Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR335 IGR333 IGR334 IGR331 IGR332 ribC, - CT405 CT404 CT399 sucB, - CT400 gltT, - CT401 ycaH, - CT402 CT398 vacB, - CT397 ribC, - CT405 CT404 CT399 sucB, - CT400 gltT, - CT401 ycaH, - CT402 CT398 vacB, - CT397 CT404 CT399 sucB, - CT400 gltT, - CT401 ycaH, - CT402 spoU, - CT403 spoU, - CT403 ribC, - CT405 CT398 vacB, - CT397
* Calculated from Protein Sequence

Gene ID: CT400

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sucB  

Definition:
dihydrolipoamide 5-succinyltransferase

Gene Start:
459600

Gene Stop:
458437

Gene Length:
1164

Molecular Weight*:
42448

pI*:
5.45

Net Charge*:
-6.75

EC:
2.3.1.61  

Functional Class:
central intermediary metabolism; TCA cycle  

Pathway: pathway table
Citrate cycle (TCA cycle)
Lysine degradation

Comment:
In E. coli, as part of the TCA cycle, this enzyme converts dihydrolipoamide to
succcinyl-dihydrolipoamide. See CT247 and CT055.
CT400 was assigned the EC number 2.3.1.61 in our original annotation. Comparison of the annotation in the STD genome database with the annotation done by KEGGs leads us to re-examine this protein.

The top hits in Gapped-BLAST were to dihydrolipoamide S-succinyltransferase which is assigned the EC number 2.3.1.61 in the Swiss-Prot and Pir databases.

Several hits to dihydrolipoamide S-acetyltransferase were observed at lower significance levels. The EC number assigned to these proteins by Swiss-Prot and Pir are 2.3.1.12.

The clustalw guide tree and the Phylogenetic tree indicate dihydrolipoamide S-acetyltransferase and dihydrolipoamide S-succinyltransferase are in the same superfamily. These analysis did not clearly indicate which group CT400 belongs to. The difference in annotation between the STD database and the KEGG database for CT400 will remain unresolved until further data is available.


Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to dihydrolipoamide transsuccinylase sequences,
e.g. residues 2-386 are approximately 30% similar to the E.coli enzyme.
CT400 is paralogously related to CT055, a dihydrolipoamide succinyltransferase, and to
CT247, a dihydrolipoamide acetyltransferase: residues 3-383 are 30% similar to the former and residues
5-384 are 26% similar to the latter. CT400 is similar to MG272, a dihydrolipoamide
acetyltransferase in M.genitalium. No similarity to T.pallidum.

CT400 is orthologously related to CPn0527:
residues 1-387 are 72% similar to CPn0527.

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 24-58, 225-238, 292-332, and 357-372 correspond to blocks for
2-oxo acid dehydrogenases, as represented by ODO2_BACSU, and ODP2_YEAST.

ProDom Summary:  Protein Domain Search
Residues 172-385 are approximately 38% similar to E2 complex sequences as
represented by ODB2_BACSU. A second E2 dehydrogenase domain, residues 22-55, is 61%
similar to ODO2_MYCTU.

Paralogs:  Local Blast Search
CT400 is paralogously related to CT055, also thought to be a dihydrolipoamide
succinyltransferase, and to CT247, a possible dihydrolipoamide acetyltransferase:
residues 3-383 are 30% similar to the former and 26% similar to the latter.

Pfam Summary:  Pfam Search
Residues 2 to 75 (E-value = 2.7e-18) place CT400 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 107 to 146 (E-value = 1.4e-13) place CT400 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 158 to 387 (E-value = 4.5e-109) place CT400 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
314  
335

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:
MFEFRFPKIGETASGGIVVRWLKQVGDPVQKDEPLIEVSTDKIATELAPS
QAGILEECLVQEGEEVFPGDILARLLETAAANTPVKSPVENPVREENHSV
DREQKWFSPAVLGFAQREGLDLQELQKISGTGEGGRITRKDVEHYLSDKR
EPRDPICSKEENRIPLSPLRRAIASSLRQSSEEVPHASLVVDVDVTDLMN
LISAERERFTAAHGVKLTITSFIIQCLAKSLEQFPLLNGSLDGDTIVLKK
AINVGVAVNLNKEGVVVPVIHNCQDRGLVSIAKVLADLSSRARSNKLDSS
ETKGGSVTVTNFGMTGALIGMPIIRYPEVAILGIGTIQKRVVVRDDDSLA
IRKMMCVTLTFDHRILDGIYGGEFLTALKNRLESVTMS

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTCGAGTTTCGATTTCCAAAAATAGGGGAGACCGCATCTGGAGGTAT
TGTTGTCCGATGGTTGAAACAGGTCGGAGATCCTGTTCAAAAAGATGAGC
CATTGATTGAGGTCTCAACAGATAAGATAGCTACAGAGTTAGCTCCTTCT
CAAGCTGGCATTTTGGAGGAGTGCCTGGTTCAGGAAGGGGAAGAGGTTTT
CCCTGGAGATATTCTAGCGCGTTTGCTAGAAACTGCTGCAGCGAATACTC
CTGTAAAAAGCCCTGTGGAGAATCCTGTTAGAGAAGAGAATCATTCTGTA
GATAGAGAGCAGAAATGGTTCTCGCCCGCAGTATTAGGATTTGCCCAAAG
AGAAGGGTTAGATCTTCAAGAATTACAAAAGATCTCGGGGACAGGAGAGG
GGGGACGGATTACTCGTAAGGATGTAGAACACTATCTTTCCGACAAGAGA
GAACCTAGGGATCCGATCTGTTCTAAAGAGGAAAATAGAATTCCTTTGTC
ACCTTTACGTCGGGCTATCGCTTCTTCTTTACGACAGTCTTCAGAAGAGG
TGCCGCATGCTTCTCTGGTTGTTGATGTAGATGTTACAGATTTAATGAAT
CTCATCTCTGCGGAGCGAGAGAGATTTACTGCTGCTCATGGAGTGAAACT
CACGATCACCAGCTTCATTATACAGTGCTTAGCTAAGTCTTTAGAGCAGT
TCCCACTGCTTAATGGTTCTTTAGACGGGGATACGATTGTCCTCAAGAAG
GCTATAAATGTAGGAGTTGCTGTAAATTTGAATAAAGAAGGAGTAGTTGT
TCCTGTTATTCATAATTGTCAGGATAGGGGTCTTGTAAGTATTGCTAAGG
TTCTTGCGGATCTTTCTTCAAGGGCGCGATCTAATAAATTAGATTCCTCA
GAAACGAAAGGGGGAAGCGTCACTGTAACCAACTTTGGTATGACTGGAGC
TCTTATTGGCATGCCGATAATTCGTTATCCGGAAGTAGCGATTTTGGGGA
TCGGAACAATTCAAAAACGAGTGGTTGTACGTGATGATGACTCGTTAGCC
ATTAGGAAAATGATGTGTGTCACTTTAACTTTCGACCATCGAATATTGGA
TGGAATTTACGGTGGAGAGTTTTTAACAGCTTTGAAAAATCGCTTAGAGT
CTGTTACGATGAGC


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy