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Conserved domains on  [gi|1736465231|gb|KAA0885697|]
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phosphoribosyl-ATP diphosphatase [Corynebacterium amycolatum]

Protein Classification

phosphoribosyl-ATP diphosphatase( domain architecture ID 10183989)

phosphoribosyl-ATP diphosphatase (PRA-PH) catalyzes the hydrolysis of 1-(5-phosphoribosyl)-ATP to form 1-(5-phosphoribosyl)-AMP and diphosphate, which is the second step in the histidine biosynthetic pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 2-87 1.81e-41

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs; This family includes M. tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs. M. tuberculosis HisE is encoded by the hisE gene, which is a separate gene presenting in many bacteria and archaea but is fused to hisI in other bacteria, fungi and plants. HisE is responsible for the second step in the histidine-biosynthetic pathway. It can irreversibly hydrolyze phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate. HisE dimerizes into a four alpha-helix bundle, forming two inferred PRATP active sites on the outer faces. M. tuberculosis HisE has been found to be essential for growth in vitro, thus making it a potential drug target for tuberculosis.


:

Pssm-ID: 212154  Cd Length: 86  Bit Score: 130.68  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  2 KNFDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPE 81
Cdd:cd11547    1 KTFEELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLE 80


                 ....*.
gi 1736465231 82 DVYKYL 87
Cdd:cd11547   81 DVYAKL 86
 
Name Accession Description Interval E-value
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 2-87 1.81e-41

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs; This family includes M. tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs. M. tuberculosis HisE is encoded by the hisE gene, which is a separate gene presenting in many bacteria and archaea but is fused to hisI in other bacteria, fungi and plants. HisE is responsible for the second step in the histidine-biosynthetic pathway. It can irreversibly hydrolyze phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate. HisE dimerizes into a four alpha-helix bundle, forming two inferred PRATP active sites on the outer faces. M. tuberculosis HisE has been found to be essential for growth in vitro, thus making it a potential drug target for tuberculosis.


Pssm-ID: 212154  Cd Length: 86  Bit Score: 130.68  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  2 KNFDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPE 81
Cdd:cd11547    1 KTFEELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLE 80


                 ....*.
gi 1736465231 82 DVYKYL 87
Cdd:cd11547   81 DVYAKL 86
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
1-87 2.61e-40

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 127.97  E-value: 2.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231   1 MKNFDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSP 80
Cdd:PRK00400    2 MDTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGISL 81


                  ....*..
gi 1736465231  81 EDVYKYL 87
Cdd:PRK00400   82 EDVLAEL 88
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 4-87 4.83e-27

phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, catalyses the second step in the histidine biosynthesis pathway. It often occurs as a fusion protein. This model a somewhat narrower scope than pfam01503, as some paralogs that appear to be functionally distinct are excluded from this model. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 274477  Cd Length: 84  Bit Score: 94.09  E-value: 4.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  4 FDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:TIGR03188  1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                 ....
gi 1736465231 84 YKYL 87
Cdd:TIGR03188 81 LAEL 84
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 4-87 6.80e-17

Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-ATP pyrophosphohydrolase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439910  Cd Length: 103  Bit Score: 68.62  E-value: 6.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231   4 FDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:COG0140     5 LDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGISLDDV 84


                  ....
gi 1736465231  84 YKYL 87
Cdd:COG0140    85 LAEL 88
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 11-85 1.55e-05

Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the histidine biosynthetic pathway.


Pssm-ID: 426294  Cd Length: 83  Bit Score: 39.14  E-value: 1.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736465231 11 LKEKAQSRPDGSGtvkalDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDVYK 85
Cdd:pfam01503  8 IGDRKPETPEGST-----AELAALRAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAVFE 77
 
Name Accession Description Interval E-value
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 2-87 1.81e-41

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs; This family includes M. tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs. M. tuberculosis HisE is encoded by the hisE gene, which is a separate gene presenting in many bacteria and archaea but is fused to hisI in other bacteria, fungi and plants. HisE is responsible for the second step in the histidine-biosynthetic pathway. It can irreversibly hydrolyze phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate. HisE dimerizes into a four alpha-helix bundle, forming two inferred PRATP active sites on the outer faces. M. tuberculosis HisE has been found to be essential for growth in vitro, thus making it a potential drug target for tuberculosis.


Pssm-ID: 212154  Cd Length: 86  Bit Score: 130.68  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  2 KNFDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPE 81
Cdd:cd11547    1 KTFEELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLE 80


                 ....*.
gi 1736465231 82 DVYKYL 87
Cdd:cd11547   81 DVYAKL 86
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
1-87 2.61e-40

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 127.97  E-value: 2.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231   1 MKNFDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSP 80
Cdd:PRK00400    2 MDTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGISL 81


                  ....*..
gi 1736465231  81 EDVYKYL 87
Cdd:PRK00400   82 EDVLAEL 88
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 4-87 4.83e-27

phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, catalyses the second step in the histidine biosynthesis pathway. It often occurs as a fusion protein. This model a somewhat narrower scope than pfam01503, as some paralogs that appear to be functionally distinct are excluded from this model. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 274477  Cd Length: 84  Bit Score: 94.09  E-value: 4.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  4 FDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:TIGR03188  1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                 ....
gi 1736465231 84 YKYL 87
Cdd:TIGR03188 81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 4-87 2.15e-21

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase (HisIE or PRATP-PH) and its homologs; This family includes Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase, HisIE, and its homologs from all three kingdoms of life. E. coli HisIE is encoded by the hisIE gene, which is formed by hisE gene fused to hisl. HisIE is a bifunctional enzyme responsible for the second and third steps of the histidine-biosynthesis pathway. Its N-terminal and C-terminal domains have phosphoribosyl-AMP cyclohydrolase (HisI) and phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) activity, respectively. This family corresponds to the C-terminal domain of HisIE and includes many hisE gene encoding proteins, all of which show significant sequence similarity to Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH). These proteins may be responsible for only the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate.


Pssm-ID: 212141  Cd Length: 84  Bit Score: 79.81  E-value: 2.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  4 FDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 1736465231 84 YKYL 87
Cdd:cd11534   81 LEEL 84
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 4-87 6.80e-17

Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-ATP pyrophosphohydrolase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439910  Cd Length: 103  Bit Score: 68.62  E-value: 6.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231   4 FDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:COG0140     5 LDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGISLDDV 84


                  ....
gi 1736465231  84 YKYL 87
Cdd:COG0140    85 LAEL 88
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
4-87 1.30e-14

bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 65.18  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231   4 FDDLFAELKEKAQSRPDGSGTVKALDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:PRK02759  116 LSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDV 195


                  ....
gi 1736465231  84 YKYL 87
Cdd:PRK02759  196 IAEL 199
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 4-87 6.34e-06

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like fungal histidine biosynthesis trifunctional proteins and their homologs; This family includes fungal histidine biosynthesis trifunctional proteins and their homologs from eukaryotes and bacteria. Some family members contain three domains responsible for phosphoribosyl-AMP cyclohydrolase (PRAMP-CH), phosphoribosyl-ATP pyrophosphohydrolase (PRATP-PH), and histidinol dehydrogenase (Histidinol-DH) activity, respectively. Some others do not have Histidinol-DH domain, but have an additional N-terminal TIM phosphate binding domain. This family corresponds to the domain for PRATP-PH activity, which shows significant sequence similarity to Mycobacterium tuberculosis PRATP-PH that catalyzes the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate.


Pssm-ID: 212153  Cd Length: 84  Bit Score: 40.34  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736465231  4 FDDLFAELKEKAQSRPDGSGTvKALDAGVHFQGKKIVEEAGEVwlaAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDV 83
Cdd:cd11546    2 LDALEATLTQRKQNAPPGSYT-ARLFNDEKLLRAKIMEEAEEL---CEAKTKDEVAWEAADLLYFALVRCVAAGVSLDDV 77


                 ....
gi 1736465231 84 YKYL 87
Cdd:cd11546   78 EREL 81
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 11-85 1.55e-05

Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the histidine biosynthetic pathway.


Pssm-ID: 426294  Cd Length: 83  Bit Score: 39.14  E-value: 1.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736465231 11 LKEKAQSRPDGSGtvkalDAGVHFQGKKIVEEAGEVWLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDVYK 85
Cdd:pfam01503  8 IGDRKPETPEGST-----AELAALRAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAVFE 77
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 37-87 6.87e-05

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 39.42  E-value: 6.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1736465231  37 KKIVEEAGEV-WLAAEHESDEALAEEISQLLYWLQVVMVGRGLSPEDVYKYL 87
Cdd:PLN02346  200 SKIREEAGELcQTLEENEGKERTASEMADVLYHAMVLLAKQGVKMEDVLEVL 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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