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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap IGR158 IGR157 IGR156 IGR159 IGR155 IGR153 IGR152 IGR160 IGR151 IGR154 UU191 UU190 UU189 UU194 UU192 UU195 prsA,kprS, - UU193 UU198 UU196 sym,metS, - UU197 rpoC, - UU188 UU191 UU190 UU189 UU194 UU192 UU195 prsA,kprS, - UU193 UU198 UU196 sym,metS, - UU197 rpoC, - UU188 Type: tandem, Name:  - 402 Type: tandem, Name:  - 124 Type: tandem, Name:  - 125 Type: tandem, Name:  - 126 UU190 UU191 UU189 UU194 UU192 UU195 prsA,kprS, - UU193 UU198 UU196 sym,metS, - UU197 rpoC, - UU188
* Calculated from Protein Sequence

Gene ID: UU193

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
prsA  kprS  

Definition:
ribose-phosphate pyrophosphokinase (phosphoribosylpyrophosphate synthetase [PRPP synthetase])

Gene Start:
236180

Gene Stop:
237172

Gene Length:
993

Molecular Weight*:
36358

pI*:
9.10

Net Charge*:
5.31

EC:
2.7.6.1  

Functional Class:
purines, pyrimidines, nucleosides, and nucleotides; salvage of nucleosides and nucleotides  

Pathway: pathway table
Pentose phosphate cycle
Purine metabolism

Comment:
Taken from Prosite PDOC00105: Phosphoribosyl pyrophosphate synthetase (EC 2.7.6.1) (PRPP synthetase) catalyzes the formation of PRPP from ATP and ribose 5-phosphate. PRPP is then used in various biosynthetic pathways, as for example in the formation of purines, pyrimidines, histidine and tryptophan. PRPP synthetase requires inorganic phosphate and magnesium ions for its stability and activity.

Reference: J Biol Chem. 1986 May 25;261(15):6765-71.

Blast Summary:  PSI-Blast Search
A gapped BLAST reveals significant similarity to a number of proteins described as ribose-phosphate pyrophosphokinase or as PRPP synthetase (they are the same thing, different names). For example: residues 8-310 are 46% similar to the prs protein of M.pneumoniae (2146588), residues 9-303 are 45% similar to the prs of L.monocytogenes (532204) and residues 4-315 are 43% similar to the PRPP synthetase of C.ammoniagenes (2289093). Other significant hits are seen against (but not limited to) KPRS_BACCL, KPRS_BACSU, KPRS_ECOLI, KPRS_HELPY and KPRS_SALTY.

A BLAST against the STDPRO database reveals significant hits to proteins found in M.genitalium (MG058) and T.pallidum (TP0294). Both proteins are described as phosphoribosyl pyrophosphate synthetase (prs). Residues 36-320 are 47% similar to MG058, and residues 38-276 are 29% similar to TP0294.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0462 is ehgpcmYu.
Cog name: Phosphoribosylpyrophosphate synthetase.
Functional class: F.
BeTs to e--pcmyu.
Number of proteins in this genome belonging to this COG is 1



Blocks Summary:  Blocks Search
Residues 57-103, 107-152, 167-201, 208-257 and 293-316 rank in the 100.00th percentile to Block BL00114(A through E respectively), described as Phosphoribosyl pyrophosphate synthetase proteins.

Residues 216-231 rank in the 99.80th percentile to Block BL00103B, described as Purine/pyrimidine phosphoribosyl transferases proteins. However, there is no significant alignment or similarity to block A (RKK motif).

ProDom Summary:  Protein Domain Search
Residues 36-209 are 56% similar to a defined domain of O33924_XXXXX, a ribose-phosphate pyrophosphokinase sequence.
Residues 217-274 are 53% similar to a defined domain of KPRS_MYCPN.

Paralogs:  Local Blast Search
UU193 shows similarity to UU104, where residues 207-250 are
35% similar to residues 98-141 of UU104, a hypoxanthine-guanine phosphoribosyltransferase.

Pfam Summary:  Pfam Search
Residues 142 to 267 (E-value = 1.7e-31) place UU193 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)

PDB Hit:


Gene Protein Sequence:
MSKNDDILLFSLSNSHQLANKIANLLKIELSPIRIDKFADGELIVAPQVP
VRGRRVIIIQSTSKPVNDSLMELLIAIDSIKRASAKAISVVIPYYGYARQ
DRKAKPREPITARLVAKMIESAGATSVLTWDIHSLQTQGFFDIPFDSLEA
VWVLMKHYFSAYKDSSNITIVSPDYGGVKRAREISIATGATLAIVDKRRS
GKNQVEINNVLGDVKDRDCVIVDDMIDTGGTILGAAKIVREKGAKSITII
ATHGLFNNNARQHFQQAIKDRIINKICIADTIENEPFDGLEIVSIAPAIA
KCIEIYSEGTGSMSFVHDENSKVLFAKKIY$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCAAAAAATGATGATATATTATTATTTAGTCTTTCAAATTCACATCA
ATTAGCTAATAAAATTGCTAATTTACTAAAAATTGAATTATCACCAATTA
GAATTGATAAGTTTGCAGATGGTGAATTAATTGTTGCACCTCAAGTTCCA
GTGCGTGGACGTCGAGTTATTATTATTCAATCAACATCTAAACCTGTTAA
CGATAGTTTAATGGAATTATTAATCGCTATTGACTCAATTAAACGAGCTA
GTGCCAAAGCAATTAGTGTTGTAATTCCTTATTATGGATATGCACGTCAA
GACCGTAAAGCTAAACCACGTGAACCAATTACAGCACGTTTAGTTGCAAA
AATGATTGAGAGTGCGGGCGCAACTAGTGTATTAACTTGAGATATTCATT
CTTTACAAACACAAGGTTTTTTTGATATTCCGTTTGATTCATTAGAGGCT
GTATGAGTTTTAATGAAACATTATTTTAGTGCTTATAAAGATTCATCAAA
TATAACTATTGTTTCACCAGATTATGGTGGTGTCAAACGTGCTCGTGAAA
TTTCAATAGCTACAGGTGCAACATTAGCAATTGTTGATAAACGAAGATCT
GGCAAAAATCAGGTGGAAATTAATAATGTATTAGGTGATGTTAAAGATCG
TGATTGTGTAATTGTTGATGATATGATTGATACTGGTGGCACAATTTTAG
GTGCTGCTAAAATTGTGCGTGAAAAAGGCGCTAAATCAATAACAATTATT
GCTACACATGGTTTGTTTAATAATAATGCACGACAACATTTTCAACAAGC
AATTAAAGATCGAATTATTAATAAAATTTGTATAGCTGATACAATTGAAA
ATGAACCTTTTGATGGTCTTGAAATTGTAAGTATCGCTCCAGCAATTGCC
AAATGTATTGAAATTTATTCAGAGGGTACAGGTTCGATGTCGTTTGTACA
TGATGAAAATTCAAAAGTTTTATTTGCTAAAAAAATATATTAA


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