ID K0CFA1_ALCDB Unreviewed; 579 AA.
AC K0CFA1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Sulfite reductase (NADPH)-like protein {ECO:0000313|EMBL:AFT71308.1};
GN Name=cysJ {ECO:0000313|EMBL:AFT71308.1};
GN OrderedLocusNames=B5T_03040 {ECO:0000313|EMBL:AFT71308.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71308.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT71308.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT71308.1; -; Genomic_DNA.
DR RefSeq; WP_014995374.1; NC_018691.1.
DR AlphaFoldDB; K0CFA1; -.
DR STRING; 930169.B5T_03040; -.
DR KEGG; adi:B5T_03040; -.
DR PATRIC; fig|930169.3.peg.3003; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_001570_17_7_6; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000006286; Chromosome.
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 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:UP000006286};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 56..194
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 223..437
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 200..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64551 MW; 1A147C8765AC4C23 CRC64;
MTAQATPPPF SDPQWSQLRQ WLETLDERQR WWLSGYLAAA NSAPAAVAGT EGTQPVLIGY
GTETDNCRHL ARTLSEHCGD AGIATEVVDL ARLRPRQLAR RDHLVIITAT HGDGDPPEPI
QDFYQGLMGD GAPQLANLKF AVLALGDSSY ERFCVTGQEF DQRLEALGGE RLIARQDCDV
DFEQPARDWI ARLLEKLPKA NTTDTAQGPA RAPTSSPPSY DKHHPLTVEV LVNQNLSAAD
RAQPIHHLEL ALDQAIPDLF PGDAVGILAD NPPELVAAVL DACELSGEQP VTVNDDAQPL
VQALRQTRDL TIAGTSFLAF WAEQSQAPAL LELCQAESRR QRAFLRDHQL LDLLHQYPAR
PPAQALVEAL RPLQPRLYDV ANSLAVLDDE LHLTVKAFHY PFRERHEQGI ASRYLLDLQP
GDPVRLYPHR NARFRLPDDD APLILIAEGT GIAPYRAFLQ ALSQQSQRPP CWLVFAEQRF
EDDFLYQLDI QQARADGVLE RVDTVFYQDQ PGAGLITPLL DQIDRLGTWI DRGAHLYLCG
DKGRLSDLES GLKTALDQRQ GDGAWKQLGR EKRLHRNLY
//