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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR82 IGR81 IGR84 IGR79 IGR83 IGR85 IGR80 CT101 fabI, - CT104 rs1, - CT098 infB, - CT096 acpS, - CT100 CT102 CT103 trxB, - CT099 CT105 CT101 fabI, - CT104 rs1, - CT098 infB, - CT096 acpS, - CT100 CT102 CT103 trxB, - CT099 CT105 CT101 fabI, - CT104 rs1, - CT098 infB, - CT096 nusA, - CT097 nusA, - CT097 acpS, - CT100 CT102 CT103 trxB, - CT099 CT105
* Calculated from Protein Sequence

Gene ID: CT099

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
trxB  

Definition:
NADPH thioredoxin reductase

Gene Start:
115919

Gene Stop:
116971

Gene Length:
1053

Molecular Weight*:
37811

pI*:
7.56

Net Charge*:
1.59

EC:
1.6.4.5  

Functional Class:
purines, pyrimidines, nucleosides and nucleotides; deoxyribonucleotide metabolism  

Pathway: pathway table
Nucleotide Metabolism; Pyrimidine metabolism

Comment:
See CT539.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to NADPH thioredoxin reductase proteins, e.g., 52% similarity to NADPH thioredoxin reductase in Arabidopsis thaliana (AC002329), 54% similarity to TRXB_YEAST.
CT099 is similar to TP0735 in T.pallidum, a predicted glutamate synthase, and to MG102
in M.genitalium, a predicted thioredoxin reductase.

CT099 is orthologously related to CPn0314: residue 40-349 are 78% similar
to CPn0314.

COGS Summary:  COGS Search
BeTs to 17 clades of COG0492
COG name: Thioredoxin reductase/alkyl hydroperoxide reductase
Functional Class:  O
The phylogenetic pattern of COG0492 is amtkYQVcEBrhUJgpolinX
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 47-68, 194-215, 80-94, 145-162, 116-133, 27-71, 277-303, 312-349, 28-65 are significantly matched to blocks BL00573A,B,C,D,E,F, concerned with Pyridine nucleotide-disulphide oxidoreductases class-II proteins, e.g. TRXB_HAEIN and TRXB_ECOLI.
Residues 191-210, 44-63 are significantly matched to blocks PR00757A, concerned with flavin-containing amine oxidase signature proteins, e.g. AOFA_HUMAN.
Residues 44-58, 1-15 are significantly matched to blocks PR00335A, concerned with tRNA potassium protein signature proteins, e.g. TRKA_ECOLI.
Residues 191-213, 44-66 are significantly matched to blocks PR00420A, concerned with aromatic-ring hydroxylase (flavoprotein monooxygenase) signature proteins, e.g. PHHY_PSEAE and PHHY_PSEFL.
Residues 44-66, 191-213, 192-206, 45-59 are significantly matched to blocks PR00419A,D, concerned with adrenodoxin reductase family proteins, e.g. ADRO_BOVIN and ADRO_HUMAN.

ProDom Summary:  Protein Domain Search
Residues 149-288 are 53% similar to a reductase domain as observed in TRB2_ARATH. Residues 82-134 and 293-324 are consistent with this observation.
Residues 40-321 are similar to a hypothetical protein domain as seen in YPDA_BACSU.
Residues 190-270 and 275-323 are similar to dehydrogenase domains seen in GLTD_AZOBR, GLTD_ECOLI.

Paralogs:  Local Blast Search
CT099 is paralogously related to CT557, a lipoamide dehydrogenase component (E3) of pyruvate dehydrogenase: residues 46-342 are 24% similar to CT557.

Pfam Summary:  Pfam Search
Residues 44 to 333 (E-value = 9.8e-84) place CT099 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
29  
46
transmembrane  
52  
75

PDB Hit:
gi|1942055|pdb|1VDC| Structure Of Nadph Dependent Thioredoxin Reductase Hypothetical Protein, Redox-Active Center, Oxidoreductase, Disulfide Oxidoreductase, Thioredoxin Reductase, Flavin Adenine Dinuleotide Mol_id: 1; Molecule: Nadph Dependent Thioredoxi

Gene Protein Sequence:
MNVVCGKSRVGYSSFFCKSREPFSCVFKALLSKFILGVPMTHAKLVIIGS
GPAGYTAAIYASRALLTPVLFEGFFSGIAGGQLMTTTEVENFPGFPEGVL
GHQLMDLMKTQAQRFGTQVLSKDITAVDFSVRPFVLKSGKETFTCDACII
ATGASAKRLSIPGAGDNEFWQKGVTACAVCDGASPIFRDKDLFVVGGGDS
ALEEAMFLTRYGKRVFVVHRRDTLRASKVMVNKAQANEKIFFLWNSEIVK
ISGDTLVRSIDIYNNVDETTTTMEAAGVFFAIGHQPNTAFLGGQVALDEN
GYIITEKGSSRTSVPGVFAAGDVQDKYYRQAITSAGSGCMAALDAERFLE
N

Gene Nucleotide Sequence:  Sequence Viewer
ATGAATGTCGTTTGCGGAAAAAGTCGGGTTGGTTATAGTTCCTTTTTTTG
TAAAAGCCGGGAACCTTTTTCCTGCGTATTTAAAGCTCTTTTATCTAAGT
TCATATTGGGGGTTCCCATGACACATGCAAAGTTAGTCATTATAGGCTCC
GGGCCTGCAGGTTACACAGCTGCTATCTATGCTTCTAGAGCACTTTTGAC
TCCAGTGCTTTTCGAGGGTTTCTTTTCTGGCATTGCTGGAGGGCAGCTAA
TGACTACAACAGAAGTGGAAAATTTCCCAGGTTTCCCAGAGGGAGTGTTG
GGGCACCAGTTGATGGATCTTATGAAAACTCAAGCGCAACGTTTCGGTAC
GCAAGTACTTTCTAAGGACATCACCGCTGTTGATTTTAGTGTCAGACCCT
TTGTTCTTAAATCTGGAAAGGAGACGTTTACCTGTGATGCTTGTATTATA
GCTACTGGAGCATCAGCAAAGCGTTTATCTATCCCTGGGGCAGGAGATAA
TGAGTTTTGGCAAAAGGGCGTAACAGCTTGCGCTGTTTGTGACGGAGCTT
CTCCCATTTTTCGTGACAAAGATTTGTTTGTTGTAGGAGGAGGAGACTCC
GCTTTAGAAGAAGCCATGTTTTTGACTCGCTATGGTAAACGTGTATTTGT
GGTTCATAGGAGAGATACATTGCGAGCTTCTAAGGTTATGGTGAATAAAG
CTCAGGCGAATGAAAAAATCTTTTTCCTTTGGAATAGTGAGATTGTCAAG
ATTTCTGGAGATACTCTAGTTCGTTCTATCGACATCTATAATAATGTGGA
TGAGACCACCACAACCATGGAAGCTGCTGGAGTTTTCTTTGCTATTGGGC
ATCAACCCAACACTGCATTTCTAGGAGGGCAGGTAGCTTTAGACGAGAAT
GGATACATTATTACAGAAAAAGGTTCTTCTCGCACATCAGTTCCTGGAGT
GTTTGCTGCGGGGGATGTCCAAGATAAATATTACAGACAAGCTATTACTT
CTGCTGGTAGTGGGTGCATGGCAGCTTTAGATGCCGAAAGATTTTTAGAA
AAT


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