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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Pro-1 IGR44 IGR46 IGR45 IGR48 IGR47 IGR49 IGR43 fer, - CT059 CT056 CT058 hemN, - CT052 CT057 sucB, - CT055 flhA, - CT060 sucA, - CT054 fer, - CT059 CT056 CT058 hemN, - CT052 CT057 sucB, - CT055 flhA, - CT060 sucA, - CT054 fer, - CT059 CT056 CT058 hemN, - CT052 CT057 CT053 CT053 sucB, - CT055 flhA, - CT060 sucA, - CT054
* Calculated from Protein Sequence

Gene ID: CT055

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sucB  

Definition:
dihydrolipoamide succinyltransferase (pyruvate dehydrogenase component E2)

Gene Start:
63599

Gene Stop:
64693

Gene Length:
1095

Molecular Weight*:
40332

pI*:
4.93

Net Charge*:
-13.13

EC:
2.3.1.61  

Functional Class:
central intermediary metabolism; TCA cycle  

Pathway: pathway table
Carbohydrate Metabolism; Citrate cycle (TCA cycle)

Secondary Evidence:
Westphal,A.H. and de Kok,A. 1990. The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component. Eur. J. Biochem. 187(1): 235-239. Medline: 90126825.

Carlsson,P. and Hederstedt,L. 1989. Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively.
J. Bacteriol. 171(7): 3667-3672. Medline: 89291708

Comment:
In H. influenzae, the ODO2 enzyme converts 2-oxoglutarate to succinyl-CoA + CO2. The E2 component of this complex (also called the pyruvate dehydrogenase complex) is a dihydrolipoamide succinyltransferase. See paralogs CT400 and CT247. See also CT054, CT245, CT246, and CT557.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to dihydrolipoamide succinyltransferase sequences e.g., residues 4-353 are 44% similar to ODO2_BACSU.

CT055 is orthologously related to CPn0377: residues 1-365 are 69% similar to CPn0377, a predicted dihydrolipoamide succinyltransferase (sucB). CT055 is similar to MG272, a predicted dihydrolipoamide acetyltransferase in M. genitalium. No similarity to T. pallidum.

COGS Summary:  COGS Search
BeTs to 8 clades of COG0508
COG name: Dihydrolipoamide acyltransferases
Functional Class:  C
The phylogenetic pattern of COG0508 is ----Y--cEBRH--gp--INX
Number of proteins in this genome belonging to this COG is 3


Blocks Summary:  Blocks Search
Residues 25-59, 58-95, 200-216, 229-243, 279-307, and 336-346 correspond to blocks BL00189A,B,C,D,E, concerned with 2-oxo acid dehydrogenases, acyltransferase component represented by ODP2_AZOWI, ODO2_BACSU and ODO2_AZOWI.
Residues 342-354 are matched to block PR00819E, concerned with
cbxX/cfqX superfamily signature, e.g. BCSP5KGEN.

ProDom Summary:  Protein Domain Search
Residues 149-353 are 57% similar to E2 complex dehydrogenase sequences, as represented by ODO2_HAEIN.

Paralogs:  Local Blast Search
CT055 is paralogously related to CT400(dihydrolipoamide succinyltransferase) and CT247(dihydrolipoamide aetyltransferase humanish but is it horizontal transfer?). Residues 4-357 are 30% similar to CT400, residues 140-363 are 34% similar to CT247.

Pfam Summary:  Pfam Search
Residues 3 to 75 (E-value = 3e-13) place CT055 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 134 to 364 (E-value = 4.1e-133) place CT055 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

PDB Hit:
gi|1064952|pdb|1DPC| Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Mutant With Asn 614 Replaced By Asp (N614d)

Gene Protein Sequence:
MSIEVRIPNIAESISEVTISALLIPSGDLVQENQGILEIESDKVNQLIYA
PCSGRVEWSVSVGDTVAVGSVVGIISEAEKSQDTAPIHEQMPFSLVEQES
DAQIIAFPSSVRQDPPAEGKTFVPLKEIQPASSDHRESRESMSAIRKTIS
RRLVQSLHDSAMLTTFNEIHMGPLIALRKERQEDFVAKYGVKLGFMSFFV
RAVVDSLKKYPRVNAYIEDNEIVYRHYYDISIAIGTDRGLVVPVIRNCDQ
LSSGEIELQLADLASRAREGKLAIHELEGGGFTITNGGVYGSLLSTPIIN
PPQVGILGMHKIEKRPVVREDAIVIADMMYVAMSYDHRIIDGKEAVGFLV
NVKEQLEQPELLLKM

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTATAGAGGTTCGTATTCCCAATATCGCAGAATCTATTAGTGAAGT
GACGATTTCTGCACTTTTGATTCCATCAGGAGATTTGGTGCAGGAGAATC
AAGGGATTCTGGAGATAGAGAGTGACAAGGTGAATCAGCTCATTTACGCT
CCTTGCTCAGGAAGGGTAGAGTGGAGCGTTTCCGTAGGGGATACGGTCGC
TGTTGGTAGTGTTGTAGGGATTATTAGTGAAGCGGAAAAGAGTCAAGATA
CTGCACCTATCCATGAGCAGATGCCATTTAGTCTTGTAGAGCAGGAAAGC
GATGCGCAGATTATTGCCTTCCCTTCATCAGTGAGACAGGATCCTCCTGC
AGAAGGGAAAACTTTTGTTCCATTAAAGGAGATCCAACCAGCTTCTTCTG
ATCATAGAGAATCTCGAGAATCTATGAGTGCTATTCGGAAGACGATTTCT
CGTAGATTGGTGCAATCTCTACATGATTCAGCAATGTTAACGACATTTAA
TGAAATCCATATGGGGCCGCTTATTGCTCTGCGTAAGGAAAGACAAGAAG
ATTTCGTTGCGAAGTATGGGGTAAAACTTGGGTTCATGTCTTTCTTTGTT
AGAGCCGTTGTAGATTCTTTGAAAAAATATCCCCGGGTGAATGCTTATAT
TGAAGATAACGAAATCGTTTACAGACATTACTACGATATTTCCATTGCCA
TAGGGACAGATCGTGGATTAGTAGTTCCTGTAATTCGTAATTGTGATCAG
TTATCTAGCGGGGAGATTGAGTTACAGCTTGCCGATTTAGCTTCTCGTGC
TCGGGAAGGCAAACTTGCTATTCATGAGTTAGAAGGGGGAGGCTTCACTA
TTACCAATGGAGGGGTATATGGTTCTCTTCTATCCACTCCCATTATCAAT
CCTCCACAGGTAGGTATTCTTGGGATGCATAAGATAGAGAAACGCCCTGT
GGTTAGAGAAGATGCAATTGTGATAGCCGATATGATGTATGTAGCTATGA
GCTATGATCATCGGATTATAGACGGAAAGGAAGCCGTAGGATTCCTTGTG
AATGTTAAAGAGCAATTAGAACAACCCGAGCTTTTGCTAAAAATG


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