ID E7RIE6_9BACL Unreviewed; 445 AA.
AC E7RIE6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Multifunctional NAD(FAD)-dependent oxidoreductase/hodanese domain-/SirA-like redox domain/Peroxiredoxin {ECO:0000313|EMBL:EGA89261.1};
GN ORFNames=GPDM_11280 {ECO:0000313|EMBL:EGA89261.1};
OS Planococcus donghaensis MPA1U2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA89261.1, ECO:0000313|Proteomes:UP000003052};
RN [1] {ECO:0000313|EMBL:EGA89261.1, ECO:0000313|Proteomes:UP000003052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA89261.1,
RC ECO:0000313|Proteomes:UP000003052};
RX PubMed=21994932; DOI=10.1128/JB.05983-11;
RA Pearson M.D., Noller H.F.;
RT "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals Nonsporulation
RT Pathways Controlled by a Conserved Spo0A Regulon.";
RL J. Bacteriol. 193:6106-6106(2011).
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:EGA89261.1}.
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DR EMBL; AEPB01000037; EGA89261.1; -; Genomic_DNA.
DR RefSeq; WP_008431396.1; NZ_AEPB01000037.1.
DR AlphaFoldDB; E7RIE6; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000003052; 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 NADP {ECO:0000256|ARBA:ARBA00022857}.
FT DOMAIN 3..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 329..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 445 AA; 48136 MW; C2F0AC0DE4DDB47B CRC64;
MKKIVIVGAV GGGATAAGQL RFYNPDVQIV VFDRDLTMSY AACGTPYVIG DVIEDEQSIV
LTNPEKFKKK RDIDVKLGHE VKEIDRAAKK VLVQNLETGN QFEESYDALI LAPGGSAILP
KIEGLDSSQV FTLRNFQDMQ RIDRFIKNEK PTSCVVSGGG FIGLEMAENL KNLGLDVSLV
HRSPAIMSIL DTDISLMIEK ELAVQGVKLL TGTEIVKTEE KTIKLSNGIE LQADFIIMSV
GLRPNTGLAV KAGLKIGETG GIQTNEFMQT DDPSIYAIGD ASENFDMVTG DPKRVPLASP
AHRQAFIAAR HILGDKIAKK GLLGTSVLKI FSLTAAMTGL NEKAIKDKNL ESATVTHNGI
SNAGYYPDHS KITLKVHYDP KTRKILGAQC IGGKGVDKRI DVIVTAIYGG LTIDDLQALE
LCYAPPYSSP KDPINMVGYK AVNDQ
//
