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Database: UniProt
Entry: F7T0G6_9BURK
LinkDB: F7T0G6_9BURK
Original site: F7T0G6_9BURK 
ID   F7T0G6_9BURK            Unreviewed;       338 AA.
AC   F7T0G6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=2Fe-2S iron-sulfur cluster binding domain-containing protein 3 {ECO:0000313|EMBL:EGP46255.1};
GN   ORFNames=AXXA_12140 {ECO:0000313|EMBL:EGP46255.1};
OS   Achromobacter insuavis AXX-A.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP46255.1};
RN   [1] {ECO:0000313|EMBL:EGP46255.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AXX-A {ECO:0000313|EMBL:EGP46255.1};
RA   Bador J., Amoureux L., Neuwirth C.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EGP46255.1}.
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DR   EMBL; AFRQ01000042; EGP46255.1; -; Genomic_DNA.
DR   RefSeq; WP_006392458.1; NZ_GL982453.1.
DR   AlphaFoldDB; F7T0G6; -.
DR   PATRIC; fig|1003200.3.peg.2405; -.
DR   eggNOG; COG0543; Bacteria.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_003827_7_0_4; -.
DR   OrthoDB; 9806195at2; -.
DR   Proteomes; UP000004853; Unassembled WGS sequence.
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; cd06189; flavin_oxioreductase; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; PR00371; FPNCR.
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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT   DOMAIN          3..92
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          97..196
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   338 AA;  36553 MW;  4D108C98FE163E1D CRC64;
     MAYRVHLLET GQSFEAEAGE SVLAAAERAA VRLPHECTFG GCGTCRIKLA EGTVAYDEFP
     MALTPEEAAQ GYALACQARP CADLTISVAN TRQFAEPRRL DATVHRIAAL CDDVTHLTLA
     LPPDAPLDYA PGQYMNVVLP DGATRSFSMA SAPAGNLVDF HVRRIPGGRY TDHWLGQARP
     GAALEIEAPL GVFSYHEEDW RPMIMMATGT GIAPIKAILE SLLDNDDCPP VTLYWGMRTE
     ADLYLRDQIA GWAGRLYEFN FVPVLSRADA GWQGRRGHVQ QAVLQDHGDL SEHALYLCGA
     PAMISEATAL LAGRGASLDH VYADSFTFQH APATAAMP
//
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