ID F0J769_ACIMA Unreviewed; 414 AA.
AC F0J769;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:BAJ82936.1, ECO:0000313|EMBL:GAN72955.1};
GN OrderedLocusNames=ACMV_P1_01400 {ECO:0000313|EMBL:BAJ82936.1};
GN ORFNames=Apmu_0041_03 {ECO:0000313|EMBL:GAN72955.1};
OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS 301).
OG Plasmid pACMV1 {ECO:0000313|EMBL:BAJ82936.1,
OG ECO:0000313|Proteomes:UP000007100}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ82936.1, ECO:0000313|Proteomes:UP000007100};
RN [1] {ECO:0000313|EMBL:BAJ82936.1, ECO:0000313|Proteomes:UP000007100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:BAJ82936.1}, and DSM 11245 / JCM 8867
RC / AIU301 {ECO:0000313|Proteomes:UP000007100};
RC PLASMID=pACMV1 {ECO:0000313|EMBL:BAJ82936.1,
RC ECO:0000313|Proteomes:UP000007100};
RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA Hosoyama A., Yamada R., Fujita N.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAN72955.1, ECO:0000313|Proteomes:UP000032662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:GAN72955.1,
RC ECO:0000313|Proteomes:UP000032662};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (NOV-2012) 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; AP012036; BAJ82936.1; -; Genomic_DNA.
DR EMBL; BANA01000041; GAN72955.1; -; Genomic_DNA.
DR RefSeq; WP_013634969.1; NC_015178.1.
DR AlphaFoldDB; F0J769; -.
DR KEGG; amv:ACMV_P1_01400; -.
DR HOGENOM; CLU_003291_4_0_5; -.
DR OrthoDB; 7809559at2; -.
DR Proteomes; UP000007100; Plasmid pACMV1.
DR Proteomes; UP000032662; 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; 3.30.390.30; -; 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 Plasmid {ECO:0000313|EMBL:BAJ82936.1}.
FT DOMAIN 9..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 321..407
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 414 AA; 43451 MW; D01A6EEA6277DCA0 CRC64;
MPATSDPGIV IIGAGEAGVL AALTLREREY AGPITIIGAE RHPPYERPPL SKTVLTAADL
PIPTLIGGAD MLTGQNILCR SGVVATGLDR EARAVQLQDG TRLSYSRLLL ATGARPRTLS
VPETEARNVL YLRTFNDALA LRARLSRGAR LVVIGGGFIG LEVAASAVER GCDVTIVEAA
PRVLGRAVPA ELAAIITTRH RTAGVTIIEG AALAAIEERA VILAGGRALE ADVIVVGIGA
VPQTCLAEAA GLAIDNGIRV DEHLATDDPA IFAAGDCCSF PHPVFGGRRL RLEAWRNAGE
QGRHAANAML GATESFASIP WFWSEQYGDT LQIAGLPDEG DETVTRDNDG TPFLFHLKSG
RIVGASAFGP IGKIARDIRL AEKLIETGAC PPATALQDPA VKLKTLLQPR ANME
//
