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Database: UniProt
Entry: A0A0H3CBK6_CAUVN
LinkDB: A0A0H3CBK6_CAUVN
Original site: A0A0H3CBK6_CAUVN 
ID   A0A0H3CBK6_CAUVN        Unreviewed;       504 AA.
AC   A0A0H3CBK6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Sulfite reductase (NADPH) flavoprotein alpha-component {ECO:0000313|EMBL:ACL96624.1};
DE            EC=1.8.1.2 {ECO:0000313|EMBL:ACL96624.1};
GN   OrderedLocusNames=CCNA_03159 {ECO:0000313|EMBL:ACL96624.1};
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL96624.1, ECO:0000313|Proteomes:UP000001364};
RN   [1] {ECO:0000313|EMBL:ACL96624.1, ECO:0000313|Proteomes:UP000001364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX   PubMed=20472802; DOI=10.1128/JB.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP001340; ACL96624.1; -; Genomic_DNA.
DR   RefSeq; WP_010920899.1; NC_011916.1.
DR   RefSeq; YP_002518532.1; NC_011916.1.
DR   AlphaFoldDB; A0A0H3CBK6; -.
DR   SMR; A0A0H3CBK6; -.
DR   GeneID; 7330997; -.
DR   KEGG; ccs:CCNA_03159; -.
DR   PATRIC; fig|565050.3.peg.3085; -.
DR   HOGENOM; CLU_001570_17_7_5; -.
DR   OrthoDB; 9791166at2; -.
DR   PhylomeDB; A0A0H3CBK6; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   CDD; cd06200; SiR_like1; 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   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; 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; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:ACL96624.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        14..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..192
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          206..365
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   504 AA;  54240 MW;  159EE54FE3B2B443 CRC64;
     MPDLAFLPPE ARRWVWAGVV VALYALFCLA IALREAWRGR QARKAADALS QGSGEPVLVA
     YASQTGFAEE LATATAKALA DTGAPVTLKD LSAVTAGDLA GRALFVVSTT GEGDAPDPAR
     AFIRDVMKDE ADLSALRYGV LALGDSSYAH YCAFGRSLDA WLSGRGGQPL FDRVEVDDAD
     PAALRHWQGQ LATLTGVTDA PDWTRPTYDA WTLAERTLLN PGSPGGEAWH LRLTPPKGAV
     WQAGDIVEIG PRNDPAQVAA LIAALDLPAE AADTLAGLRL PQDAAALDAL RGLPLEALAE
     RLTALPHREY SIASLPDDGG VELIVRLMTR ADGAPGLGSG WLCRHAPIGA AIEARVRVNR
     SFHAPETKRP LILIGSGTGL AGLRAHLKAR AAAGVRWNWL IFGERTAAHD YFHRAELEAW
     QASGLLDRLD LAFSRDQAER VYVQHRLRES ADILRRWVAN GAAIYVCGSL EGMSREAHTA
     LVEILGAPML ERLTDEGRYR RDVY
//
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