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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR593 IGR598 IGR597 IGR592 IGR599 IGR596 IGR594 IGR595 CT718 nifU, - CT720 fliF, - CT719 rodA, - CT726 nifS,yfhO, - CT721 fliI, - CT717 zntA,cadA, - CT727 CT724 birA, - CT725 yjbC, - CT723 CT718 nifU, - CT720 fliF, - CT719 rodA, - CT726 nifS,yfhO, - CT721 fliI, - CT717 zntA,cadA, - CT727 CT724 birA, - CT725 yjbC, - CT723 CT718 nifU, - CT720 fliF, - CT719 rodA, - CT726 nifS,yfhO, - CT721 fliI, - CT717 zntA,cadA, - CT727 pgmA,gpmA, - CT722 pgmA,gpmA, - CT722 CT724 birA, - CT725 yjbC, - CT723
* Calculated from Protein Sequence

Gene ID: CT722

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pgmA  gpmA  

Definition:
phosphoglycerate mutase

Gene Start:
834539

Gene Stop:
833862

Gene Length:
678

Molecular Weight*:
25771

pI*:
7.23

Net Charge*:
0.64

EC:
5.4.2.1  

Functional Class:
energy metabolism; glycolysis and gluconeogenesis  

Pathway: pathway table
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis

Comment:
See the comment to CT720. This phosphoglycerate mutase is 2,3-bisphosphoglycerate dependant.

From Prosite PDOC00158:

Phosphoglycerate mutase (EC 5.4.2.1) (PGAM) and bisphosphoglycerate mutase (EC 5.4.2.4) (BPGM) are structurally related enzymes which catalyze reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate. Both enzymes can catalyze three different reactions, although in different proportions:

- The isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction.
- The synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer.
- The degradation of 2,3-DPG to 3-PGA (phosphatase EC 3.1.3.13 activity).

In mammals, PGAM is a dimeric protein. There are two isoforms of PGAM: the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein. BPGM is a dimeric protein and is found mainly in erythrocytes where it plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-DPG concentration.

The catalytic mechanism of both PGAM and BPGM involves the formation of a phosphohistidine intermediate.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to Phosphoglycerate mutase 1 proteins, e.g., 47% similarity to PMGY_SCHPO, 42% similarity to PMGY_ZYMMO.
CT722 is similar to TP0168, a predicted phosphoglycerate mutase in T.pallidum.
No similarity to M.genitalium.

CT722 is orthologously related to CPn0863:
residues 1-226 are 75% similar to CPn0863.

COGS Summary:  COGS Search
BeTs to 6 clades of COG0588
COG name: Phosphoglycerate mutase 1
Functional Class:  G
The phylogenetic pattern of COG0588 is ----Y---e-rh----olin-
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 4-36, 52-63, 99-130, 144-162 are significantly matched to BL00175A,B,C,D, concerned with phosphoglycerate mutase proteins, e.g. PMG1_YEAST and PMGE_HUMAN. Residues 16-26 are significantly matched to BL00019A, concerned with Actinin-type actin-binding domain proteins, e.g. DMD_HUMAN. Residues 1-13 are significantly matched to PR00774A, concerned with guanylin precursor signature proteins, e.g. CPUGUMRNA.

ProDom Summary:  Protein Domain Search
Residues 161-212, 4-41, 96-143, 49-76 are 59%, 71%, 57%, 42% similar to a phosphoglyceromutase domain as seen in PMGY_ZYMMO. Residues 99-196, 4-63 are 30%, 35% similar to a 6-phosphofructo-2-kinase domain as seen in F261_RAT.

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

Pfam Summary:  Pfam Search
Residues 2 to 221 (E-value = 1.9e-62) place CT722 in the PGAM family which is described as Phosphoglycerate mutase family (PF00300)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
48  
66

PDB Hit:
gi|2624630|pdb|4PGM|A Chain A, Saccharomyces Cerevisiae Phosphoglycerate Mutase Transferase (Phosphoryl), Glycolytic Enzyme, Isomerase Mol_id: 1; Molecule: Phosphoglycerate Mutase 1; Chain: A, B, C, D; Ec: 5.4.2.1; Engineered: Yes; Biological_unit: Homote

Gene Protein Sequence:
MTLLILLRHGQSVWNQKNLFTGWVDIPLSQQGIQEAIAAGESIKHLPIDC
IFTSTLVRSLITALLAMTNHSSQKVPYIVHEERPDMSRIHSQKEMEQMIP
LFQSSALNERMYGELQGKNKQEVAAQFGEEQVKLWRRSYRIAPPQGESLF
DTGQRTLPYFQERIFPLLQQGKNIFISAHGNSLRSLIMDLEKLSEEQVLS
LELPTGQPIVYEWTGQKFTKHAPSLG

Gene Nucleotide Sequence:  Sequence Viewer
ATGACGCTTCTTATCTTGCTACGCCATGGCCAATCCGTATGGAATCAAAA
AAATCTGTTTACAGGCTGGGTAGACATCCCTCTTAGCCAACAAGGAATTC
AAGAGGCTATTGCCGCTGGAGAATCTATTAAACATCTTCCTATTGATTGC
ATCTTCACTTCCACCTTGGTTAGAAGTTTGATAACAGCCCTGTTAGCAAT
GACTAACCACAGCTCTCAAAAAGTTCCTTATATCGTTCATGAAGAGCGCC
CCGACATGAGCCGGATTCATAGTCAAAAAGAAATGGAGCAGATGATCCCT
CTTTTTCAATCTAGCGCTCTCAATGAACGCATGTACGGAGAACTTCAAGG
AAAAAATAAACAAGAAGTCGCTGCTCAATTCGGAGAAGAACAGGTAAAAC
TGTGGCGCCGAAGCTACCGCATTGCCCCTCCTCAGGGCGAAAGTCTTTTC
GATACAGGGCAACGAACCCTCCCCTATTTTCAAGAGAGAATTTTCCCTCT
CCTTCAGCAAGGGAAAAATATTTTTATCTCTGCTCACGGGAATTCTTTGC
GCTCCTTAATTATGGACCTAGAAAAATTATCTGAAGAACAAGTACTCTCT
TTGGAGTTGCCAACAGGACAGCCTATTGTATACGAATGGACGGGACAAAA
ATTCACGAAACACGCTCCTTCTCTTGGT


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