ID A0A1V0GT22_9RHOB Unreviewed; 397 AA.
AC A0A1V0GT22;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:ARC36982.1};
GN ORFNames=A6J80_11910 {ECO:0000313|EMBL:ARC36982.1};
OS Paracoccus yeei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC36982.1, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) 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; CP020442; ARC36982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GT22; -.
DR STRING; 147645.A6J80_11910; -.
DR KEGG; pye:A6J80_11910; -.
DR eggNOG; COG1251; Bacteria.
DR Proteomes; UP000191257; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
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; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000191257}.
FT DOMAIN 2..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 316..397
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 397 AA; 41645 MW; 7D3200AA700F7BD5 CRC64;
MNIAILGAGQ AAASLAARLR ALGHGGPITV IGDEAAPPYQ RPPLSKAYLL GQMDLDRLTL
RAPDWWADQN IALRLGETAT AIDRDARVVR TDRGEYPYDR LALTLGARPR RLPAAMGGEM
PGVHVVRNLA DIAVLRPALA PGRRLVVIGG GYIGLEAAAV ARKLGLAVTL VEAAPRILGR
VAAAETADMI RDLHRTHGVE IIEGVDIARI TGDTAANGVA LADGRHLPAD LVICGIGVSP
ETALAEAAGL EIDNGIAVDA RGRTSDPAVW AAGDCASFPM SRGRLRLESV GNAIDMAEAV
AANMLGAGAD YVPKPWFWSD QFDAKLQIAG LNLGYDRVVT RPGANGGSVW YFRDGGLIAV
DALNDPRAYM IGKRLIEAGR SPAPEAIAEA PDLKALL
//
