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Database: UniProt
Entry: A0A158M5W2_9BORD
LinkDB: A0A158M5W2_9BORD
Original site: A0A158M5W2_9BORD 
ID   A0A158M5W2_9BORD        Unreviewed;       434 AA.
AC   A0A158M5W2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Flavodoxin {ECO:0000313|EMBL:KAK90763.1};
GN   ORFNames=L497_0707 {ECO:0000313|EMBL:KAK90763.1};
OS   Bordetella holmesii CDC-H585-BH.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK90763.1, ECO:0000313|Proteomes:UP000026682};
RN   [1] {ECO:0000313|EMBL:KAK90763.1, ECO:0000313|Proteomes:UP000026682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK90763.1,
RC   ECO:0000313|Proteomes:UP000026682};
RA   Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA   Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA   Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA   Losada L.;
RT   "Genome sequence of Bordetella holmseii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KAK90763.1}.
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DR   EMBL; JFZZ01000070; KAK90763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158M5W2; -.
DR   STRING; 35814.BBB42_06840; -.
DR   PATRIC; fig|1331206.3.peg.1909; -.
DR   Proteomes; UP000026682; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          30..169
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          183..297
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   434 AA;  47380 MW;  88205F4F1E095119 CRC64;
     MLVIAWLLLS WRAWRRSRPT PVPLAQAEAW LVAHASQTGL AQELAERSAE ALRAAGQVAV
     VVPLNQVDAP CLARCTRALL VVSTYGEGDA PDGAARFAQQ VMRPVMHGSL PQLRYALLAL
     GDSSYARFCG FGRELDQWLA AQKAQRLFDR VEVDRADPAA LRHWQRELAA ICGAADPQVW
     QAPDYQTWRL TARQHLNPGS SAGPCYLVSL TCQTEVFWQA GDIAEVGPRT APQTPLQNPR
     EYSIASLPAD GCLQLLVRQQ RHADGTLGLG SGWLTQRCPI GGEVALRVRS NPGFHLPPGP
     MPLVLIGNGT GLAGLRAWLK ARVAAGHGRN WLVYGERHPA YDALLEDELR AWKATGMLAQ
     LDLVYSRQGQ GYVQDRLRER ADALRSWVDN GATIAICGSL HGMAQGVDDA LSDILGVPLL
     LALRADGRLR RDVY
//
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