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MULTISPECIES: bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE [Paenibacillus]

Protein Classification

bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase( domain architecture ID 11479841)

bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase catalyzes the irreversible hydrolysis of phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate, and the hydrolysis of the adenine ring of PRAMP, the second and third steps in histidine biosynthesis, respectively

EC:  3.5.4.19|3.6.1.31
Gene Ontology:  GO:0005737|GO:0005524|GO:0004635|GO:0004636|GO:0000105

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
2-220 1.01e-128

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


:

Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 361.40  E-value: 1.01e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   2 TGIQLDSIRYDSQ-GLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCD 80
Cdd:PRK02759   1 TEQQIEELDFDKNdGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  81 ADTLLVLAEQTGPACHTGSYTCFGSEIPvagadsaetgepaavtaSADRFGILSRLESVIASREAERPEGAYTTYLFEKG 160
Cdd:PRK02759  81 NDTLLVLVEPIGPACHTGTRSCFYREKK-----------------AAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASG 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 161 IDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDVMAELERRH 220
Cdd:PRK02759 144 TKRIAQKVGEEAVEVVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
2-220 1.01e-128

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 361.40  E-value: 1.01e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   2 TGIQLDSIRYDSQ-GLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCD 80
Cdd:PRK02759   1 TEQQIEELDFDKNdGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  81 ADTLLVLAEQTGPACHTGSYTCFGSEIPvagadsaetgepaavtaSADRFGILSRLESVIASREAERPEGAYTTYLFEKG 160
Cdd:PRK02759  81 NDTLLVLVEPIGPACHTGTRSCFYREKK-----------------AAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASG 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 161 IDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDVMAELERRH 220
Cdd:PRK02759 144 TKRIAQKVGEEAVEVVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 1-103 7.67e-72

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


Pssm-ID: 439909  Cd Length: 106  Bit Score: 213.78  E-value: 7.67e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   1 MTGIQLDSIRYDSQGLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCD 80
Cdd:COG0139    1 LEEGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCD 80

                         90       100
                 ....*....|....*....|...
gi 497362623  81 ADTLLVLAEQTGPACHTGSYTCF 103
Cdd:COG0139   81 GDALLLKVEQIGPACHTGRRSCF 103
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 31-104 2.32e-54

Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine biosynthetic pathway. It requires Zn ions for activity.


Pssm-ID: 460233 [Multi-domain]  Cd Length: 74  Bit Score: 168.30  E-value: 2.32e-54
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497362623   31 MLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCDADTLLVLAEQTGPACHTGSYTCFG 104
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCFY 74
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 133-216 6.78e-41

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: 134.54  E-value: 6.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  133 LSRLESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDV 212
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ....
gi 497362623  213 MAEL 216
Cdd:TIGR03188  81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 133-216 1.00e-40

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: 134.12  E-value: 1.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 133 LSRLESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDV 212
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 497362623 213 MAEL 216
Cdd:cd11534   81 LEEL 84
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
2-220 1.01e-128

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 361.40  E-value: 1.01e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   2 TGIQLDSIRYDSQ-GLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCD 80
Cdd:PRK02759   1 TEQQIEELDFDKNdGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  81 ADTLLVLAEQTGPACHTGSYTCFGSEIPvagadsaetgepaavtaSADRFGILSRLESVIASREAERPEGAYTTYLFEKG 160
Cdd:PRK02759  81 NDTLLVLVEPIGPACHTGTRSCFYREKK-----------------AAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASG 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 161 IDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDVMAELERRH 220
Cdd:PRK02759 144 TKRIAQKVGEEAVEVVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 1-103 7.67e-72

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


Pssm-ID: 439909  Cd Length: 106  Bit Score: 213.78  E-value: 7.67e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   1 MTGIQLDSIRYDSQGLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCD 80
Cdd:COG0139    1 LEEGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCD 80

                         90       100
                 ....*....|....*....|...
gi 497362623  81 ADTLLVLAEQTGPACHTGSYTCF 103
Cdd:COG0139   81 GDALLLKVEQIGPACHTGRRSCF 103
hisI PRK00051
phosphoribosyl-AMP cyclohydrolase; Reviewed
 6-123 7.10e-60

phosphoribosyl-AMP cyclohydrolase; Reviewed


Pssm-ID: 234598  Cd Length: 125  Bit Score: 183.94  E-value: 7.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   6 LDSIRYDSQGLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCDADTLL 85
Cdd:PRK00051   4 LDRLKFDADGLVPAIAQDAETGEVLMVAWMNEEALAKTLETGRAHYWSRSRQKLWRKGETSGHVQKVHEVRLDCDGDAVL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 497362623  86 VLAEQTGPACHTGSYTCFGSEIP--VAGADSAETGEPAAV 123
Cdd:PRK00051  84 LKVEQVGAACHTGRRSCFYRKLEggLWVTVDPVLFDPDEV 123
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 31-104 2.32e-54

Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine biosynthetic pathway. It requires Zn ions for activity.


Pssm-ID: 460233 [Multi-domain]  Cd Length: 74  Bit Score: 168.30  E-value: 2.32e-54
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497362623   31 MLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCDADTLLVLAEQTGPACHTGSYTCFG 104
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCFY 74
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 6-219 7.09e-53

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 171.16  E-value: 7.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623   6 LDSIRYDSQGLVPAIVQDAISKDVLMLAYMNKESLEKTVATGTTWFWSRSRQELWNKGATSGHTQRVVSLRYDCDADTLL 85
Cdd:PLN02346  44 LDSVKWDDKGLAVAIAQNVDTGAILMQGFANREAISATISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLDCDRDSII 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  86 VLAEQTGPACHTGSYTCFGSEIPVAGADSAETGEPAAVTAsadrfgiLSRLESVIASREAER----PEGAYTTYLFEkgi 161
Cdd:PLN02346 124 YLGTPDGPTCHTGAETCYYTSVDDALQNGGPHGNKLALTT-------LYSLEETIQQRKEEAvpqgGKPSWTKRLLQ--- 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497362623 162 DKIL--KKVGEETAEVI-IAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDVMAELERR 219
Cdd:PLN02346 194 DPELlcSKIREEAGELCqTLEENEGKERTASEMADVLYHAMVLLAKQGVKMEDVLEVLRKR 254
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 130-220 4.48e-49

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: 156.06  E-value: 4.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 130 FGILSRLESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPL 209
Cdd:COG0140    2 SDVLDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGISL 81

                         90
                 ....*....|.
gi 497362623 210 DDVMAELERRH 220
Cdd:COG0140   82 DDVLAELARRH 92
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
132-220 4.79e-43

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 140.68  E-value: 4.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 132 ILSRLESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDD 211
Cdd:PRK00400   4 TLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGISLED 83


                 ....*....
gi 497362623 212 VMAELERRH 220
Cdd:PRK00400  84 VLAELERRE 92
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 133-216 6.78e-41

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: 134.54  E-value: 6.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  133 LSRLESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDV 212
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ....
gi 497362623  213 MAEL 216
Cdd:TIGR03188  81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 133-216 1.00e-40

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: 134.12  E-value: 1.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 133 LSRLESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDV 212
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 497362623 213 MAEL 216
Cdd:cd11534   81 LEEL 84
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 133-220 1.15e-19

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 79.97  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623  133 LSRLESVIASREAERPEGaYTTYLFekgiDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDV 212
Cdd:pfam01503   1 VREFHRTIGDRKPETPEG-STAELA----ALRAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAV 75


                  ....*...
gi 497362623  213 MAELERRH 220
Cdd:pfam01503  76 FEEVHRAN 83
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 136-216 1.07e-13

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: 64.43  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 136 LESVIASREAERPEGAYTTYLFEKGIDKILKKVGEETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDVMAE 215
Cdd:cd11547    6 LFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLEDVYAK 85


                 .
gi 497362623 216 L 216
Cdd:cd11547   86 L 86
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 133-219 8.38e-12

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: 59.22  E-value: 8.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497362623 133 LSRLESVIASREAERPEGAYTTYLFEKgiDKILK-KVGEETAEVIIAaknRDHDELRYETSDLIFHLMVLLRESKLPLDD 211
Cdd:cd11546    2 LDALEATLTQRKQNAPPGSYTARLFND--EKLLRaKIMEEAEELCEA---KTKDEVAWEAADLLYFALVRCVAAGVSLDD 76


                 ....*...
gi 497362623 212 VMAELERR 219
Cdd:cd11546   77 VERELDRR 84
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 170-220 6.95e-04

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: 38.26  E-value: 6.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497362623 170 EETAEVIIAAKNRDHDELRYETSDL----IFHLMVLLRESKLPLDDVMAELE----RRH 220
Cdd:cd11528   33 EEAYELVEAIEEGDPDNLREELGDVllqvLFHAQIAEEEGAFDLDDVIDGLTekliRRH 91
NTP-PPase_DR2231 cd11544
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 170-223 5.78e-03

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: 35.59  E-value: 5.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497362623 170 EETAEVIIAAKNRDHDELRYETSDLIFHLMVLLRESKLPLDDVMAELERRHMSK 223
Cdd:cd11544   37 EEAAEVRAAIDHGDLVPLAHELADLLYVTYGTALQYGIDLDAVFAEVHRANLTK 90
 
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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