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
//