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Conserved domains on  [gi|12321304|gb|AAG50725|]
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phosphoribosyl-ATP pyrophosphohydrolase (At-IE) [Arabidopsis thaliana]

Protein Classification

PLN02346 family protein( domain architecture ID 11476673)

PLN02346 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 13-281 1.35e-169

histidine biosynthesis bifunctional protein hisIE


:

Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 469.69  E-value: 1.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   13 ARSSCFIPKPYSFRDTKLRSRSNVVFACNDNKNIALQAKVDNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALST 92
Cdd:PLN02346   1 PRSSVFSPASPCRRDRKISAASKAAAGSKTLAEPALEPKVESLLDSVKWDDKGLAVAIAQNVDTGAILMQGFANREAISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   93 TISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRDSIIYLGTPDGPTCHTGEETCYYTSVFDQLNNDEASGNKLA 172
Cdd:PLN02346  81 TISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLDCDRDSIIYLGTPDGPTCHTGAETCYYTSVDDALQNGGPHGNKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  173 LTTLYSLESIISKRKEEStVPQEGKPSWTRRLLTDDALLCSKIREEADELCRTLEDNEEVSRTPSEMADVLYHAMVLLSK 252
Cdd:PLN02346 161 LTTLYSLEETIQQRKEEA-VPQGGKPSWTKRLLQDPELLCSKIREEAGELCQTLEENEGKERTASEMADVLYHAMVLLAK 239

                        250       260
                 ....*....|....*....|....*....
gi 12321304  253 RGVKMEDVLEVLRKRFSQSGIEEKQNRTK 281
Cdd:PLN02346 240 QGVKMEDVLEVLRKRFSQSGIEEKASRPP 268
 
Name Accession Description Interval E-value
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 13-281 1.35e-169

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 469.69  E-value: 1.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   13 ARSSCFIPKPYSFRDTKLRSRSNVVFACNDNKNIALQAKVDNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALST 92
Cdd:PLN02346   1 PRSSVFSPASPCRRDRKISAASKAAAGSKTLAEPALEPKVESLLDSVKWDDKGLAVAIAQNVDTGAILMQGFANREAISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   93 TISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRDSIIYLGTPDGPTCHTGEETCYYTSVFDQLNNDEASGNKLA 172
Cdd:PLN02346  81 TISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLDCDRDSIIYLGTPDGPTCHTGAETCYYTSVDDALQNGGPHGNKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  173 LTTLYSLESIISKRKEEStVPQEGKPSWTRRLLTDDALLCSKIREEADELCRTLEDNEEVSRTPSEMADVLYHAMVLLSK 252
Cdd:PLN02346 161 LTTLYSLEETIQQRKEEA-VPQGGKPSWTKRLLQDPELLCSKIREEAGELCQTLEENEGKERTASEMADVLYHAMVLLAK 239

                        250       260
                 ....*....|....*....|....*....
gi 12321304  253 RGVKMEDVLEVLRKRFSQSGIEEKQNRTK 281
Cdd:PLN02346 240 QGVKMEDVLEVLRKRFSQSGIEEKASRPP 268
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 53-155 2.74e-52

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: 166.02  E-value: 2.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  53 DNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRD 132
Cdd:COG0139   3 EGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCDGD 82

                        90       100
                ....*....|....*....|...
gi 12321304 133 SIIYLGTPDGPTCHTGEETCYYT 155
Cdd:COG0139  83 ALLLKVEQIGPACHTGRRSCFYR 105
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 81-154 4.18e-37

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: 126.31  E-value: 4.18e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12321304    81 MQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRDSIIYLGTPDGPTCHTGEETCYY 154
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCFY 74
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 176-264 2.54e-23

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: 90.60  E-value: 2.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304 176 LYSLESIISKRKEEstvPQEGkpSWTRRLLTD-DALLCSKIREEADELCRTLEdNEEVSRTPSEMADVLYHAMVLLSKRG 254
Cdd:cd11534   1 LEELEAVIEDRKEA---PPEG--SYTAKLLEKgLDKILKKVGEEAVEVIIAAK-NGDKEELVYEAADLLYHLLVLLAYRG 74

                        90
                ....*....|
gi 12321304 255 VKMEDVLEVL 264
Cdd:cd11534  75 ISLEDVLEEL 84
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 176-264 5.82e-19

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: 79.07  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   176 LYSLESIISKRKEEStvPQEgkpSWTRRLLTD-DALLCSKIREEADELCRTL--EDNEEVSrtpSEMADVLYHAMVLLSK 252
Cdd:TIGR03188   1 LEELEATIAERKAAD--PEG---SYTARLFAKgLDKILKKVGEEAVEVIIAAknGDKEELV---YEAADLLYHLLVLLAA 72

                          90
                  ....*....|..
gi 12321304   253 RGVKMEDVLEVL 264
Cdd:TIGR03188  73 QGVSLEDVLAEL 84
 
Name Accession Description Interval E-value
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 13-281 1.35e-169

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 469.69  E-value: 1.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   13 ARSSCFIPKPYSFRDTKLRSRSNVVFACNDNKNIALQAKVDNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALST 92
Cdd:PLN02346   1 PRSSVFSPASPCRRDRKISAASKAAAGSKTLAEPALEPKVESLLDSVKWDDKGLAVAIAQNVDTGAILMQGFANREAISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   93 TISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRDSIIYLGTPDGPTCHTGEETCYYTSVFDQLNNDEASGNKLA 172
Cdd:PLN02346  81 TISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLDCDRDSIIYLGTPDGPTCHTGAETCYYTSVDDALQNGGPHGNKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  173 LTTLYSLESIISKRKEEStVPQEGKPSWTRRLLTDDALLCSKIREEADELCRTLEDNEEVSRTPSEMADVLYHAMVLLSK 252
Cdd:PLN02346 161 LTTLYSLEETIQQRKEEA-VPQGGKPSWTKRLLQDPELLCSKIREEAGELCQTLEENEGKERTASEMADVLYHAMVLLAK 239

                        250       260
                 ....*....|....*....|....*....
gi 12321304  253 RGVKMEDVLEVLRKRFSQSGIEEKQNRTK 281
Cdd:PLN02346 240 QGVKMEDVLEVLRKRFSQSGIEEKASRPP 268
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
53-268 1.90e-68

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 210.79  E-value: 1.90e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   53 DNLLDRIKWDDK-GLAVAIAQNVDTGAVLMQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDR 131
Cdd:PRK02759   2 EQQIEELDFDKNdGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  132 DSIIYLGTPDGPTCHTGEETCYYtsvfdqlnndEASGNKLALTTLYSLESIISKRKEEstvPQEGkpSWTRRLLT--DDA 209
Cdd:PRK02759  82 DTLLVLVEPIGPACHTGTRSCFY----------REKKAAPPWDFLSQLEQLIAERKNA---PPEG--SYTAKLFAsgTKR 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12321304  210 LLcSKIREEADE--LCRTLEDNEEVSrtpSEMADVLYHAMVLLSKRGVKMEDVLEVLRKRF 268
Cdd:PRK02759 147 IA-QKVGEEAVEvvLAAKNNDKEELI---NEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 53-155 2.74e-52

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: 166.02  E-value: 2.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  53 DNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRD 132
Cdd:COG0139   3 EGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCDGD 82

                        90       100
                ....*....|....*....|...
gi 12321304 133 SIIYLGTPDGPTCHTGEETCYYT 155
Cdd:COG0139  83 ALLLKVEQIGPACHTGRRSCFYR 105
hisI PRK00051
phosphoribosyl-AMP cyclohydrolase; Reviewed
 53-161 4.22e-41

phosphoribosyl-AMP cyclohydrolase; Reviewed


Pssm-ID: 234598  Cd Length: 125  Bit Score: 138.10  E-value: 4.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   53 DNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRD 132
Cdd:PRK00051   1 PKILDRLKFDADGLVPAIAQDAETGEVLMVAWMNEEALAKTLETGRAHYWSRSRQKLWRKGETSGHVQKVHEVRLDCDGD 80

                         90       100
                 ....*....|....*....|....*....
gi 12321304  133 SIIYLGTPDGPTCHTGEETCYYTSVFDQL 161
Cdd:PRK00051  81 AVLLKVEQVGAACHTGRRSCFYRKLEGGL 109
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 81-154 4.18e-37

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: 126.31  E-value: 4.18e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12321304    81 MQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRDSIIYLGTPDGPTCHTGEETCYY 154
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCFY 74
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 174-279 2.82e-25

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: 96.35  E-value: 2.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304 174 TTLYSLESIISKRKEEstvPQEGkpSWTRRLLT--DDALLcSKIREEADELCR--TLEDNEEVsrtPSEMADVLYHAMVL 249
Cdd:COG0140   3 DVLDELEAVIEERKAA---DPEG--SYTAKLFAkgIDKIL-KKVGEEAVEVVIaaKNGDKEEL---IYEAADLLYHLLVL 73

                        90       100       110
                ....*....|....*....|....*....|
gi 12321304 250 LSKRGVKMEDVLEVLRKRFSQSGIEEKQNR 279
Cdd:COG0140  74 LAARGISLDDVLAELARRHGLSGLEEKASR 103
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 176-264 2.54e-23

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: 90.60  E-value: 2.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304 176 LYSLESIISKRKEEstvPQEGkpSWTRRLLTD-DALLCSKIREEADELCRTLEdNEEVSRTPSEMADVLYHAMVLLSKRG 254
Cdd:cd11534   1 LEELEAVIEDRKEA---PPEG--SYTAKLLEKgLDKILKKVGEEAVEVIIAAK-NGDKEELVYEAADLLYHLLVLLAYRG 74

                        90
                ....*....|
gi 12321304 255 VKMEDVLEVL 264
Cdd:cd11534  75 ISLEDVLEEL 84
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
175-281 7.29e-22

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 87.52  E-value: 7.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304  175 TLYSLESIISKRKEEstvPQEGkpSWTRRLLT--DDALLcSKIREEADElcrTL-----EDNEEVSrtpSEMADVLYHAM 247
Cdd:PRK00400   4 TLERLAATIEERKGA---DPEG--SYTAKLLDkgLDKIL-KKVGEEATE---VViaakdGDREELV---YEIADLLYHLL 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 12321304  248 VLLSKRGVKMEDVLEVLRKRFSQSGIEEKQNRTK 281
Cdd:PRK00400  72 VLLAARGISLEDVLAELERREGLSGLEEKASRKI 105
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 176-264 5.82e-19

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: 79.07  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   176 LYSLESIISKRKEEStvPQEgkpSWTRRLLTD-DALLCSKIREEADELCRTL--EDNEEVSrtpSEMADVLYHAMVLLSK 252
Cdd:TIGR03188   1 LEELEATIAERKAAD--PEG---SYTARLFAKgLDKILKKVGEEAVEVIIAAknGDKEELV---YEAADLLYHLLVLLAA 72

                          90
                  ....*....|..
gi 12321304   253 RGVKMEDVLEVL 264
Cdd:TIGR03188  73 QGVSLEDVLAEL 84
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 175-267 4.71e-17

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: 74.24  E-value: 4.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304 175 TLYSLESIISKRKEEstvPQEGkpSWTRRLLTDDALLCSKIREEADELCRTlEDNEEVSrtpSEMADVLYHAMVLLSKRG 254
Cdd:cd11546   1 GLDALEATLTQRKQN---APPG--SYTARLFNDEKLLRAKIMEEAEELCEA-KTKDEVA---WEAADLLYFALVRCVAAG 71

                        90
                ....*....|...
gi 12321304 255 VKMEDVLEVLRKR 267
Cdd:cd11546  72 VSLDDVERELDRR 84
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 176-267 3.62e-11

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 58.01  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304   176 LYSLESIISKRKEEstvpqegKPSW-TRRLLTDdalLCSKIREEADELCRTLEDN--EEVSRtpsEMADVLYHAMVLLSK 252
Cdd:pfam01503   1 VREFHRTIGDRKPE-------TPEGsTAELAAL---RAAKIGEEAVELLEAAKAGdlAELAD---ELADLLYHTYGLLVL 67

                          90
                  ....*....|....*
gi 12321304   253 RGVKMEDVLEVLRKR 267
Cdd:pfam01503  68 QGVDLDAVFEEVHRA 82
NTP-PPase_COG4997 cd11532
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 194-272 4.55e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from archaea and bacteria; The family includes some uncharacterized hypothetical proteins from archaea and bacteria. Although their biological roles remain unclear, the family members show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, the family contains a single MazG-like domain.


Pssm-ID: 212139  Cd Length: 95  Bit Score: 35.60  E-value: 4.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12321304 194 QEGKPSWTRRLlTDDAL---LCSKIREEADELcrtLEDNEEVSrtPSEMADVL---YHamvLLSKRGVKMEDVLEVLRKR 267
Cdd:cd11532  15 ASGKTCVTRIL-SDEEYleaLKKKLVEEAAEY---AEAKTEDS--LEELADLLeviYA---IAEAHGISLEELEKVREKK 85


                ....*
gi 12321304 268 FSQSG 272
Cdd:cd11532  86 REERG 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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