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Database: UniProt
Entry: Q6WB80_ALCFA
LinkDB: Q6WB80_ALCFA
Original site: Q6WB80_ALCFA 
ID   Q6WB80_ALCFA            Unreviewed;       333 AA.
AC   Q6WB80;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Putative naphthalene 1,2-dioxygenase system ferredoxin-NAD(+) reductase {ECO:0000313|EMBL:AAQ19820.1};
OS   Alcaligenes faecalis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511 {ECO:0000313|EMBL:AAQ19820.1};
RN   [1] {ECO:0000313|EMBL:AAQ19820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCIB 8687 {ECO:0000313|EMBL:AAQ19820.1};
RA   Silver S., Phung L.T., Malo B.J.;
RT   "Genes for Arsenite Oxidation from Alcaligenes faecalis.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; AY297781; AAQ19820.1; -; Genomic_DNA.
DR   RefSeq; WP_003804033.1; NZ_CP123895.1.
DR   AlphaFoldDB; Q6WB80; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06187; O2ase_reductase_like; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 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; 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   Dioxygenase {ECO:0000313|EMBL:AAQ19820.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:AAQ19820.1}.
FT   DOMAIN          2..94
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          102..201
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   333 AA;  36197 MW;  2D376D715EC854C3 CRC64;
     MSSKTIIIRQ TGTQFDAQEG QNILQAALEN GIVYPYGCRQ GRCGGCKTRL VQGQVDLLDY
     SRFALTEAQS ARGLILACRA IPRSDVTLDW IGTDDVRGRV PLRQVEGTVV TLEALTHDIR
     RVRIRLADEQ PLMFFAGQYA DIKFGQAPAR SYCMANRPGE AELEFHIRRV PGGVASAYVH
     TVLEPGERVT LELPKGTSYL REGHGGPMLC IAGGAGLAPI KSIVETALAS GMSQAIHVYF
     GVREGRDLYG LEEFRALARD YPTLLFTPVV SGIPVAHCSR GLVTDIAGSE QADLRGWKVY
     VAGSPTLVDA TIGMALKRGL KIQDLHAQIY VTP
//
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