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Database: UniProt
Entry: A0A2P8H9R4_9BACI
LinkDB: A0A2P8H9R4_9BACI
Original site: A0A2P8H9R4_9BACI 
ID   A0A2P8H9R4_9BACI        Unreviewed;       604 AA.
AC   A0A2P8H9R4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Sulfite reductase (NADPH) alpha subunit {ECO:0000313|EMBL:PSL42958.1};
GN   ORFNames=B0H94_11241 {ECO:0000313|EMBL:PSL42958.1};
OS   Salsuginibacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salsuginibacillus.
OX   NCBI_TaxID=517424 {ECO:0000313|EMBL:PSL42958.1, ECO:0000313|Proteomes:UP000242310};
RN   [1] {ECO:0000313|EMBL:PSL42958.1, ECO:0000313|Proteomes:UP000242310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.07653 {ECO:0000313|EMBL:PSL42958.1,
RC   ECO:0000313|Proteomes:UP000242310};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
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:PSL42958.1}.
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DR   EMBL; PYAV01000012; PSL42958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8H9R4; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000242310; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:InterPro.
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; IPR010199; CysJ.
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   NCBIfam; TIGR01931; cysJ; 1.
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   PIRSF; PIRSF000207; SiR-FP_CysJ; 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:ARBA00022605};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000207-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000207-1};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000207-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242310};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          70..208
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          238..453
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         76..81
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         123..126
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         159..168
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         391..394
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         409..411
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         424..427
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         524..525
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         530..534
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         566
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         604
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ   SEQUENCE   604 AA;  66450 MW;  7A666EF99CDB44A6 CRC64;
     MNIHATNSPF TEDQASLLNQ VLPSLSEQQR IWLSGYLTAA FAPAVTATAE PQPAPEAPAA
     APTSAPKRAI TLLIGSHTGN GQALAAEFKQ KLQNKAFDVQ AYDMDQFKPK QLKQVEDLLI
     ITSTHGEGDP PDNALTLYEH LYSKKAPDLT GVRFSVLALG DSSYEFFCQT GIDFDNRLAE
     LGAERLHDRV DCDVDFEAPA ASWLNGVIDK LGAASPVPAA AEETAAAAVA EAPVYSKKNP
     FWAEVVENFN LNGRGSNKET RHLVLDLEGS GLTYEPGDAL GLIPQNDPLL VDNIIAEAGW
     DPATYIQVDE ESPERPLRDV LIDTVEITVL TKPLLQKAAE ASGNPGLKEL VGGRVKAYTE
     GRDLLDLMKD YGPWQTSAAE TVAMLRKIPP RLYSIASSLT ANPDEVHLTI GALRYSAHGR
     PRNGVCSVQC AERVQPGEKL PVFIQQNPNF KLPDDPETAT IMIGAGTGIA PYRSFLEERE
     ETEATGDNWV FFGDQHFLTD FLYQTEWQSW LQDGTLTHMD VAFSRDGTEK TYVQHKLLAQ
     AEALYRWIEG GAYIYVCGDK NYMAKDVHEA LTTVIAEQSG RSNEEAEAYL SDLRQEKRYQ
     RDVY
//
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