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

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;
1-205 2.17e-118

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


:

Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 334.44  E-value: 2.17e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   1 MIKADELTFNE-AGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQ 79
Cdd:PRK02759   2 EQQIEELDFDKnDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  80 DALIVLVEPAGPACHKGSYSCFSPGEhirqTDGGRFDIINELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAE 159
Cdd:PRK02759  82 DTLLVLVEPIGPACHTGTRSCFYREK----KAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489277922 160 VIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLGVLKERH 205
Cdd:PRK02759 158 VVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
1-205 2.17e-118

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 334.44  E-value: 2.17e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   1 MIKADELTFNE-AGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQ 79
Cdd:PRK02759   2 EQQIEELDFDKnDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  80 DALIVLVEPAGPACHKGSYSCFSPGEhirqTDGGRFDIINELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAE 159
Cdd:PRK02759  82 DTLLVLVEPIGPACHTGTRSCFYREK----KAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489277922 160 VIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLGVLKERH 205
Cdd:PRK02759 158 VVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 1-101 1.98e-71

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: 212.24  E-value: 1.98e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   1 MIKADELTFNEAGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQD 80
Cdd:COG0139    3 EGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCDGD 82

                         90       100
                 ....*....|....*....|.
gi 489277922  81 ALIVLVEPAGPACHKGSYSCF 101
Cdd:COG0139   83 ALLLKVEQIGPACHTGRRSCF 103
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 30-101 1.05e-52

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: 163.68  E-value: 1.05e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489277922   30 LAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQDALIVLVEPAGPACHKGSYSCF 101
Cdd:pfam01502   2 LAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCF 73
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 118-201 6.55e-27

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: 98.30  E-value: 6.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922 118 INELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDV 197
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 489277922 198 LGVL 201
Cdd:cd11534   81 LEEL 84
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 120-201 7.23e-27

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: 97.94  E-value: 7.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  120 ELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLG 199
Cdd:TIGR03188   3 ELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDVLA 82


                  ..
gi 489277922  200 VL 201
Cdd:TIGR03188  83 EL 84
 
Name Accession Description Interval E-value
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
1-205 2.17e-118

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


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 334.44  E-value: 2.17e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   1 MIKADELTFNE-AGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQ 79
Cdd:PRK02759   2 EQQIEELDFDKnDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQKVVSIRLDCDN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  80 DALIVLVEPAGPACHKGSYSCFSPGEhirqTDGGRFDIINELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAE 159
Cdd:PRK02759  82 DTLLVLVEPIGPACHTGTRSCFYREK----KAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLFASGTKRIAQKVGEEAVE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489277922 160 VIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLGVLKERH 205
Cdd:PRK02759 158 VVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH 203
HisI1 COG0139
Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-AMP ...
 1-101 1.98e-71

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: 212.24  E-value: 1.98e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   1 MIKADELTFNEAGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQD 80
Cdd:COG0139    3 EGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQKVKEIRLDCDGD 82

                         90       100
                 ....*....|....*....|.
gi 489277922  81 ALIVLVEPAGPACHKGSYSCF 101
Cdd:COG0139   83 ALLLKVEQIGPACHTGRRSCF 103
hisI PRK00051
phosphoribosyl-AMP cyclohydrolase; Reviewed
 1-101 2.06e-58

phosphoribosyl-AMP cyclohydrolase; Reviewed


Pssm-ID: 234598  Cd Length: 125  Bit Score: 179.70  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   1 MIKADELTFNEAGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQD 80
Cdd:PRK00051   1 PKILDRLKFDADGLVPAIAQDAETGEVLMVAWMNEEALAKTLETGRAHYWSRSRQKLWRKGETSGHVQKVHEVRLDCDGD 80

                         90       100
                 ....*....|....*....|.
gi 489277922  81 ALIVLVEPAGPACHKGSYSCF 101
Cdd:PRK00051  81 AVLLKVEQVGAACHTGRRSCF 101
PRA-CH pfam01502
Phosphoribosyl-AMP cyclohydrolase; This enzyme catalyzes the third step in the histidine ...
 30-101 1.05e-52

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: 163.68  E-value: 1.05e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489277922   30 LAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQDALIVLVEPAGPACHKGSYSCF 101
Cdd:pfam01502   2 LAYMNREALEKTLETGRATYWSRSRQRLWHKGETSGNTQKVVEIRLDCDGDALLLKVEQKGPACHTGTRSCF 73
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 4-204 2.36e-42

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 143.81  E-value: 2.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922   4 ADELTFNEAGLIPAIVQDAASKEVLTLAYMNKESFEKTLETKETWFFSRSRGELWHKGATSGNIQRVKDIRLDCDQDALI 83
Cdd:PLN02346  44 LDSVKWDDKGLAVAIAQNVDTGAILMQGFANREAISATISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLDCDRDSII 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  84 VLVEPAGPACHKGSYSC-FSPGEHIRQTDGGRFD-----IINELETVIAKRQAEM----PEGAYTTYLFREgvDKIL-KK 152
Cdd:PLN02346 124 YLGTPDGPTCHTGAETCyYTSVDDALQNGGPHGNklaltTLYSLEETIQQRKEEAvpqgGKPSWTKRLLQD--PELLcSK 201

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489277922 153 VGEEAAEVI-IAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLGVLKER 204
Cdd:PLN02346 202 IREEAGELCqTLEENEGKERTASEMADVLYHAMVLLAKQGVKMEDVLEVLRKR 254
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 115-209 2.42e-33

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: 115.22  E-value: 2.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922 115 FDIINELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPL 194
Cdd:COG0140    2 SDVLDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHLLVLLAARGISL 81

                         90
                 ....*....|....*
gi 489277922 195 DDVLGVLKERHEGSE 209
Cdd:COG0140   82 DDVLAELARRHGLSG 96
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 118-201 6.55e-27

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: 98.30  E-value: 6.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922 118 INELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDV 197
Cdd:cd11534    1 LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAYRGISLEDV 80


                 ....
gi 489277922 198 LGVL 201
Cdd:cd11534   81 LEEL 84
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 120-201 7.23e-27

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: 97.94  E-value: 7.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  120 ELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLG 199
Cdd:TIGR03188   3 ELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLLAAQGVSLEDVLA 82


                  ..
gi 489277922  200 VL 201
Cdd:TIGR03188  83 EL 84
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
116-205 3.32e-25

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 94.45  E-value: 3.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922 116 DIINELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLD 195
Cdd:PRK00400   3 DTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHLLVLLAARGISLE 82

                         90
                 ....*....|
gi 489277922 196 DVLGVLKERH 205
Cdd:PRK00400  83 DVLAELERRE 92
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 120-205 3.28e-13

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 62.64  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277922  120 ELETVIAKRQAEMPEGaYTTYLFREgvdkILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDVLG 199
Cdd:pfam01503   3 EFHRTIGDRKPETPEG-STAELAAL----RAAKIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDAVFE 77


                  ....*.
gi 489277922  200 VLKERH 205
Cdd:pfam01503  78 EVHRAN 83
NTP-PPase_HisE cd11547
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 120-197 1.32e-07

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: 47.48  E-value: 1.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489277922 120 ELETVIAKRQAEMPEGAYTTYLFREGVDKILKKVGEEAAEVIIAAKNRDPEELKWEAADLLYHLLVLLREQSLPLDDV 197
Cdd:cd11547    5 ELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQVMMIAKGLTLEDV 82
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 121-178 2.59e-05

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: 41.11  E-value: 2.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489277922 121 LETVIAKRQAEMPEGAYTTYLFREgvDKILK-KVGEEAAEVIIAaknRDPEELKWEAAD 178
Cdd:cd11546    5 LEATLTQRKQNAPPGSYTARLFND--EKLLRaKIMEEAEELCEA---KTKDEVAWEAAD 58
 
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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