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Database: UniProt
Entry: A0A3P0XAG7_9BACT
LinkDB: A0A3P0XAG7_9BACT
Original site: A0A3P0XAG7_9BACT 
ID   A0A3P0XAG7_9BACT        Unreviewed;       597 AA.
AC   A0A3P0XAG7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Sulfite reductase subunit alpha {ECO:0000313|EMBL:RRA49606.1};
GN   ORFNames=D1Y84_16350 {ECO:0000313|EMBL:RRA49606.1};
OS   Acidipila sp. EB88.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidipila.
OX   NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA49606.1, ECO:0000313|Proteomes:UP000279598};
RN   [1] {ECO:0000313|EMBL:RRA49606.1, ECO:0000313|Proteomes:UP000279598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB88 {ECO:0000313|EMBL:RRA49606.1,
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:RRA49606.1, ECO:0000313|Proteomes:UP000279598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB88 {ECO:0000313|EMBL:RRA49606.1,
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:RRA49606.1}.
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DR   EMBL; QWEV01000005; RRA49606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P0XAG7; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000279598; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; 3.40.50.360; -; 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; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
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; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279598};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          47..185
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          228..446
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   597 AA;  64950 MW;  44AED42A85A45565 CRC64;
     MTTATVPFIP DNAPFSTEQR AWLNGFLAGL FSQAPAQQPA PSPALSLTVL YATQGGTAER
     LAKKVAKELK AKGHTTELFS LEDMPPATLA DKEHALILAS TYGEGDPPDA CRRFADAMSA
     PDAPRMEKLR YSVFALGDHS YEHFCKFGVD LDERLAALGA ERLMPRVESG VDVDAPFDQW
     KSSLSSRLAE RVAGSSGKSA PASMVATATS AVAPGVGAAK IEPLHTRDHP FLAPLRARTP
     LTSGHSSKVT MHLAFDIEDA QIEYAAGDSC GVVPTNDPVL VADILEALAF DAGASIALPK
     VGEVSMEQAL LHHLQPTRLT RKIVQAFASK SGSKTLTALL PAEQSAHLES FMYDRGLIDL
     LLEYPGLITE PAEIAAMLPR LSPRLYSISS SPAAHGREVH TTVAVVRYKA HGRERGGICS
     TLLADRTGVG ARLPIYIQAN PKFRIPENNH TPIIMVGPGT GIAPFRSFLY ERRALGASGK
     NWLFFGERSA STDFLYCEEL RAMAADGHLT RLDTAFSRDQ EHKIYVQDRM LERGAELWHW
     LGEGAVFYVC GDASRMAKDV DAALHTVVEQ HGGMDRDAAR EYISQLHDEH RYHRDVY
//
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