ID B0SNL5_LEPBP Unreviewed; 587 AA.
AC B0SNL5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component (SIR-FP) {ECO:0000313|EMBL:ABZ97296.1};
DE EC=1.8.1.2 {ECO:0000313|EMBL:ABZ97296.1};
GN Name=cysJ {ECO:0000313|EMBL:ABZ97296.1};
GN OrderedLocusNames=LEPBI_I1180 {ECO:0000313|EMBL:ABZ97296.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97296.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97296.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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};
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DR EMBL; CP000786; ABZ97296.1; -; Genomic_DNA.
DR RefSeq; WP_012388177.1; NC_010602.1.
DR AlphaFoldDB; B0SNL5; -.
DR STRING; 456481.LEPBI_I1180; -.
DR KEGG; lbi:LEPBI_I1180; -.
DR HOGENOM; CLU_001570_17_7_12; -.
DR OrthoDB; 9789468at2; -.
DR BioCyc; LBIF456481:LEPBI_RS05785-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABZ97296.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 68..205
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 235..437
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 587 AA; 65513 MW; E8FAE7A3E8B2F844 CRC64;
MLSDEKRNRF LQLLKESTKD EWVWMSGYLS ALTQASIGGS VDVSLNAPVS ISSNDPSHGN
LKAAPIQCTV VYGTETGNSK KLATELVKKL KELGVQAKLK STDTYKAKDL KEEEYLFVIV
STHGDGEPPQ AAKPFIQILS DAKDSLSKMK FAVLGLGDTS YPLFCQTGID VDSMLEKLGA
ERIHDLGKCD VDFELVSKPW ITDLISKLNA ISKTATTQVS KQTQTTASKP NSGGKVVYEG
TIVTNLVLND IGATKSTRHI EIKSSLPVDY LPGDSAGFLA YNREDEVNRI LGLLQTDRET
RVTYKGETWM LYDLLRKKVS IRFLPDRVIQ KYVSLSKKEI PSGKLDLDVL LTLYPSDTKL
EIQSIVDILE PIVPRYYSIA SSPSAHGEEE VHLTVAEVEI ETFTGIKTGF CSGFLSSLKE
GDTVPFFIQK NNSFRLPSPD TDIIMIGPGT GIAPFRSFLF EREQSGGNGK NWLFFGERNF
VSDFYYQTEL LELMDTGVLH KLNTAFSRDT KEKVYVQDRM GENAEELLKW IQNGAVIYLC
GSKDPMSKDV DRKLIEILSE RTFDTGKEAS DYLKELEENG RYIKDVY
//
