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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR303 IGR302 IGR298 IGR299 IGR301 IGR305 IGR304 IGR300 bioY, - CT359 CT360 dapB, - CT364 dapA, - CT361 lysC, - CT362 CT365 CT357 CT358 aroA, - CT366 bioY, - CT359 CT360 dapB, - CT364 dapA, - CT361 lysC, - CT362 CT365 CT357 CT358 aroA, - CT366 bioY, - CT359 CT360 dapB, - CT364 dapA, - CT361 lysC, - CT362 CT365 asd, - CT363 asd, - CT363 CT358 aroA, - CT366 aroL, - CT367 aroL, - CT367 CT357
* Calculated from Protein Sequence

Gene ID: CT363

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
asd  

Definition:
aspartate semialdehyde dehydrogenase

Gene Start:
415226

Gene Stop:
414225

Gene Length:
1002

Molecular Weight*:
36662

pI*:
6.34

Net Charge*:
-5.71

EC:
1.2.1.11  

Functional Class:
amino acid biosynthesis; aspartate family  

Pathway: pathway table
Amino Acid Metabolism; Lysine biosynthesis

Comment:
This enzyme interconverts aspartate semialdehyde and aspartyl-phosphate in the biosynthesis of threonine and methionine. See CT361, CT362, CT364 and CT430.

From Prosite PDOC00847:

Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) (ASD) catalyzes the second step in the common biosynthetic pathway leading from Asp to diaminopimelate and Lys, to Met, and to Thr; the NADP-dependent reductive dephosphorylation of L-aspartyl phosphate to L-aspartate-semialdehyde. In bacteria and fungi, ASD is a protein of about 40 Kd (340 to 370 residues) whose sequence is not extremely well conserved. A conserved cysteine residue has been implicated as important for the catalytic activity.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to aspartate semialdehyde dehydrogenase sequences,
e.g. residues 1-322 are 35% similar to DHAS_METJA. No similarities to T.pallidum
and M.genitalium.

CT363 is orthologously related to CPn1048: residues 3-321 are 63% similar to
CPn1048.

COGS Summary:  COGS Search
BeTs to 14 clades of COG0136
COG name: Aspartate-semialdehyde dehydrogenase
Functional Class:  E
The phylogenetic pattern of COG0136 is amtkyqvcEbrHuj----inx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 5-16, 21-45, 100-121, 165-175, 195-207, 216-241
are significantly matched to aspartate semialdehyde dehydrogenase
blocks BL01103A,B,C,D,E,F; see DHAS_METJA, DHAS_CAMJE, etc.
Residues 7-26, 135-155 and 294-328 match blocks BL01224A,D,H,
which include N-acetyl-gamma-glutamyl-phosphate reductase
sequences, e.g., ARGC_BACSU, AR56_CANAL.

ProDom Summary:  Protein Domain Search
Residues 70-179 are 47% similar to an aspartate semialdehyde
dehydrogenase domain seen in DHAS_METJA. Residues 7-60,
181-318 and 195-247 support this assignment, as evidenced
by matches to domains of DHAS_LEPIN, DHAS_YEAST, DHAS_CORFL.

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

Pfam Summary:  Pfam Search
Residues 2 to 139 (E-value = 2.8e-18) place CT363 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain (PF01118)
Residues 152 to 306 (E-value = 2.5e-22) place CT363 in the Semialdhyde_dhC family which is described as Semialdehyde dehydrogenase, dimerisation domain (PF02774)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
141  
168

PDB Hit:
none

Gene Protein Sequence:
MTMRIAILGATGLVGQKLIALLQNHKQWEIAELGASSEKHALRYESACLW
QEPLMGMPESVRDLSIRSVEEIESNIVVSCLPSSVAFSAETTCLSSGKIV
FSNATAYRMHKAVPILIPEINSDHLSLLEEQPFLGKIITNSNCCVSGIAL
ALKPLLLFNIEHVHVITLQSASGAGYPGVSSLDLIGNTVPYILGEEEKIL
RETVKILGQPGFPAEFSITASVHRVPVAHGHVISVHVMFDQEVDLEEITS
CYEKDSATYVLYDSPWHPQVRKDLAHDDMRLHIGPISYGGNTRTIKMCIL
LHNLVRGAAGALIANMNLFRDRGGFVHQERLTYA

Gene Nucleotide Sequence:  Sequence Viewer
ATGACGATGCGCATTGCGATTTTAGGTGCTACAGGCCTTGTTGGACAAAA
GCTTATTGCTTTGTTACAAAATCATAAACAGTGGGAAATTGCTGAATTAG
GAGCTTCTTCTGAGAAGCATGCGTTGCGTTACGAATCTGCTTGTTTATGG
CAAGAGCCATTAATGGGGATGCCAGAGTCTGTTCGTGATTTATCTATTCG
CTCCGTTGAAGAGATAGAATCAAATATTGTTGTATCTTGTCTTCCTTCGT
CTGTTGCTTTTTCAGCAGAAACTACTTGTTTATCTTCGGGAAAGATAGTG
TTTTCTAATGCCACCGCCTATCGTATGCATAAAGCGGTTCCTATTTTAAT
TCCTGAGATAAACAGTGATCATTTGTCTCTGTTAGAAGAACAGCCTTTTT
TAGGTAAGATTATTACTAATTCTAATTGTTGTGTTTCAGGCATTGCTCTG
GCTCTTAAGCCACTGCTGTTGTTTAATATCGAGCATGTGCATGTTATCAC
TTTACAATCAGCTAGTGGGGCTGGATATCCTGGAGTTTCCTCTTTAGATT
TAATTGGAAACACTGTGCCTTATATCTTAGGAGAGGAAGAGAAGATACTC
CGAGAGACTGTAAAAATTTTAGGACAGCCAGGTTTTCCTGCAGAGTTTTC
TATAACTGCGTCTGTACATCGTGTTCCCGTTGCACATGGGCATGTCATCT
CTGTACACGTTATGTTTGATCAAGAGGTCGATTTAGAAGAGATAACTTCT
TGTTATGAGAAGGATTCGGCTACCTATGTTCTTTATGATTCTCCTTGGCA
TCCTCAGGTTCGAAAGGATCTAGCTCATGATGATATGCGATTACATATAG
GGCCCATTTCTTACGGCGGTAATACGCGAACTATTAAGATGTGTATCTTA
TTGCACAATTTGGTTCGAGGAGCTGCAGGAGCTTTGATAGCGAATATGAA
TCTTTTCCGAGATAGAGGAGGATTCGTTCATCAAGAGAGGCTGACGTATG
CT


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