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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR632 IGR635 IGR636 IGR633 IGR637 IGR638 IGR634 ipyR, - CT772 CT774 CT767 CT769 CT771 CT775 miaA, - CT766 ldh,dhlE, - CT773 fabF, - CT770 CT768 ipyR, - CT772 CT774 CT767 CT769 CT771 CT775 miaA, - CT766 ldh,dhlE, - CT773 fabF, - CT770 CT768 ipyR, - CT772 CT774 CT767 CT769 CT771 CT775 miaA, - CT766 ldh,dhlE, - CT773 fabF, - CT770 CT768
* Calculated from Protein Sequence

Gene ID: CT770

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fabF  

Definition:
beta-ketoacyl-ACP synthase

Gene Start:
903954

Gene Stop:
905207

Gene Length:
1254

Molecular Weight*:
44807

pI*:
5.36

Net Charge*:
-8.48

EC:
2.3.1.41  

Functional Class:
fatty acid and phospholipid metabolism  

Pathway: pathway table
Lipid Metabolism; Fatty acid biosynthesis

Secondary Evidence:
Kutchma,A.J., Hoang,T.T. and Schweizer,H.P. Molecular characterization of the acpP-containing region of the Pseudomonas aeruginosa chromosome. Unpublished.

Comment:
In E. coli, the FabB protein catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP. See CT237, CT238, and CT239. See also CT426, CT104, and CT532.



Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to beta-ketoacyl-ACP synthase sequences, some from plants:
residues 3-416 are 56% similar to 1) L13242 from Ricinus communis, 2) AF026148 from Perilla frutescens
3) FABB_ARATH.

CT770 is orthologous to CPn0916: residues 1-416 are 86% similar to CPn0916. This protein is also similar to PG1538, a predicted beta-ketoacyl-ACP synthase from Porphyromonas gingivalis. No similarities to T.pallidum or M.genitalium.

COGS Summary:  COGS Search
BeTs to 10 clades of COG0304
COG name: 3-oxoacyl-(acyl-carrier-protein) synthase I
Functional Class:  I
The phylogenetic pattern of COG0304 is ----YqvCEBRhuj----inx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 156-191 are matched to block BL00606, concerned with beta-ketoacyl synthase sequences,
e.g. FABB_HORVU. Residues 101-114, 227-240 are matched to block BL01240A,
concerned with purine and other phosphorylases family 2 proteins,
e.g. PNPH_BOVIN. Residues 160-191, 271-313, 330-355, 338-351 are matched
to blocks BL00098A,D,E,F, concerned with thiolases acyl-enzyme intermediate proteins,
e.g. THIL_HUMAN, THIM_RAT, YKA3_CAEEL. Residues 107-116 and 176-202 are
weakly matched to blocks BL00923A,E, which encompass aspartate and glutamate racemases,
e.g. MURI_BACSU.

ProDom Summary:  Protein Domain Search
Residues 222-369 are 61% similar to a polyketide synthase domain of FABB_ARATH.
Residues 4-112, 7-69, 70-124, 97-110, 164-217, 372-416
are supportive of this relationship through similarities to
FABB_HORVU, FABB_HAEIN, FABB_ARATH.

Paralogs:  Local Blast Search
No evidence of paralogs in C.trachomatis.

Pfam Summary:  Pfam Search
Residues 4 to 248 (E-value = 2.1e-86) place CT770 in the ketoacyl-synt family which is described as Beta-ketoacyl synthase, N-terminal domain (PF00109)
Residues 256 to 415 (E-value = 1.8e-67) place CT770 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain (PF02801)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
134  
155

PDB Hit:
None.

Gene Protein Sequence:
MNKKRVVVTGMGIVSCLGNEVESFYDSLLAGISGVRTITSFPCDDYATRF
AGWIEEFNSEPYLDKKQARRVDPFITYAVVAAKKAIAMSRWDQDTLPADS
HRCGVIIGSGMGGLRTLDEGIEKLSAGNRKLSPFFIPYIITNMAPALIAM
DYGLMGPNYSISTACATANYCIDAAYQHLIEGRADVIVCGGTEAAINRVG
LAGFIANRALSERNDAPEQASRPWDRDRDGFVLGEGAGILVLETLDNALK
RGAPIFAEVLGTYTTCDAFHITAPRDDGEGITACILGALNKAGIPKERVN
YINAHGTSTPLGDLSEVLALKKAFGSHVKNLRMNSTKSLIGHCLGAAGGV
EAVATIQAIQTGKLHPTINVENPIAEIEEFDVVANKAQDWDVDVAMSNSF
GFGGHNSTILFSRYEPSL

Gene Nucleotide Sequence:  Sequence Viewer
ATGAACAAAAAACGTGTAGTCGTTACAGGAATGGGGATCGTCTCCTGCCT
TGGGAATGAAGTAGAATCTTTCTATGATAGCCTATTGGCGGGAATTAGTG
GAGTGCGAACAATCACGTCTTTTCCCTGCGATGATTATGCTACGCGTTTT
GCTGGCTGGATAGAAGAATTTAACTCAGAGCCTTACTTAGATAAAAAACA
AGCTAGACGAGTTGATCCTTTTATTACTTATGCAGTTGTAGCTGCAAAGA
AGGCAATAGCTATGTCCCGTTGGGATCAAGATACTCTTCCCGCAGATTCT
CATCGTTGTGGGGTGATTATTGGTTCTGGAATGGGAGGATTACGAACCCT
GGATGAGGGGATTGAAAAACTATCGGCTGGAAATAGAAAATTATCTCCAT
TCTTTATTCCTTACATCATTACGAATATGGCTCCGGCTTTAATCGCAATG
GATTATGGGTTAATGGGACCTAATTATTCTATTTCAACAGCCTGTGCAAC
AGCAAACTACTGTATTGATGCCGCTTATCAACACCTCATTGAGGGTCGAG
CAGATGTTATCGTTTGTGGAGGAACTGAAGCGGCTATTAACCGTGTTGGT
TTAGCTGGATTTATTGCGAATCGCGCATTGTCAGAAAGAAATGATGCTCC
AGAACAAGCTTCGCGCCCTTGGGATAGGGATCGAGACGGTTTTGTTTTGG
GGGAGGGTGCAGGAATTCTTGTTTTGGAAACCCTTGATAATGCTTTGAAA
AGAGGGGCTCCGATTTTTGCGGAGGTACTTGGCACATATACAACGTGCGA
TGCTTTTCATATTACTGCTCCTAGAGATGATGGCGAAGGAATCACTGCCT
GTATATTGGGAGCCTTGAATAAGGCTGGGATTCCTAAAGAACGGGTGAAT
TATATTAATGCACACGGAACGTCGACGCCTCTAGGGGATCTATCAGAGGT
ATTGGCTTTGAAGAAAGCTTTTGGAAGCCACGTCAAAAACTTGCGAATGA
ATTCAACGAAGTCGTTGATAGGGCACTGCTTGGGAGCTGCAGGAGGAGTA
GAAGCTGTTGCAACCATTCAAGCCATCCAGACTGGGAAGTTGCACCCAAC
AATCAATGTAGAAAATCCGATAGCAGAAATAGAAGAATTCGATGTGGTTG
CGAACAAAGCTCAAGATTGGGATGTCGATGTAGCTATGTCAAATTCTTTT
GGTTTTGGCGGACACAATTCAACGATATTATTTTCGAGGTATGAACCTTC
ATTA


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