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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR461 IGR463 IGR460 IGR458 IGR459 IGR462 CT556 sctL,yscL, - CT561 CT560 yscR,sctR, - CT562 lipA, - CT558 sctJ,yscJ, - CT559 lpdA, - CT557 mot1, - CT555 CT556 sctL,yscL, - CT561 CT560 yscR,sctR, - CT562 lipA, - CT558 sctJ,yscJ, - CT559 lpdA, - CT557 mot1, - CT555 CT556 sctL,yscL, - CT561 CT560 yscR,sctR, - CT562 lipA, - CT558 sctJ,yscJ, - CT559 lpdA, - CT557 mot1, - CT555
* Calculated from Protein Sequence

Gene ID: CT557

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
lpdA  

Definition:
pyruvate dehydrogenase E3 component (dihydrolipoamide dehydrogenase)

Gene Start:
629017

Gene Stop:
630411

Gene Length:
1395

Molecular Weight*:
49480

pI*:
6.78

Net Charge*:
-1.42

EC:
1.8.1.4  

Functional Class:
energy metabolism; pyruvate metabolism, glycolysis and gluconeogenesis  

Pathway: pathway table
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis
Carbohydrate Metabolism; Pyruvate metabolism

Comment:
The CT557 protein is thought to belong to the pyridine nucleotide-disulphide oxidoreductases, class-I. Analogous to E.coli, the lipoamide dehydrogenase might serve as the L component protein in the glycine cleavage system (see CT282). E1 and E2 components are represented by CT245, CT246 and CT247.

From Prosite PDOC00073:

The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contains a pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to lipoamide dehydrogenase proteins, e.g., 39% similarity to lipoamide dehydrogenase from Pisum sativum (X62995), 39% similarity to DLDH_HUMAN, 38% similarity to DLDH_PSEFL.
CT557 is similar to TP0921, a predicted NADH oxidase in T.pallidum. It
is also similar to MG271, a predicted dihydrolipoamide dehydrogenase in
M.genitalium.


CT557 is orthologously related to CPn0833:
residues 1-462 are 71% similar to residues
1-459 of CPn0833.


COGS Summary:  COGS Search
BeTs to 11 clades of COG1249
COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymes
Functional Class:  C
The phylogenetic pattern of COG1249 is amt-YqvCEBRH--gp--inX
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 5-34, 174-203, 39-51, 280-292, 296-303, 392-440, 263-311, 289-337, 3-51, 168-216 are matched to blocks BL00076A,B,C,D, which encompass pyridine nucleotide-disulphide oxidoreductases class-I. e.g., DLD2_PSEPU, DLD2_BACSU. Residues 9-30, 134-151, 158-202, 297-334, 357-401 are matched to blocks BL00573A,C,D,F, which encompass pyridine nucleotide-disulphide oxidoreductases class-II e.g., R34K_CLOPA, TRXB_EUBAC, TRXB_ECOLI, TRXB_CLOLI. Residues 8-39, 177-208 are matched to block BL00982A which encompasses Bacterial-type phytoene dehydrogenase proteins, e.g.,CRTD_RMOCA. Residues 6-28, 175-197 are significantly matched to block PR00420A, concerned with aromatic-ring hydroxylase (flavoprotein monooxygenase) signature proteins, e.g. PHHY_PSEAE, PHHY_PSEFL. Residues 6-20 are significantly matched to BL00504A concerned with fumarate reductase / succinate dehydrogenase FAD-binding site proteins, e.g. DHSA_YEAST. Residues 6-28, 175-197, 121-143, 176-190 are significantly matched to PR00419A, D, concerned with adrenodoxin reductase family signature, e.g.ADRO_BOVIN, GLSN_MEDSA. Residues 6-57 are significantly matched to BL00977A, concerned with FAD-dependent glycerol-3-phosphate dehydrogenase proteins, e.g. GLPD_MYCLE.

ProDom Summary:  Protein Domain Search
Residues 310 to 444 are 48% similar to a dihydrolipoamide reductase dehydrogenase dihydrolipoamide domain as seen in DLD2_BACSU. Residues 137 to 267 are 39% similar to the hypothetical 41.3 KDa protein domain as seen in DLDH_PEA. Residues 41 to 102 are 51% similar to a reductase dehydrogenase dihydrolipoamide domain as seen in DLD2_BACSU. Residues 107 to 381 are 24% similar to a reductase dehydrogenase dihydrolipoamide domain as seen in YN9B_YEAST. Residues from 274 to 308 are 57% similar to a reductase dehydrogenase domain as seen in DLD1_BACSU.

Paralogs:  Local Blast Search
CT557 is paralogous to CT099, also thought to be thioredoxin reductase: residues 8 to 326 are 24% similar to CT099.

Pfam Summary:  Pfam Search
Residues 6 to 317 (E-value = 1.7e-105) place CT557 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 341 to 450 (E-value = 1.6e-48) place CT557 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

PDB Hit:
gi|1633234|pdb|1EBD|A Chain A, Dihydrolipoamide Dehydrogenase Complexed With The Binding Domain Of The Dihydrolipoamide Acetylase Redox-Active Center, Glycolysis, Oxidoreductase Mol_id: 1; Molecule: Dihydrolipoamide Dehydrogenase; Chain: A, B; Synonym: E3

Gene Protein Sequence:
MNEAFDCVVIGAGPGGYVAAITAAQAGLKTALIEKREAGGTCLNRGCIPS
KALLAGAEVVTQIRHADQFGIHVEGFSINYPAMVQRKDSVVRSIRDGLNG
LIRSNKITVFSGRGSLISSTEVKILGENPSVIKAHSIILATGSEPRAFPG
IPFSAESPRILCSTGVLNLKEIPQKMAIIGGGVIGCEFASLFHTLGSEVS
VIEASSQILALNNPDISKTMFDKFTRQGLRFVLEASVSNIEDIGDRVRLT
INGNVEEYDYVLVSIGRRLNTENIGLDKAGVICDERGVIPTDATMRTNVP
NIYAIGDITGKWQLAHVASHQGIIAARNIAGHKEEIDYSAVPSVIFTFPE
VASVGLSPTAAQQQKIPVKVTKFPFRAIGKAVAMGEADGFAAIISHETTQ
QILGAYVIGPHASSLISEITLAVRNELTLPCIYETIHAHPTLAEVWAESA
LLAVDTPLHMPPAKK

Gene Nucleotide Sequence:  Sequence Viewer
ATGAATGAAGCTTTCGACTGTGTAGTTATCGGAGCGGGGCCAGGGGGCTA
TGTTGCAGCAATCACTGCCGCTCAAGCAGGACTCAAAACTGCGCTAATCG
AAAAGCGAGAGGCTGGCGGAACCTGTTTAAACCGAGGGTGTATTCCTTCT
AAAGCCCTCTTAGCAGGAGCTGAAGTCGTTACCCAAATACGCCATGCTGA
CCAGTTTGGGATTCATGTAGAAGGATTCAGCATCAACTATCCCGCTATGG
TACAAAGGAAGGATTCCGTAGTCCGTAGCATCCGCGATGGACTTAATGGT
CTCATTCGCAGCAATAAGATCACTGTCTTCTCTGGAAGAGGCTCTTTGAT
CTCTTCAACAGAAGTAAAAATCTTAGGAGAAAACCCTTCTGTAATCAAAG
CGCACTCCATTATCCTAGCCACCGGCTCTGAACCACGAGCTTTCCCCGGG
ATTCCTTTTTCCGCAGAATCTCCTCGGATTTTATGCTCAACAGGCGTGCT
AAACCTCAAAGAAATCCCTCAAAAAATGGCCATTATTGGCGGTGGTGTGA
TCGGTTGCGAATTCGCTTCCTTATTCCATACGTTAGGCTCCGAAGTTTCT
GTGATCGAAGCAAGCTCTCAAATCCTTGCTTTGAATAATCCAGATATTTC
AAAAACCATGTTCGATAAATTCACCCGACAAGGACTCCGTTTCGTACTAG
AAGCCTCTGTATCAAATATTGAGGATATAGGAGATCGCGTTCGGTTAACT
ATCAATGGGAATGTCGAAGAATACGATTACGTTCTCGTATCTATAGGACG
CCGTTTGAATACAGAAAATATTGGCTTGGATAAAGCTGGTGTTATTTGTG
ATGAACGCGGAGTCATCCCTACCGATGCCACAATGCGCACAAACGTACCT
AACATTTATGCTATTGGAGATATCACAGGAAAATGGCAACTTGCCCATGT
AGCTTCTCATCAAGGAATCATTGCAGCACGGAATATAGCTGGCCATAAAG
AGGAAATCGATTACTCTGCCGTCCCTTCTGTGATCTTTACCTTCCCTGAA
GTCGCTTCAGTAGGCCTATCCCCAACAGCAGCTCAACAACAAAAAATCCC
CGTCAAAGTAACAAAATTCCCATTTCGAGCTATTGGAAAAGCGGTCGCAA
TGGGCGAGGCCGATGGATTTGCAGCCATTATCAGCCATGAGACTACTCAG
CAGATCCTAGGAGCTTATGTGATTGGCCCTCATGCCTCATCACTGATTTC
CGAAATTACCCTAGCAGTTCGTAATGAACTGACTCTTCCTTGTATTTACG
AAACTATCCACGCACATCCAACCTTAGCAGAAGTTTGGGCTGAAAGTGCG
TTGTTAGCTGTTGATACCCCATTACATATGCCCCCTGCTAAAAAA


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