ID   A0A1W6YW27_9BORD        Unreviewed;       688 AA.
AC   A0A1W6YW27;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:ARP85312.1};
GN   ORFNames=CAL13_03090 {ECO:0000313|EMBL:ARP85312.1};
OS   Bordetella genomosp. 9.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP85312.1, ECO:0000313|Proteomes:UP000194139};
RN   [1] {ECO:0000313|EMBL:ARP85312.1, ECO:0000313|Proteomes:UP000194139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17164 {ECO:0000313|EMBL:ARP85312.1,
RC   ECO:0000313|Proteomes:UP000194139};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021109; ARP85312.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6YW27; -.
DR   Proteomes; UP000194139; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR   Gene3D; 3.10.20.30; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR42815; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR   PANTHER; PTHR42815:SF2; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194139}.
FT   DOMAIN          331..434
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          599..688
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   688 AA;  74760 MW;  D2B5D3C2434E5E22 CRC64;
     MAQKPSKLPT WHAGEIFIQE KLGVAERMAV VGKRVVRDYM PDQHRDFYAQ LPFIVLGSVD
     AAGDAWATTL AGRPGFMTSP TPTILDISAR ADSGDPAGEG LGAGAPIGLL GIEMHTRRRN
     RMNGIIARVT DGLRVQVDQS FGNCPRYIQL RDFAFARDPG EAFAAPREDL AELDADARAA
     IAAADAFFVA SYADREDRRQ VDVSHRGGKA GFVRVADDGV LTVPDFDGNL FFATLGNIVL
     NGKAGLLFVD YERGDVLQMT GDAEVILDSP EIAAFQGAER LWTFRPRRIV RRRGALALRW
     TFQQDGWSPN SLMTGDWRQA AERLRASELA AQWRPFTVAR IVDESRSIRS FHLEPADGLG
     VLPHQAGQHL PIRVTLPGAA TPAVRTYTLS VAPSDHIYRI SVKRDGAVSR HLHDHVRAGD
     VIEARAPAGT FTIDARQNRP AVLLAGGVGI TPMLAMLRHI VYEGLRKHRV RPAILFQAAR
     SKADRAFDAE LSELVAAAKG AVRIVRVLSD TTGAEEGRDY DAAGRIDMTL LTRFLSFNDY
     DFYLCGPPAF SQALYDGLRS YGVADGRIHA ESFGPSSLAR TADTGLAAPP PRPAATTPVP
     VAFLRSLKEA RWTPRAGTLL ELAEARGLQP EFGCRTGSCG TCRTKLLKGS VAYVRMPTAD
     VADDEVLICC AVPARQDTGE ETPIHLAL
//