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Conserved domains on  [gi|493017101|ref|WP_006094152|]
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MULTISPECIES: phosphoribosyl-ATP diphosphatase [Bacillus]

Protein Classification

phosphoribosyl-ATP diphosphatase( domain architecture ID 10011417)

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
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
1-96 6.17e-46

phosphoribosyl-ATP diphosphatase;


:

Pssm-ID: 179005  Cd Length: 105  Bit Score: 143.37  E-value: 6.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   1 MEDVLKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIP 80
Cdd:PRK00400   1 MMDTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGIS 80

                         90
                 ....*....|....*.
gi 493017101  81 LEDVLEEVKERQGKLS 96
Cdd:PRK00400  81 LEDVLAELERREGLSG 96
 
Name Accession Description Interval E-value
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
1-96 6.17e-46

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 143.37  E-value: 6.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   1 MEDVLKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIP 80
Cdd:PRK00400   1 MMDTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGIS 80

                         90
                 ....*....|....*.
gi 493017101  81 LEDVLEEVKERQGKLS 96
Cdd:PRK00400  81 LEDVLAELERREGLSG 96
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 1-94 3.74e-45

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: 141.03  E-value: 3.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   1 MEDVLKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIP 80
Cdd:COG0140    1 MSDVLDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGIS 80

                         90
                 ....*....|....
gi 493017101  81 LEDVLEEVKERQGK 94
Cdd:COG0140   81 LDDVLAELARRHGL 94
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 5-87 6.45e-39

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: 124.88  E-value: 6.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   5 LKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ...
gi 493017101  85 LEE 87
Cdd:cd11534   81 LEE 83
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 5-87 5.92e-38

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: 122.21  E-value: 5.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101    5 LKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ...
gi 493017101   85 LEE 87
Cdd:TIGR03188  81 LAE 83
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 5-91 1.29e-20

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 78.43  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101    5 LKSLYETIEQRKESPISESyTNYLFTKgedkILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:pfam01503   1 VREFHRTIGDRKPETPEGS-TAELAAL----RAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAV 75


                  ....*..
gi 493017101   85 LEEVKER 91
Cdd:pfam01503  76 FEEVHRA 82
 
Name Accession Description Interval E-value
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
1-96 6.17e-46

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 143.37  E-value: 6.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   1 MEDVLKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIP 80
Cdd:PRK00400   1 MMDTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGIS 80

                         90
                 ....*....|....*.
gi 493017101  81 LEDVLEEVKERQGKLS 96
Cdd:PRK00400  81 LEDVLAELERREGLSG 96
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 1-94 3.74e-45

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: 141.03  E-value: 3.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   1 MEDVLKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIP 80
Cdd:COG0140    1 MSDVLDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGIS 80

                         90
                 ....*....|....
gi 493017101  81 LEDVLEEVKERQGK 94
Cdd:COG0140   81 LDDVLAELARRHGL 94
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
3-91 9.13e-42

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 136.06  E-value: 9.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   3 DVLKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLE 82
Cdd:PRK02759 114 DFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLS 193


                 ....*....
gi 493017101  83 DVLEEVKER 91
Cdd:PRK02759 194 DVIAELKER 202
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 5-87 6.45e-39

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: 124.88  E-value: 6.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   5 LKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ...
gi 493017101  85 LEE 87
Cdd:cd11534   81 LEE 83
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 5-87 5.92e-38

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: 122.21  E-value: 5.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101    5 LKSLYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ...
gi 493017101   85 LEE 87
Cdd:TIGR03188  81 LAE 83
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 5-91 1.29e-20

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 78.43  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101    5 LKSLYETIEQRKESPISESyTNYLFTKgedkILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:pfam01503   1 VREFHRTIGDRKPETPEGS-TAELAAL----RAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAV 75


                  ....*..
gi 493017101   85 LEEVKER 91
Cdd:pfam01503  76 FEEVHRA 82
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 5-94 6.55e-17

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 73.32  E-value: 6.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   5 LKSLYETIEQRKESPISE----SYTNYLFtkgEDKIL--KKIGEECTEVV-IAAKNDDKEELIKEMVDVIYHCFVLLAAK 77
Cdd:PLN02346 164 LYSLEETIQQRKEEAVPQggkpSWTKRLL---QDPELlcSKIREEAGELCqTLEENEGKERTASEMADVLYHAMVLLAKQ 240

                         90
                 ....*....|....*..
gi 493017101  78 NIPLEDVLEEVKERQGK 94
Cdd:PLN02346 241 GVKMEDVLEVLRKRFSQ 257
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 5-91 1.99e-11

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: 54.98  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017101   5 LKSLYETIEQRKESPISESYTNYLFTKgEDKILKKIGEECTEVVIAaknDDKEELIKEMVDVIYHCFVLLAAKNIPLEDV 84
Cdd:cd11546    2 LDALEATLTQRKQNAPPGSYTARLFND-EKLLRAKIMEEAEELCEA---KTKDEVAWEAADLLYFALVRCVAAGVSLDDV 77


                 ....*..
gi 493017101  85 LEEVKER 91
Cdd:cd11546   78 ERELDRR 84
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 8-86 7.40e-09

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: 48.64  E-value: 7.40e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493017101   8 LYETIEQRKESPISESYTNYLFTKGEDKILKKIGEECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDVLE 86
Cdd:cd11547    6 LFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLEDVYA 84
NTP-PPase_DR2231 cd11544
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 42-105 6.25e-05

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs; This family corresponds to the DR2231 protein, a MazG-like NTP-PPase from Deinococcus radiodurans, and its bacterial homologs. All family members contain a well-conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for all-alpha-helical NTP-PPase superfamily. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It might be an evolutionary precursor of dimeric dUTPases with very high specificity in hydrolyzing dUTP into dUMP, but an inability to hydrolyze dTTP, a typical feature of dUTPases. Moreover, unlike the dUPase monomer containing a single active site, the DR2231 protein dimer holds two putative active sites.


Pssm-ID: 212151  Cd Length: 116  Bit Score: 39.05  E-value: 6.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493017101  42 EECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDVLEEVkeRQGKLSKTGERKEID 105
Cdd:cd11544   37 EEAAEVRAAIDHGDLVPLAHELADLLYVTYGTALQYGIDLDAVFAEV--HRANLTKASGPRRAD 98
NTP-PPase_DR2231_like cd11530
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 42-88 2.15e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs; This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD.


Pssm-ID: 212137  Cd Length: 88  Bit Score: 36.87  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 493017101  42 EECTEVVIAAKNDDKEELIKEMVDVIYHCFVLLAAKNIPLEDVLEEV 88
Cdd:cd11530   35 EELAELAEALKKGDMVELADALADLLYVAYGTAVEHGIDLDAAFAEV 81
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 36-90 5.39e-03

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 32.95  E-value: 5.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 493017101   36 ILKKIGEECTEVVIAAKNDDKEELIKEMVD----VIYHCFVLLAAKNIPLEDVLEEVKE 90
Cdd:pfam03819   6 LLPYLIEEVYEVAEAIEKEDLDNLEEELGDvllqVLFHANIAEEEGGFDLEDVFQRILE 64
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 42-90 5.57e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 33.64  E-value: 5.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493017101  42 EECTEVVIAAKNDDKEELIKEMVD----VIYHCFVLLAAKNIPLEDVLEEVKE 90
Cdd:cd11528   33 EEAYELVEAIEEGDPDNLREELGDvllqVLFHAQIAEEEGAFDLDDVIDGLTE 85
 
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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