ID A0A3P0XBV4_9BACT Unreviewed; 379 AA.
AC A0A3P0XBV4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:RRA49717.1};
GN ORFNames=D1Y84_17040 {ECO:0000313|EMBL:RRA49717.1};
OS Acidipila sp. EB88.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA49717.1, ECO:0000313|Proteomes:UP000279598};
RN [1] {ECO:0000313|EMBL:RRA49717.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA49717.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Pold G., Deangelis K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRA49717.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA49717.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Horta L.;
RT "Genome sequence of EB88, a novel member of the group I Acidobacteria.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:RRA49717.1}.
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DR EMBL; QWEV01000005; RRA49717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P0XBV4; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000279598; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06199; SiR; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000279598}.
FT DOMAIN 11..228
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 379 AA; 43190 MW; 25174A0FB03D0CEF CRC64;
MSTEKQKYTR NNPFMSRMLV NSRMTDPVSE KETRHIELSL EPGMDYTPGD AVGIVPENRP
SEVAEVLAAL HLTGDERVLD HYKKEISLEE ALRTRLAIGK LTRSSVVQYG KLVQHADLQL
LSQAEHRSKA DEWVYGREFI DLLREYPGGI TNPQQLFTVL ARLTPRMYSI ASSQAMANDA
VHTIVRVIRY HTHNRDRQGL CSGHLGERAP EGESMPIFLH ANNNFRLPED PTAPVIMVGP
GTGIAPFRAF LQHRKAHGHT GQNWLFFGDQ RRETDFLYKD DLEGMVKDGV LTRLDLAFSR
DQPKKVYVQD RMTENGHELF QWLERGAYFY VCGDATRMAK DVETALLDSI AKGHNSTPDD
AQAYLAEMKK NKRYQLDVY
//
