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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR359 IGR361 IGR356 IGR360 IGR354 IGR355 IGR358 IGR357 rs10, - CT436 dapF, - CT430 CT429 cysJ, - CT435 glyA, - CT432 fusA, - CT437 CT434 CT433 ubiE, - CT428 CT426 rs10, - CT436 dapF, - CT430 CT429 cysJ, - CT435 glyA, - CT432 fusA, - CT437 CT434 CT433 ubiE, - CT428 CT426 rs10, - CT436 dapF, - CT430 CT429 cysJ, - CT435 glyA, - CT432 fusA, - CT437 clpP, - CT431 clpP, - CT431 CT434 CT433 ubiE, - CT428 CT427 CT426 CT427
* Calculated from Protein Sequence

Gene ID: CT432

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
glyA  

Definition:
serine hydroxymethyltransferase

Gene Start:
502443

Gene Stop:
500953

Gene Length:
1491

Molecular Weight*:
54262

pI*:
6.70

Net Charge*:
-2.21

EC:
2.1.2.1  

Functional Class:
amino acid biosynthesis; serine-glycine family  

Pathway: pathway table
Cyanoamino acid metabolism
Glycine, serine and threonine metabolism
Lysine degradation
Methane metabolism
One carbon pool by folate

Comment:
This enzyme is involved in the interconversion of glycine and serine. In E.coli, it is homotetrameric. Pyridoxal phosphate is a cofactor in the reaction.

From Prosite PDOC00090:

Serine hydroxymethyltransferase (EC 2.1.2.1) (SHMT) catalyzes the transfer of the hydroxymethyl group of serine to tetrahydrofolate to form 5,10-methylenetetrahydrofolate and glycine. In vertebrates, it exists in a cytoplasmic and a mitochondrial form whereas only one form is found in prokaryotes. Serine hydroxymethyltransferase is a pyridoxal-phosphate containing enzyme. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to serine hydroxymethyltransferase sequences,
e.g., residues 29-91 are 44% similar to the enzyme from A.aeolicus (AE000692).
Residues 17-492 are 51% similar to TP0329, a predicted serine hydroxymethyltransferase in T.pallidum.
CT432 is also similar to MG394 in M.genitalium.

CT432 is orthologously related to CPn0521: residues 1-497 are 77% similar
to CPn0521.

COGS Summary:  COGS Search
BeTs to 17 clades of COG0112
COG name: Glycine hydroxymethyltransferase
Functional Class:  E
The phylogenetic pattern of COG0112 is amtkYqvcebRhujgpolinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 49-439 span nine blocks, BL00096A-G, which encompass
serine hydroxymethyltransferase sequences, e.g. GLYA_HELPY, GLYA_MYCGE.

ProDom Summary:  Protein Domain Search
Residues 314-492 are 43% similar to a glyA domain as observed in
GLYA_BACSU. Residues 37-99 also match a serine hydroxymethyltransferase domain of
GLYA_SYNY3 and residues 104-136 and 172-304 are similar to phosphate pyridoxal
transferase domains of GLYA_BACSU and GLYA_RICPR.

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

Pfam Summary:  Pfam Search
Residues 32 to 442 (E-value = 7.9e-139) place CT432 in the SHMT family which is described as Serine hydroxymethyltransferase (PF00464)

PDB Hit:
none

Gene Protein Sequence:
MASLLDRYLRNISDKSQQNLASVAYLASLDHLLHAFPSIGQSIVQELKSQ
RSRLKMIASENFSSLSVQLAMGNLLTDKYCEGSPFKRFYSCCENVDAIEW
ECAETAKELFGAESAFVQPHSGADANLLAIMSIITQKIQSPAVQRLGYKT
INDLPEQEYEALKAEMAQHKCLGPSLNSGGHLTHGTVRMNIMSKLMHCLP
YEVNLDTELFDYDEIAKIAKEHKPTVLIAGYSSYSRRLNFATLKQIAEDC
GAVLWVDMAHFAGLVAGGVFVGEENPMPYADIVTTTTHKTLRGPRGGLVL
AKKEYANTLNKACPLMMGGPLPHVIAAKAIALKEAMTINFRKYAHKVVEN
ARTLAEVFQRNGLRLLTGGTDNHMLIIDLTSLGVPGRIAEDMLTSVGIAV
NRNTIPSDASGQWKTSGIRLGTPALTTLGMGSAEMEEVANIIVKVLRNIT
VRSNAESGSSKSEGELSEGIAQEARQRVADLLGRFPLYPEIDLETLV

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCATCGTTATTGGATAGATATCTGAGAAATATTTCCGACAAAAGTCA
GCAAAATTTGGCATCAGTGGCCTATTTAGCATCATTAGATCATCTGTTAC
ACGCTTTTCCATCTATAGGACAGAGCATTGTACAAGAATTAAAGAGTCAG
CGATCTCGTTTAAAAATGATTGCTTCAGAAAACTTTTCTTCTCTATCTGT
GCAACTTGCTATGGGGAATTTACTTACAGACAAGTATTGTGAAGGGAGCC
CATTCAAACGATTTTATTCCTGTTGCGAGAATGTGGATGCAATTGAATGG
GAATGCGCAGAGACGGCAAAAGAATTATTTGGTGCGGAAAGTGCTTTTGT
TCAGCCTCATTCTGGAGCCGATGCGAATTTATTAGCGATCATGTCGATCA
TTACACAGAAGATCCAGAGCCCTGCGGTTCAACGGTTGGGATATAAAACG
ATCAATGATCTGCCTGAGCAGGAATACGAAGCATTAAAAGCTGAGATGGC
TCAGCACAAATGCCTAGGCCCCTCTTTAAATTCTGGAGGGCATCTGACAC
ATGGGACTGTGCGCATGAATATCATGTCTAAATTAATGCATTGTCTCCCT
TATGAGGTGAATTTAGATACTGAATTATTTGATTATGATGAGATAGCAAA
AATAGCGAAAGAACATAAGCCCACCGTTCTGATCGCAGGGTATTCGTCTT
ATTCTAGACGATTAAACTTTGCCACCTTGAAGCAAATTGCAGAAGACTGT
GGCGCTGTTTTATGGGTGGATATGGCTCATTTCGCAGGCTTGGTTGCTGG
AGGTGTGTTTGTAGGAGAAGAAAATCCTATGCCTTATGCAGATATCGTGA
CAACGACGACGCATAAGACTTTGCGAGGGCCAAGAGGTGGATTGGTTCTA
GCTAAAAAAGAATATGCAAATACCTTGAACAAGGCTTGTCCTCTAATGAT
GGGCGGCCCACTTCCTCATGTTATAGCTGCTAAAGCTATTGCTCTGAAAG
AAGCTATGACGATCAATTTCAGGAAGTATGCGCATAAAGTGGTAGAGAAT
GCACGGACTTTGGCTGAAGTGTTCCAGCGGAACGGGCTACGATTACTCAC
TGGCGGGACAGATAATCACATGTTGATTATTGATCTAACTTCTCTAGGAG
TCCCTGGACGTATTGCAGAAGATATGTTAACCTCAGTAGGTATCGCAGTA
AATCGTAATACTATTCCTTCAGATGCCTCTGGGCAGTGGAAGACTTCTGG
TATTCGATTGGGGACTCCAGCTCTGACAACGCTAGGGATGGGCAGTGCCG
AAATGGAAGAAGTTGCGAATATTATCGTGAAAGTATTGCGAAATATTACT
GTGAGAAGCAATGCTGAGAGCGGTTCTAGTAAAAGTGAGGGAGAGCTGTC
AGAAGGGATCGCTCAGGAAGCGAGACAACGTGTGGCTGATTTATTAGGAA
GATTCCCTCTTTATCCTGAAATCGATCTGGAAACGCTAGTT


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