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BupsA.00010.b: enoyl-(acyl carrier protein) reductase

Target Characteristics

from organism: Burkholderia pseudomallei 1710b
most recent status: in PDB
center reference id: BupsA.00010.b
is community request: True
associated disease: Melioidosis
NIH risk group: 3
is select agent: True
NIH priority
pathogens category:
IIIB

Ordering Clones & Proteins

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Proteins

CENTER
REFERENCE ID
DOMAIN/REGION
DESCRIPTION
INFO AA
START
AA
STOP
ORDER
MATERIAL
BupsA.00010.b.B1.PS00034 Full length( BupsA.00010.b ) 1 263

Structures

image of structure for 3EK2
3EK2
Deposited: 9/18/2008
Determination: XRay
Diffraction Image
Clone: BupsA.00010.b.B1.GE25083
Protein: BupsA.00010.b.B1.PS00034
image of structure for 5TRT
5TRT
Deposited: 10/27/2016
Determination: XRay
Diffraction Image
Clone: BupsA.00010.b.B1.GE25083
Protein: BupsA.00010.b.B1.PS00034

Publications by SSGCID

Combining functional and structural genomics to sample the essential Burkholderia structome.
Abendroth J, Armour B, Barrett L, Baugh L, Begley DW, Buchko GW, Choi R, Clifton MC, Dieterich SH, Dranow DM, Edwards TE, Fairman JW, Fox D, Gallagher LA, Gardberg AS, Gillespie A, Manoil C, Myler PJ, Nakazawa-Hewitt S, Napuli A, Nguyen MT, Patrapuvich R, Phan I, Stacy R, Staker BL, Stewart LJ, Van Voorhis WC
PLoS ONE - 2012
volume 8, issue 1, pages e53851
PMID: 23382856; PMCID: PMC3561365

Citations by Others

Rational Optimization of Diphenyl Ether Binding Kinetics to the Enoyl-ACP Reductase FabI1 from Burkholderia pseudomallei
C Neckles, S Eltschkner, JE Cummings- Biochemistry, 2017 - ncbi.nlm.nih.gov
PDB: 3EK2
Crystalline Structure of FABI from Burkholderia Pseudomallei
NR Krishnamurthy - US Patent , 2017 - freepatentsonline.com
PDB: 3EK2
Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase
C Neckles, S Eltschkner, JE Cummings - Biochemistry, 2017 - ACS Publications
PDB: 3EK2
Pyridone FabI Inhibitors and Uses Thereof
P Tonge - US Patent App. 15/130,365, 2016 - Google Patents
PDB: 3EK2
Rare Sidechain Conformations in Proteins and DNA
BJ Hintze - 2015 - search.proquest.com
PDB: 3EK2
Rational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (ACP) Reductase Inhibitor
J Schiebel, A Chang, S Shah, Y Lu, L Liu, P Pan - Journal of Biological Chemistry, 2014 - ASBMB
cited by: 13 others
PDB: 3EK2
Paclitaxel Induces Apoptosis in Breast Cancer Cells through Different Calcium-Regulating Mechanisms Depending on External Calcium Conditions
Z Pan, A Avila, L Gollahon - International journal of molecular sciences, 2014 - mdpi.com
PDB: 3EK2
< i> Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality
J Schiebel, A Chang, H Lu, MV Baxter, PJ Tonge? - Structure, 2012 - Elsevier
cited by: 33 others
PDB: 3EK2
High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD+ and in complex with NAD+ and triclosan
JM Otero, AJ Noel, P Guardado-Calvo? - Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2012 - scripts.iucr.org
cited by: 2 others
PDB: 3EK2
Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP and triclosan
A Priyadarshi, EEK Kim? - Proteins: Structure, Function, and Bioinformatics, 2010 - Wiley Online Library
cited by: 23 others
PDB: 3EK2

This list was obtained from Google Scholar searches using the Open Source tool https://github.com/ckreibich/scholar.py and each citation has been manually reviewed.

External Resources

Resource Reference ID
OrthoMCL: OG5_130466
PATRIC ID: fig|320372.6.peg.2759
RefSeq: YP_334023
UniProt: Q3JQY0

Enzyme & Pathway Information

Pathway Pathway ID EC Number
biotin biosynthesis I BIOTIN-BIOSYNTHESIS-PWY 1.3.1.9
fatty acid elongation -- saturated FASYN-ELONG-PWY 1.3.1.9
(5Z)-dodecenoate biosynthesis I PWY0-862 1.3.1.9
superpathway of fatty acid biosynthesis I (E. coli) PWY0-881 1.3.1.9
superpathway of fatty acid biosynthesis II (plant) PWY-5156 1.3.1.9
palmitate biosynthesis II (bacteria and plants) PWY-5971 1.3.1.9
cis-vaccenate biosynthesis PWY-5973 1.3.1.9
stearate biosynthesis II (bacteria and plants) PWY-5989 1.3.1.9
superpathway of mycolate biosynthesis PWY-6113 1.3.1.9
palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate) PWY-6282 1.3.1.9
superpathway of unsaturated fatty acids biosynthesis (E. coli) PWY-6284 1.3.1.9
superpathway of fatty acids biosynthesis (E. coli) PWY-6285 1.3.1.9
8-amino-7-oxononanoate biosynthesis I PWY-6519 1.3.1.9
triclosan resistance PWY-7096 1.3.1.9
gondoate biosynthesis (anaerobic) PWY-7663 1.3.1.9
oleate biosynthesis IV (anaerobic) PWY-7664 1.3.1.9
(5Z)-dodecenoate biosynthesis II PWY-7858 1.3.1.9
mycolate biosynthesis PWYG-321 1.3.1.9

Sequences

These sequences are the native gene sequence; sequences of constructs derived from these sequences may differ due to codon optimization or other protocols. To find the specific sequence of any material you may have ordered, click on the "more" button next to the name of that material.
AA Sequence
MGFLDGKRIL LTGLLSNRSI AYGIAKACKR EGAELAFTYV GDRFKDRITE FAAEFGSELV FPCDVADDAQ IDALFASLKT HWDSLDGLVH SIGFAPREAI AGDFLDGLTR ENFRIAHDIS AYSFPALAKA ALPMLSDDAS LLTLSYLGAE RAIPNYNTMG LAKAALEASV RYLAVSLGAK GVRVNAISAG PIKTLAASGI KSFGKILDFV ESNSPLKRNV TIEQVGNAGA FLLSDLASGV TAEVMHVDSG FNAVVGGMAG LEE

NT Sequence
ATGGGCTTTC TCGACGGTAA ACGTATTCTG CTGACGGGCC TCTTGTCGAA CCGTTCGATC GCTTACGGCA TCGCCAAGGC GTGCAAGCGC GAAGGCGCCG AGCTGGCGTT CACCTACGTC GGCGATCGCT TCAAGGATCG CATCACCGAG TTCGCGGCCG AGTTCGGCAG CGAACTCGTG TTCCCGTGCG ATGTCGCCGA CGATGCGCAG ATCGATGCGC TCTTCGCGTC GCTGAAGACG CACTGGGATT CGCTCGACGG CCTCGTCCAC TCGATCGGCT TCGCGCCGCG CGAGGCGATC GCGGGCGACT TCCTCGACGG CCTCACGCGC GAGAACTTCC GCATCGCGCA CGACATCTCC GCATACAGCT TCCCCGCGCT CGCGAAGGCG GCGCTGCCGA TGCTGTCGGA CGATGCGTCG CTGCTCACGC TGTCGTATCT CGGCGCGGAG CGGGCGATCC CGAACTACAA CACGATGGGC CTCGCGAAGG CGGCGCTCGA GGCGAGCGTG CGCTATCTCG CGGTGTCGCT CGGCGCGAAG GGCGTGCGCG TGAACGCGAT CTCGGCGGGC CCGATCAAGA CGCTCGCGGC AAGCGGCATC AAGAGCTTCG GCAAGATCCT CGATTTCGTC GAGAGCAACT CGCCGCTCAA GCGCAACGTG ACGATCGAGC AGGTCGGCAA CGCGGGCGCG TTCCTGCTGT CGGACCTCGC GAGCGGCGTC ACGGCCGAAG TCATGCACGT CGACTCGGGC TTCAACGCGG TGGTGGGCGG GATGGCCGGC CTCGAGGAA

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