTPPLGSPW DAVQVATQAW SREHRQAVTA
//
