ID Q2T230_BURTA Unreviewed; 271 AA.
AC Q2T230;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN OrderedLocusNames=BTH_I0211 {ECO:0000313|EMBL:ABC38486.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38486.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC38486.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2] {ECO:0007829|PDB:4F7D, ECO:0007829|PDB:4FK8}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=23382856; DOI=10.1371/journal.pone.0053851;
RA Baugh L., Gallagher L.A., Patrapuvich R., Clifton M.C., Gardberg A.S.,
RA Edwards T.E., Armour B., Begley D.W., Dieterich S.H., Dranow D.M.,
RA Abendroth J., Fairman J.W., Fox D., Staker B.L., Phan I., Gillespie A.,
RA Choi R., Nakazawa-Hewitt S., Nguyen M.T., Napuli A., Barrett L.,
RA Buchko G.W., Stacy R., Myler P.J., Stewart L.J., Manoil C.,
RA Van Voorhis W.C.;
RT "Combining functional and structural genomics to sample the essential
RT Burkholderia structome.";
RL PLoS ONE 8:E53851-E53851(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000086; ABC38486.1; -; Genomic_DNA.
DR PDB; 4F7D; X-ray; 2.35 A; A/B=1-271.
DR PDB; 4FK8; X-ray; 2.10 A; A/B=1-271.
DR PDBsum; 4F7D; -.
DR PDBsum; 4FK8; -.
DR AlphaFoldDB; Q2T230; -.
DR SMR; Q2T230; -.
DR KEGG; bte:BTH_I0211; -.
DR HOGENOM; CLU_003827_3_0_4; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd06195; FNR1; 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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR033892; FNR_bac.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47878:SF1; FERREDOXIN--NADP(+) REDUCTASE; 1.
DR PANTHER; PTHR47878; OXIDOREDUCTASE FAD/NAD(P)-BINDING DOMAIN PROTEIN; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4F7D, ECO:0007829|PDB:4FK8};
KW FAD {ECO:0007829|PDB:4FK8}; Flavoprotein {ECO:0007829|PDB:4FK8};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0007829|PDB:4FK8}.
FT DOMAIN 17..117
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
FT BINDING 270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:4FK8"
SQ SEQUENCE 271 AA; 30424 MW; 4ED32642910285DD CRC64;
MGPLWGPLYA PVSESMSKFD TATVLSVHHW TDTLFSFTCT RDQALRFNNG EFTMVGLEVD
GKPLTRAYSI VSPNYEEHLE FFSIKVQNGP LTSRLQHLKV GDPVLIGKKP TGTLVADNLL
PGKTLWMLST GTGLAPFMSI IRDPDIYERF DKVVLTHTCR LKGELAYMDY IKHDLPGHEY
LGDVIREKLV YYPTVTREEF ENEGRITDLI ASGKLFTDLD MPPFSPEQDR VMLCGSTAML
KDTTELLKKA GLVEGKNSAP GHYVIERAFV D
//
