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Database: UniProt
Entry: K0CFA1_ALCDB
LinkDB: K0CFA1_ALCDB
Original site: K0CFA1_ALCDB 
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
//
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