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Database: UniProt
Entry: Q3JV40_BURP1
LinkDB: Q3JV40_BURP1
Original site: Q3JV40_BURP1 
ID   Q3JV40_BURP1            Unreviewed;       343 AA.
AC   Q3JV40;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehy drase reductase {ECO:0000313|EMBL:ABA49995.1};
GN   Name=ascD {ECO:0000313|EMBL:ABA49995.1};
GN   OrderedLocusNames=BURPS1710b_1151 {ECO:0000313|EMBL:ABA49995.1};
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA49995.1, ECO:0000313|Proteomes:UP000002700};
RN   [1] {ECO:0000313|EMBL:ABA49995.1, ECO:0000313|Proteomes:UP000002700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b {ECO:0000313|EMBL:ABA49995.1,
RC   ECO:0000313|Proteomes:UP000002700};
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) 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; CP000124; ABA49995.1; -; Genomic_DNA.
DR   RefSeq; WP_004185343.1; NC_007434.1.
DR   AlphaFoldDB; Q3JV40; -.
DR   EnsemblBacteria; ABA49995; ABA49995; BURPS1710b_1151.
DR   GeneID; 56595017; -.
DR   KEGG; bpm:BURPS1710b_1151; -.
DR   HOGENOM; CLU_003827_7_0_4; -.
DR   Proteomes; UP000002700; Chromosome I.
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..93
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          100..200
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   343 AA;  38012 MW;  B75151DE98B61B4A CRC64;
     MAFNVTLKQS GRQFQVEADE TVLAAALRQN VHLPYGCKNG ACGSCKGTIV QGQFEQGPHS
     ASALSNDERT RGLALLCCSK PQSDLEVDVR EIAGVDGVQV KKLPCRVAAL ERRADDVIVL
     KLQLPANERL QYLAGQYIEF ILKDGARRSY SMATAPHEEG PIELHIRHMP GGKFTDHVFG
     PMKERDILRF EGPLGTFFLR EDSDKPIVLL ASGTGFAPIK AIIEHAHHVK LERPMTLYWG
     ARRKKDLYLL DAAEQWAKEI PNFKFVPVLS EPDASDAWTG RTGFVHRAVI EDLPDLSGHQ
     VYACGAPVMV ESAQRDFTQH HRLPADEFYA DSFTSAADLA HTV
//
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