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Conserved domains on  [gi|1801989507|gb|QHO82124|]
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bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE [Enterobacter hormaechei]

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;
3-202 3.14e-137

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


:

Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 381.82  E-value: 3.14e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   3 TEQQQAQLDWEKTDGLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDCD 82
Cdd:PRK02759    1 TEQQIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507  83 NDTLLVLVIPIGPTCHKGTSSCFGEA---SHQWLFLYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETAL 159
Cdd:PRK02759   81 NDTLLVLVEPIGPACHTGTRSCFYREkkaAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1801989507 160 AATVHDREELTNEASDLMYHLLVLLQDQELDLTAVIENLRKRH 202
Cdd:PRK02759  161 AAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
3-202 3.14e-137

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 381.82  E-value: 3.14e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   3 TEQQQAQLDWEKTDGLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDCD 82
Cdd:PRK02759    1 TEQQIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507  83 NDTLLVLVIPIGPTCHKGTSSCFGEA---SHQWLFLYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETAL 159
Cdd:PRK02759   81 NDTLLVLVEPIGPACHTGTRSCFYREkkaAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1801989507 160 AATVHDREELTNEASDLMYHLLVLLQDQELDLTAVIENLRKRH 202
Cdd:PRK02759  161 AAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 2-108 2.88e-65

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: 196.06  E-value: 2.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   2 LTEQQQAQLDWEKtDGLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDC 81
Cdd:COG0139     1 LEEGILDKLKFDE-DGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDC 79

                          90       100
                  ....*....|....*....|....*..
gi 1801989507  82 DNDTLLVLVIPIGPTCHKGTSSCFGEA 108
Cdd:COG0139    80 DGDALLLKVEQIGPACHTGRRSCFYRE 106
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 33-106 2.54e-49

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: 154.82  E-value: 2.54e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801989507  33 MLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDCDNDTLLVLVIPIGPTCHKGTSSCFG 106
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCFY 74
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 115-198 3.88e-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: 126.45  E-value: 3.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ....
gi 1801989507 195 IENL 198
Cdd:TIGR03188  81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 115-198 1.18e-36

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: 122.95  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:cd11534     1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                  ....
gi 1801989507 195 IENL 198
Cdd:cd11534    81 LEEL 84
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
3-202 3.14e-137

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 381.82  E-value: 3.14e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   3 TEQQQAQLDWEKTDGLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDCD 82
Cdd:PRK02759    1 TEQQIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507  83 NDTLLVLVIPIGPTCHKGTSSCFGEA---SHQWLFLYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETAL 159
Cdd:PRK02759   81 NDTLLVLVEPIGPACHTGTRSCFYREkkaAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1801989507 160 AATVHDREELTNEASDLMYHLLVLLQDQELDLTAVIENLRKRH 202
Cdd:PRK02759  161 AAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 2-108 2.88e-65

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: 196.06  E-value: 2.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   2 LTEQQQAQLDWEKtDGLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDC 81
Cdd:COG0139     1 LEEGILDKLKFDE-DGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDC 79

                          90       100
                  ....*....|....*....|....*..
gi 1801989507  82 DNDTLLVLVIPIGPTCHKGTSSCFGEA 108
Cdd:COG0139    80 DGDALLLKVEQIGPACHTGRRSCFYRE 106
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 2-201 5.49e-55

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 175.78  E-value: 5.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   2 LTEQQQAQLDWEKTD--GLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITP 79
Cdd:PLN02346   36 LEPKVESLLDSVKWDdkGLAVAIAQNVDTGAILMQGFANREAISATISSRKATFYSRSRSGLWTKGETSGNFINVHDIYL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507  80 DCDNDTLLVLVIPIGPTCHKGTSSCFGEASHQWLF-------------LYQLEQLLAERKSA----DPESSYTAKLYaSG 142
Cdd:PLN02346  116 DCDRDSIIYLGTPDGPTCHTGAETCYYTSVDDALQnggphgnklalttLYSLEETIQQRKEEavpqGGKPSWTKRLL-QD 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801989507 143 TKRIAQKVGEEGVEtaLAATVH---DREELTNEASDLMYHLLVLLQDQELDLTAVIENLRKR 201
Cdd:PLN02346  195 PELLCSKIREEAGE--LCQTLEeneGKERTASEMADVLYHAMVLLAKQGVKMEDVLEVLRKR 254
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 33-106 2.54e-49

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: 154.82  E-value: 2.54e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801989507  33 MLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDCDNDTLLVLVIPIGPTCHKGTSSCFG 106
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCFY 74
hisI PRK00051
phosphoribosyl-AMP cyclohydrolase; Reviewed
 8-105 1.13e-45

phosphoribosyl-AMP cyclohydrolase; Reviewed


Pssm-ID: 234598  Cd Length: 125  Bit Score: 147.35  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507   8 AQLDWEKtDGLLPVVVQHAVSGEVLMLGYMNQEALAKTLDSGKVTFFSRTKQRLWTKGETSGHFLNVVGITPDCDNDTLL 87
Cdd:PRK00051    5 DRLKFDA-DGLVPAIAQDAETGEVLMVAWMNEEALAKTLETGRAHYWSRSRQKLWRKGETSGHVQKVHEVRLDCDGDAVL 83

                          90
                  ....*....|....*...
gi 1801989507  88 VLVIPIGPTCHKGTSSCF 105
Cdd:PRK00051   84 LKVEQVGAACHTGRRSCF 101
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 114-203 1.63e-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: 146.04  E-value: 1.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 114 FLYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTA 193
Cdd:COG0140     4 VLDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGISLDD 83

                          90
                  ....*....|
gi 1801989507 194 VIENLRKRHK 203
Cdd:COG0140    84 VLAELARRHG 93
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 115-198 3.88e-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: 126.45  E-value: 3.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ....
gi 1801989507 195 IENL 198
Cdd:TIGR03188  81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 115-198 1.18e-36

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: 122.95  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:cd11534     1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                  ....
gi 1801989507 195 IENL 198
Cdd:cd11534    81 LEEL 84
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
115-203 1.58e-31

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 110.25  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:PRK00400    5 LERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGISLEDV 84


                  ....*....
gi 1801989507 195 IENLRKRHK 203
Cdd:PRK00400   85 LAELERREG 93
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 115-202 6.50e-24

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 90.37  E-value: 6.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSyTAKLYAsgtkRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:pfam01503   1 VREFHRTIGDRKPETPEGS-TAELAA----LRAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAV 75


                  ....*...
gi 1801989507 195 IENLRKRH 202
Cdd:pfam01503  76 FEEVHRAN 83
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 117-198 2.67e-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: 52.10  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 117 QLEQLLAERKSADPESSYTAKLYASGTKRIAQKVGEEGVETALAATVHDREELTNEASDLMYHLLVLLQDQELDLTAVIE 196
Cdd:cd11547     5 ELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLEDVYA 84


                  ..
gi 1801989507 197 NL 198
Cdd:cd11547    85 KL 86
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 115-201 4.81e-09

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: 51.51  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801989507 115 LYQLEQLLAERKSADPESSYTAKLYASgTKRIAQKVGEEGVETALAATvhdREELTNEASDLMYHLLVLLQDQELDLTAV 194
Cdd:cd11546     2 LDALEATLTQRKQNAPPGSYTARLFND-EKLLRAKIMEEAEELCEAKT---KDEVAWEAADLLYFALVRCVAAGVSLDDV 77


                  ....*..
gi 1801989507 195 IENLRKR 201
Cdd:cd11546    78 ERELDRR 84
 
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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