ID B1LY82_METRJ Unreviewed; 441 AA.
AC B1LY82;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACB25853.1};
GN OrderedLocusNames=Mrad2831_3879 {ECO:0000313|EMBL:ACB25853.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB25853.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB25853.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) 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; CP001001; ACB25853.1; -; Genomic_DNA.
DR RefSeq; WP_012320810.1; NC_010505.1.
DR AlphaFoldDB; B1LY82; -.
DR STRING; 426355.Mrad2831_3879; -.
DR KEGG; mrd:Mrad2831_3879; -.
DR PATRIC; fig|426355.14.peg.3970; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_5; -.
DR OrthoDB; 7809559at2; -.
DR Proteomes; UP000006589; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 8..313
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..406
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 441 AA; 45910 MW; 2947D524538EEC14 CRC64;
MTPEPAGIVV VGASLAGLRG AEALRRGGYD GPLTLVGAEP YRPYDRPPLS KHVLAGELAA
DATRLPELAE LRARWRLGSP AVALDRAART LRLADGSTLA YESLLIATGA EARPWPAETG
GGLAGIFTLR GRDDAAALRD ALVARPRQVL IVGGGLIGCE AASCLRDLGL PVTLVDPNAA
PLARGLGTFV GSVIAECLRA SGATFRPGAT VRAFEGDASG HVARARLADG STIETNLVIV
ALGATRATGW LRGAGLRADA GGVTCDAACR VLDADRVPCP DIYAAGDVAR WPIPLYGNRL
IAVEHWGNAV EQAAHAARNM LADPGDQRPY GHLPAFWSSQ FGINIKLVGL PDGADSVAVV
QGSRASRRFL AVYGRAGRSI AAVSFDQARW LPAYAEAITA GDPFPPITDA TDRPRVEMAV
PGFPPPHRAA EARPSAETVH V
//
