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Database: UniProt
Entry: R9AAY9_9LEPT
LinkDB: R9AAY9_9LEPT
Original site: R9AAY9_9LEPT 
ID   R9AAY9_9LEPT            Unreviewed;       589 AA.
AC   R9AAY9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Putative sulfite reductase (NADPH) flavoprotein, alpha component {ECO:0000313|EMBL:EOQ97360.1};
GN   ORFNames=LEP1GSC195_2124 {ECO:0000313|EMBL:EOQ97360.1};
OS   Leptospira wolbachii serovar Codice str. CDC.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1218599 {ECO:0000313|EMBL:EOQ97360.1, ECO:0000313|Proteomes:UP000013984};
RN   [1] {ECO:0000313|EMBL:EOQ97360.1, ECO:0000313|Proteomes:UP000013984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC {ECO:0000313|EMBL:EOQ97360.1,
RC   ECO:0000313|Proteomes:UP000013984};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (APR-2013) 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:EOQ97360.1}.
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DR   EMBL; AOGZ02000014; EOQ97360.1; -; Genomic_DNA.
DR   RefSeq; WP_015682657.1; NZ_AOGZ02000014.1.
DR   AlphaFoldDB; R9AAY9; -.
DR   STRING; 1218599.LEP1GSC195_2124; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000013984; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          70..207
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          237..439
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   589 AA;  65624 MW;  F48F44852F47FD26 CRC64;
     MLSDEKRNRF LQLLKESTKD EWVWMSGYLS ALTQPSIGGS SVDVSFTPPV SIDSGNDPLH
     GNLKTQPIQC SVVYGTETGN SKKLGTELVK KLKELGVSAK LKSTDTYKAK DLKEEEYLFV
     IVSTHGDGEP PQAAKPFIQI LADSKDSLAK VKFAVLGLGD TSYPLFCQTG EDVDSMLSKL
     GAERIQPLGK CDVDFDLVAK PWMSELISQL NARSKTATTQ NTTQTQTPIA KPASGGKVVY
     EGSVVTNIVL NDIGASKSTR HIEIKTPVPI DYQPGDSAGF LAYNRDEEVN RILSLLKTDR
     ESRVTYKGET WMAYDLFRKK VSVRFLPDRV IQKYATLVGK EIPSGKTDLD VLLTLHPSEK
     KIELQTLVDV LEPIVPRYYS IASSPSAHGE DEVHLTVAEV EIETFTGIKT GFCSGFLAEL
     KEGEVVPFFI QRNNSFRLPS PDTDIIMIGP GTGVAPFRSF LFEREQNAGN GRNWLFFGER
     NFVSDFYYQT ELLELMDTGV LHRLNAAFSR DTKQKVYVQD RMGENAAELL KWIENGAVIY
     LCGSKDPMSK DVDRKLIEIL SERTFDTGKD ASDYLKELEE AGRYIKDVY
//
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