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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR249 IGR248 IGR246 IGR244 IGR245 IGR247 dcrA, - CT296 mrsA,mrsA, - CT295 pknD, - CT301 valS, - CT302 CT300 radA,sms, - CT298 dcrA, - CT296 mrsA,mrsA, - CT295 pknD, - CT301 valS, - CT302 CT300 radA,sms, - CT298 dcrA, - CT296 mrsA,mrsA, - CT295 pknD, - CT301 valS, - CT302 CT300 radA,sms, - CT298 rnc, - CT297 hemC, - CT299 rnc, - CT297 hemC, - CT299
* Calculated from Protein Sequence

Gene ID: CT299

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
hemC  

Definition:
porphobilinogen deaminase (pre-uroporphyrinogen synthase or hydroxymethylbilane synthase)

Gene Start:
332710

Gene Stop:
333432

Gene Length:
723

Molecular Weight*:
26981

pI*:
7.90

Net Charge*:
2.87

EC:
4.3.1.8  

Functional Class:
cofactor biosynthesis; heme and porphyrin  

Pathway: pathway table
Metabolism of Cofactors, Vitamins, and Other Substances; Porphyrin and chlorophyll metabolism

Comment:
The HEM3 protein in E.coli catalyzes one or more steps in the porphyrin biosynthesis pathway. A 3D structure is available.

From Prosite PDOC00461:

Porphobilinogen deaminase (EC 4.3.1.8), or hydroxymethylbilane synthase, is an enzyme involved in the biosynthesis of porphyrins and related macrocycles. It catalyzes the assembly of four porphobilinogen (PBG) units in a head to tail fashion to form hydroxymethylbilane.

The enzyme covalently binds a dipyrromethane cofactor to which the PBG subunits are added in a stepwise fashion. In the Escherichia coli enzyme (gene hemC), this cofactor has been shown to be bound by the sulfur atom of a cysteine. The region around this cysteine is conserved in porphobilinogen deaminases from various prokaryotic and eukaryotic sources.


Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to hydroxymethylbilane synthase sequences, e.g.
residues 21-202 are 36% similar to HEM3_ECOLI. No similarities to T.pallidum
or M.genitalium.

CT299 is similar to CPn0052, a predicted Porphobilinogen Deaminase: residues
1-226 are 53% similar to CPn0052.

COGS Summary:  COGS Search
BeTs to 12 clades of COG0181
COG name: Porphobilinogen deaminase
Functional Class:  H
The phylogenetic pattern of COG0181 is amt-yq-cebr-uj----inx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 21-43, 72-122, 74-124, 138-181 are similar to blocks BL0533A-C, which comprise
porphobilinogen deaminase sequences, e.g. HEM3_ECOLI, HEM3_CLOJO. Residues
117-137 are similar to block PR00716D, concerned with inducer phosphatases, e.g.
MPI3_HUMAN. Residues 13-26 and 80-102 are similar to blocks BL01316B,C, which consist of
ATP phosphoribosyltransferase sequences, e.g. HIS1_SYNY3.

ProDom Summary:  Protein Domain Search
Residues 52-213 are 35% similar to a HEM3 domain as observed in HEM3_ECOLI.

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

Pfam Summary:  Pfam Search
Residues 20 to 224 (E-value = 8.2e-18) place CT299 in the Porphobil_deam family which is described as Porphobilinogen deaminase, dipyromethane cofactor binding domain (PF01379)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
99  
181

PDB Hit:
gi|2624859|pdb|1AH5| Reduced Form Selenomethionine-Labelled Hydroxymethylbilane Synthase Determined By Mad Lyase, Biosynthesis Of Linear Tetrapyrrole, All AlphaBETA Mol_id: 1; Molecule: Hydroxymethylbilane Synthase; Chain: Null; Fragment: Three Domains;

Gene Protein Sequence:
MLSAYYNDPFLADFCLGNIPLRLASRQSSLAVLQAHECLRKLQIFFPRLW
GQIITTTTQGDLDQETPLCAVENTGFFTDDVDFLVQSGQCDLGIHSAKDL
PENPKATVVSITASIDPRDILVFHEKYLSIPLPRRLRIGSSSVRRKELLS
LLYPSAIITDIRGTIQTRLKLLEEKNFDAIVMANAAVSRLGLRLPCTKIL
PPPYHPLQGRLAITASRHIRSWRGLFLTCGITEDVEIMCFS

Gene Nucleotide Sequence:  Sequence Viewer
ATGCTGTCCGCTTACTACAATGACCCATTTTTAGCTGATTTTTGTTTAGG
GAACATTCCTTTACGTTTGGCATCTAGACAATCTTCTCTGGCAGTTCTGC
AAGCTCACGAATGCCTGAGAAAACTACAGATATTTTTCCCTCGATTATGG
GGACAGATTATCACCACAACAACACAGGGTGATCTTGATCAAGAGACACC
TCTGTGTGCTGTAGAAAATACAGGTTTTTTTACAGATGATGTCGATTTCT
TGGTGCAATCTGGGCAATGTGATCTTGGTATACATTCCGCTAAGGACCTT
CCAGAAAATCCGAAGGCAACGGTTGTCTCCATTACAGCCAGTATAGATCC
TCGAGATATCCTCGTATTTCATGAAAAATACCTTTCGATCCCGTTACCTC
GCCGTTTACGCATAGGGAGCTCCTCCGTGAGACGAAAAGAGCTTCTCTCT
CTGCTCTATCCCTCTGCCATTATTACCGATATTCGAGGGACTATCCAGAC
TCGCTTAAAGCTGTTAGAAGAGAAAAATTTTGATGCCATAGTCATGGCTA
ATGCTGCGGTGTCTCGACTAGGACTACGTCTTCCTTGCACAAAAATCCTC
CCCCCACCCTATCATCCTCTTCAAGGACGTCTAGCCATCACTGCTAGCCG
ACATATACGGAGCTGGAGAGGTTTATTCTTAACTTGCGGCATCACAGAAG
ATGTAGAAATTATGTGTTTTTCT


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