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

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;
11-210 2.25e-133

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


:

Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 372.57  E-value: 2.25e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  11 LAERINWEKVDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDNDT 90
Cdd:PRK02759   4 QIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDNDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  91 LLVKVNPIGPTCHLGNTTCWDVDPQEESQMVWLHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAAT 170
Cdd:PRK02759  84 LLVLVEPIGPACHTGTRSCFYREKKAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVLAAK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 519041094 171 SGDKAELVCESADLVYHLLVLLQDQGLSMNDVVNKLKERH 210
Cdd:PRK02759 164 NNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
11-210 2.25e-133

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 372.57  E-value: 2.25e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  11 LAERINWEKVDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDNDT 90
Cdd:PRK02759   4 QIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDNDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  91 LLVKVNPIGPTCHLGNTTCWDVDPQEESQMVWLHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAAT 170
Cdd:PRK02759  84 LLVLVEPIGPACHTGTRSCFYREKKAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVLAAK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 519041094 171 SGDKAELVCESADLVYHLLVLLQDQGLSMNDVVNKLKERH 210
Cdd:PRK02759 164 NNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 9-111 1.71e-62

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: 189.51  E-value: 1.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094   9 SSLAERINWEKvDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDN 88
Cdd:COG0139    3 EGILDKLKFDE-DGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCDG 81

                         90       100
                 ....*....|....*....|...
gi 519041094  89 DTLLVKVNPIGPTCHLGNTTCWD 111
Cdd:COG0139   82 DALLLKVEQIGPACHTGRRSCFY 104
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 38-110 6.28e-47

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: 149.04  E-value: 6.28e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519041094   38 MMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDNDTLLVKVNPIGPTCHLGNTTCW 110
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCF 73
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 123-206 1.99e-40

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: 132.61  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  123 LHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ....
gi 519041094  203 VNKL 206
Cdd:TIGR03188  81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 123-206 8.23e-38

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: 126.03  E-value: 8.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094 123 LHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 519041094 203 VNKL 206
Cdd:cd11534   81 LEEL 84
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
11-210 2.25e-133

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 372.57  E-value: 2.25e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  11 LAERINWEKVDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDNDT 90
Cdd:PRK02759   4 QIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDNDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  91 LLVKVNPIGPTCHLGNTTCWDVDPQEESQMVWLHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAAT 170
Cdd:PRK02759  84 LLVLVEPIGPACHTGTRSCFYREKKAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVEVVLAAK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 519041094 171 SGDKAELVCESADLVYHLLVLLQDQGLSMNDVVNKLKERH 210
Cdd:PRK02759 164 NNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 9-111 1.71e-62

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: 189.51  E-value: 1.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094   9 SSLAERINWEKvDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDN 88
Cdd:COG0139    3 EGILDKLKFDE-DGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCDG 81

                         90       100
                 ....*....|....*....|...
gi 519041094  89 DTLLVKVNPIGPTCHLGNTTCWD 111
Cdd:COG0139   82 DALLLKVEQIGPACHTGRRSCFY 104
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 6-209 1.82e-51

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 167.31  E-value: 1.82e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094   6 AEVSSLAERINWEKvDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLD 85
Cdd:PLN02346  38 PKVESLLDSVKWDD-KGLAVAIAQNVDTGAILMQGFANREAISATISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  86 CDNDTLLVKVNPIGPTCHLGNTTCW----------DVDPQEESQMVWLHQLEQLLAARKSA----DPDSSYTASLYaRGT 151
Cdd:PLN02346 117 CDRDSIIYLGTPDGPTCHTGAETCYytsvddalqnGGPHGNKLALTTLYSLEETIQQRKEEavpqGGKPSWTKRLL-QDP 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519041094 152 KRISQKVGEEGVEvaLAAT---SGDKAELVCESADLVYHLLVLLQDQGLSMNDVVNKLKER 209
Cdd:PLN02346 196 ELLCSKIREEAGE--LCQTleeNEGKERTASEMADVLYHAMVLLAKQGVKMEDVLEVLRKR 254
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 38-110 6.28e-47

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: 149.04  E-value: 6.28e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519041094   38 MMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDNDTLLVKVNPIGPTCHLGNTTCW 110
Cdd:pfam01502   1 MLAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCF 73
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 123-211 1.04e-46

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: 149.51  E-value: 1.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094 123 LHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:COG0140    5 LDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGISLDDV 84


                 ....*....
gi 519041094 203 VNKLKERHK 211
Cdd:COG0140   85 LAELARRHG 93
hisI PRK00051
phosphoribosyl-AMP cyclohydrolase; Reviewed
 10-110 1.61e-46

phosphoribosyl-AMP cyclohydrolase; Reviewed


Pssm-ID: 234598  Cd Length: 125  Bit Score: 149.66  E-value: 1.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  10 SLAERINWEKvDGLVPAIVQDFQSSQVLMMGYMNQDALAKTGETGQVTFFSRTKQRLWTKGETSGNVLQLVNMQLDCDND 89
Cdd:PRK00051   2 KILDRLKFDA-DGLVPAIAQDAETGEVLMVAWMNEEALAKTLETGRAHYWSRSRQKLWRKGETSGHVQKVHEVRLDCDGD 80

                         90       100
                 ....*....|....*....|.
gi 519041094  90 TLLVKVNPIGPTCHLGNTTCW 110
Cdd:PRK00051  81 AVLLKVEQVGAACHTGRRSCF 101
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 123-206 1.99e-40

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: 132.61  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  123 LHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:TIGR03188   1 LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDV 80


                  ....
gi 519041094  203 VNKL 206
Cdd:TIGR03188  81 LAEL 84
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 123-206 8.23e-38

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: 126.03  E-value: 8.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094 123 LHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 519041094 203 VNKL 206
Cdd:cd11534   81 LEEL 84
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
123-211 4.39e-35

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 119.88  E-value: 4.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094 123 LHQLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:PRK00400   5 LERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGISLEDV 84


                 ....*....
gi 519041094 203 VNKLKERHK 211
Cdd:PRK00400  85 LAELERREG 93
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 123-210 2.78e-21

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 83.82  E-value: 2.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094  123 LHQLEQLLAARKSADPdSSYTASLYARgtkrISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:pfam01503   1 VREFHRTIGDRKPETP-EGSTAELAAL----RAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAV 75


                  ....*...
gi 519041094  203 VNKLKERH 210
Cdd:pfam01503  76 FEEVHRAN 83
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 125-206 1.26e-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: 53.26  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094 125 QLEQLLAARKSADPDSSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLVYHLLVLLQDQGLSMNDVVN 204
Cdd:cd11547    5 ELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLEDVYA 84


                 ..
gi 519041094 205 KL 206
Cdd:cd11547   85 KL 86
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 123-209 2.20e-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: 52.29  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519041094 123 LHQLEQLLAARKSADPDSSYTASLYARgTKRISQKVGEEGVEVALAATsgdKAELVCESADLVYHLLVLLQDQGLSMNDV 202
Cdd:cd11546    2 LDALEATLTQRKQNAPPGSYTARLFND-EKLLRAKIMEEAEELCEAKT---KDEVAWEAADLLYFALVRCVAAGVSLDDV 77


                 ....*..
gi 519041094 203 VNKLKER 209
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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