LeishBase: Leishmania Structural Database
header
Home List of Proteins How to Visualize Structures Download Contact Us
Citrate synthase, putative [Q4QDX3]
Systematic NameLmjF.18.0680 [Leishmania major]
Gene NameLmjF18.0680
Molecular Weight52329 Da
Protein Sequence Size470
Function
Charge5
Isoelectric Point7.1929 pH
DescriptionCitrate synthase, putative (EC 2.3.3.1).
Subcellular Locationcytoplasm[Predict]
E. C. Number 2.3.3.1
Sequence>tr|Q4QDX3|Q4QDX3_LEIMA Citrate synthase, putative (EC 2.3.3.1) - Leishmania major.
RAVRCSLIRGVAGLRMASSALDEMKEQMLRRWKEDQKKIDDLRKKHGHEKLCDATIDAVY
GGMRGITGLVYEPSLLDPAEGIRFRGLTILECQEMLPKAPGGKEPLPEAMFWLLMTGEVP
TEEQVRGLNAELHRRADPEAIAAAQKAIAALPRNAHPMTAFSVGVLALQSYSKFAAAYAA
GKSNKKTYWEYALEDSLDMLARTPTVAAMIYNRETKGQVELAAPSNSDLDWAANFAKMMG
YQDEEFWECMRLYLSVHADHEGGNVSAHTTTLVASALSDPYLAFSAGLNGLAGPLHGLAN
QEVLNYLLSMQERVKADGVNMHDEAALEKALSNYTWELLNSGQVVPGYGHAVLRKVDPRY
TCQRNFCLRHKFDDDLFKLVNTIYSIMPGILKEHGKTKNPYPNVDAHSGVLLQHYGLTEQ
NYYTVLFGLSRQMGVLAGVVWDRLQGRPLERPKSITTEMLAKKYLCNSL
DNA Sequence>LmjF18.0680 |||citrate synthase, putative|Leishmania major|chr 18|||Manual
ATGCGCGCTG TTCGCTGCTC CCTAATTCGC GGCGTCGCCG GTCTCCGCAT GGCGTCATCGGCATTGGATG AGATGAAGGA GCAGATGCTG AGGCGCTGGA AAGAGGACCA GAAGAAGATCGACGACCTCA GGAAGAAGCA CGGCCATGAG AAGCTGTGCG ACGCGACCAT CGATGCGGTGTACGGCGGCA TGCGCGGCAT CACCGGCCTC GTGTACGAGC CATCACTGCT GGACCCCGCAGAGGGCATCC GCTTCCGCGG CCTCACGATC CTGGAGTGCC AGGAGATGCT GCCCAAAGCGCCGGGCGGCA AGGAGCCGCT GCCGGAGGCG ATGTTCTGGC TACTGATGAC CGGCGAGGTGCCGACGGAGG AGCAGGTAAG GGGCCTGAAC GCGGAGCTGC ACCGTCGCGC CGACCCCGAGGCGATTGCCG CGGCGCAGAA GGCGATCGCG GCGCTGCCGA GGAACGCGCA CCCGATGACGGCATTCAGTG TGGGCGTGCT TGCGCTGCAG AGCTACTCGA AGTTTGCTGC GGCTTACGCGGCGGGCAAGT CGAACAAGAA GACGTACTGG GAGTACGCGC TGGAGGACTC GCTGGACATGCTGGCGCGCA CGCCGACGGT GGCGGCGATG ATCTACAACC GCGAGACCAA GGGCCAGGTGGAGTTGGCGG CACCGAGCAA CAGCGACCTG GACTGGGCGG CGAACTTTGC GAAAATGATGGGCTACCAGG ACGAGGAGTT CTGGGAGTGC ATGCGTCTGT ACCTGTCTGT CCACGCCGACCACGAGGGTG GAAACGTGTC GGCACACACA ACGACACTGG TTGCGTCAGC ACTGAGCGACCCCTACCTCG CCTTCAGCGC TGGCCTGAAC GGTCTTGCTG GCCCGCTGCA TGGGCTGGCGAACCAGGAGG TGCTGAATTA CTTGCTCAGC ATGCAGGAGC GTGTGAAGGC GGATGGCGTGAACATGCATG ATGAGGCAGC GCTCGAGAAG GCGCTGAGCA ACTACACGTG GGAGTTGCTCAACTCCGGCC AGGTGGTGCC CGGCTACGGC CACGCGGTGC TGCGCAAGGT GGACCCGCGCTACACCTGCC AGCGCAACTT CTGCCTGCGC CACAAATTTG ATGACGACCT GTTCAAGCTGGTCAACACCA TCTACTCGAT CATGCCCGGC ATCCTGAAGG AGCACGGTAA GACCAAGAACCCCTACCCCA ACGTCGACGC GCACTCCGGC GTGCTACTGC AGCACTACGG GCTGACGGAGCAGAACTACT ACACGGTGCT GTTCGGCCTG TCGCGCCAGA TGGGCGTCTT GGCCGGCGTCGTCTGGGACC GCCTGCAGGG CCGCCCGCTC GAGCGCCCGA AGTCGATCAC GACGGAGATGCTCGCAAAGA AATACCTGTG CAACTCCTTG TGA
Citrate synthase, putative Q4QDX3]
Metabolite Information
Molecular Functioncitrate (Si)-synthase activity; transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Biochemical Pathwaymain pathways of carbohydrate metabolism; tricarboxylic acid cycle
Regulatory Pathway
KEGG PathwaysK01647
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapienscitrate synthase precursor, isoform a [Homo sapiens]551e-137484
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
HP0775 penta-phosphate guanosine-3'-pyrophosphohydrolase (spoT)Helicobacter pylori23%0.5130
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00017ATP/GTP-binding site motif A (P-loop)177-184; PS00017
PDOC00422Citrate synthase signature348-360; PS00480
PDOC00015The rule PS00015 has been deleted from the PROSITE database and replaced by the following motif: PS50079 (Bipartite nuclear localization signal profile31-47; PS00015
AcylationN-myristoylation site14-19; 62-67; 263-268; 264-269; 435-440; PS00008
GlycosylationN-glycosylation site265-268; 334-337; PS00001
PhosphorylationCasein kinase II phosphorylation site20-23; 75-78; 89-92; 188-191; 226-229; 228-231; 310-313; PS00006
PhosphorylationProtein kinase C phosphorylation site184-186; PS00005
PhosphorylationTyrosine kinase phosphorylation site355-361; PS00007
SulfationTyrosine sulfation site185-199; 235-249; PS00003
Citrate synthase, putative [Q4QDX3]
Model Information
Template PDB ID2ctsA
Percent Identity56%
Target Region20-470
Template Region1-437
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
SER248Sidechain
HIS278Sidechain
HIS332Sidechain
ASP387Sidechain
Co-Factor
Metal Description
Ligands
CAS number Name Mol. Weight Mol. Formula Smile Notation PDB Reference
5949-29-1CITRIC ACID192.124C6 H8 O7O=C(O)CC(O)(C(=O)O)CC(=O)O2cts
31416-98-5COENZYME A767.534C21 H36 N7 O16 P3 SO=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O2cts
Mutational Information
Residue Feature Description
Modeled Protein Template Structure
+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/1388340/Q4QDX3.pdb 2.0 450 = residues | | = | *| Ramachandran plot: 94.6% core 4.6% allow 0.5% gener 0.3% = disall | | = | +| All Ramachandrans: 9 labelled residues (out of 444) = | +| Chi1-chi2 plots: 4 labelled residues (out of 259) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 6.6 Bad contacts: = 6 | *| Bond len/angle: 7.2 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.08 Covalent: -0.16 Overall: = -0.01 | | = | | M/c bond lengths: 98.9% within limits 1.1% highlighted = | | M/c bond angles: 93.4% within limits 6.6% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database