NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2047800786|pdb|7OJ5|V]
View 

Chain V, Imidazoleglycerol-phosphate dehydratase

Protein Classification

imidazoleglycerol-phosphate dehydratase( domain architecture ID 11477152)

imidazoleglycerol-phosphate dehydratase catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate in the biosynthesis of L-histidine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02800 PLN02800
imidazoleglycerol-phosphate dehydratase
10-206 2.99e-135

imidazoleglycerol-phosphate dehydratase


:

Pssm-ID: 215430 [Multi-domain]  Cd Length: 261  Bit Score: 379.56  E-value: 2.99e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        10 ARIGEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQ 89
Cdd:PLN02800  64 GRIGEVKRVTKETNVSVKINLDGTGVADSSTGIPFLDHMLDQLASHGLFDVHVKATGDLWIDDHHTNEDVALAIGTALLK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        90 ALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFS-GTNS 168
Cdd:PLN02800 144 ALGDRKGINRFGDFSAPLDEALIEVVLDLSGRPYLGYNLEIPTERVGDLDTEMVEHFFQSLVNNSGMTVHIRQLAaGKNS 223
                        170       180       190
                 ....*....|....*....|....*....|....*...
7OJ5_V       169 HHIIEATFKAFARALRQATEYDTRRRGTIPSSKGVLSR 206
Cdd:PLN02800 224 HHIIEATAKAFGRALRQCAEVDPRRAGTVASSKGTLSV 261
 
Name Accession Description Interval E-value
PLN02800 PLN02800
imidazoleglycerol-phosphate dehydratase
10-206 2.99e-135

imidazoleglycerol-phosphate dehydratase


Pssm-ID: 215430 [Multi-domain]  Cd Length: 261  Bit Score: 379.56  E-value: 2.99e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        10 ARIGEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQ 89
Cdd:PLN02800  64 GRIGEVKRVTKETNVSVKINLDGTGVADSSTGIPFLDHMLDQLASHGLFDVHVKATGDLWIDDHHTNEDVALAIGTALLK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        90 ALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFS-GTNS 168
Cdd:PLN02800 144 ALGDRKGINRFGDFSAPLDEALIEVVLDLSGRPYLGYNLEIPTERVGDLDTEMVEHFFQSLVNNSGMTVHIRQLAaGKNS 223
                        170       180       190
                 ....*....|....*....|....*....|....*...
7OJ5_V       169 HHIIEATFKAFARALRQATEYDTRRRGTIPSSKGVLSR 206
Cdd:PLN02800 224 HHIIEATAKAFGRALRQCAEVDPRRAGTVASSKGTLSV 261
IGPD cd07914
Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2. ...
13-204 1.07e-116

Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2.1.19) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites. IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides.


Pssm-ID: 153419  Cd Length: 190  Bit Score: 329.75  E-value: 1.07e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V       13 GEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQALG 92
Cdd:cd07914   1 AEIERKTKETDIEVELNLDGTGKSKIDTGIGFFDHMLTLFARHGGFDLTVKAKGDLEVDDHHTVEDVGIVLGQALKKALG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V       93 DRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSHHII 172
Cdd:cd07914  81 DKKGIRRYGSALVPMDEALARVAVDLSGRPYLVFDAEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVLYGRNDHHII 160
                       170       180       190
                ....*....|....*....|....*....|..
7OJ5_V      173 EATFKAFARALRQATEYDtrRRGTIPSSKGVL 204
Cdd:cd07914 161 EAIFKAFARALRQAVAID--GRGGVPSTKGVL 190
HisB2 COG0131
Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; ...
21-204 1.47e-113

Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; Imidazoleglycerol phosphate dehydratase HisB is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439901  Cd Length: 183  Bit Score: 321.21  E-value: 1.47e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V       21 ETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQALGDRKGINRF 100
Cdd:COG0131   1 ETDISVELNLDGTGKSDISTGVGFFDHMLEQFARHGLFDLTVKAKGDLHVDDHHTVEDVGIVLGQALAEALGDKKGIRRY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V      101 GNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSHHIIEATFKAFA 180
Cdd:COG0131  81 GHAYVPMDEALARVAVDLSGRPYLVFDVEFPREKIGDFDTELVEEFFRAFANNAGITLHIRVLYGENAHHIIEAIFKAFA 160
                       170       180
                ....*....|....*....|....
7OJ5_V      181 RALRQATEYDTRRRGtIPSSKGVL 204
Cdd:COG0131 161 RALREAVEIDPRRAG-VPSTKGVL 183
IGPD pfam00475
Imidazoleglycerol-phosphate dehydratase;
44-183 1.31e-88

Imidazoleglycerol-phosphate dehydratase;


Pssm-ID: 459824  Cd Length: 140  Bit Score: 256.52  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V         44 FLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPH 123
Cdd:pfam00475   1 FLDHMLDQLAKHGGFDLTVKAKGDLHVDDHHTVEDVGIALGQALKEALGDKKGIRRYGSAIVPMDEALARVAVDLSGRPY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        124 LGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSHHIIEATFKAFARAL 183
Cdd:pfam00475  81 LVFDGEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVLYGENDHHIIEAIFKAFARAL 140
 
Name Accession Description Interval E-value
PLN02800 PLN02800
imidazoleglycerol-phosphate dehydratase
10-206 2.99e-135

imidazoleglycerol-phosphate dehydratase


Pssm-ID: 215430 [Multi-domain]  Cd Length: 261  Bit Score: 379.56  E-value: 2.99e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        10 ARIGEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQ 89
Cdd:PLN02800  64 GRIGEVKRVTKETNVSVKINLDGTGVADSSTGIPFLDHMLDQLASHGLFDVHVKATGDLWIDDHHTNEDVALAIGTALLK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        90 ALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFS-GTNS 168
Cdd:PLN02800 144 ALGDRKGINRFGDFSAPLDEALIEVVLDLSGRPYLGYNLEIPTERVGDLDTEMVEHFFQSLVNNSGMTVHIRQLAaGKNS 223
                        170       180       190
                 ....*....|....*....|....*....|....*...
7OJ5_V       169 HHIIEATFKAFARALRQATEYDTRRRGTIPSSKGVLSR 206
Cdd:PLN02800 224 HHIIEATAKAFGRALRQCAEVDPRRAGTVASSKGTLSV 261
hisB PRK00951
imidazoleglycerol-phosphate dehydratase HisB;
10-204 8.39e-123

imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 234873  Cd Length: 195  Bit Score: 345.17  E-value: 8.39e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        10 ARIGEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQ 89
Cdd:PRK00951   2 MRTAEVERKTKETDISVELNLDGTGKSDIDTGVGFLDHMLDQFARHGLFDLTVKAKGDLHIDDHHTVEDVGIVLGQALKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        90 ALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSH 169
Cdd:PRK00951  82 ALGDKKGIRRYGHAYVPMDEALARVAVDLSGRPYLVFDVEFTREKIGTFDTELVREFFEAFANNAGITLHIRVLYGRNAH 161
                        170       180       190
                 ....*....|....*....|....*....|....*
7OJ5_V       170 HIIEATFKAFARALRQATEYDTRRRGtIPSSKGVL 204
Cdd:PRK00951 162 HIIEALFKAFARALRMAVEIDPRVAG-VPSTKGVL 195
IGPD cd07914
Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2. ...
13-204 1.07e-116

Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2.1.19) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites. IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides.


Pssm-ID: 153419  Cd Length: 190  Bit Score: 329.75  E-value: 1.07e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V       13 GEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQALG 92
Cdd:cd07914   1 AEIERKTKETDIEVELNLDGTGKSKIDTGIGFFDHMLTLFARHGGFDLTVKAKGDLEVDDHHTVEDVGIVLGQALKKALG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V       93 DRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSHHII 172
Cdd:cd07914  81 DKKGIRRYGSALVPMDEALARVAVDLSGRPYLVFDAEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVLYGRNDHHII 160
                       170       180       190
                ....*....|....*....|....*....|..
7OJ5_V      173 EATFKAFARALRQATEYDtrRRGTIPSSKGVL 204
Cdd:cd07914 161 EAIFKAFARALRQAVAID--GRGGVPSTKGVL 190
HisB2 COG0131
Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; ...
21-204 1.47e-113

Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; Imidazoleglycerol phosphate dehydratase HisB is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439901  Cd Length: 183  Bit Score: 321.21  E-value: 1.47e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V       21 ETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQALGDRKGINRF 100
Cdd:COG0131   1 ETDISVELNLDGTGKSDISTGVGFFDHMLEQFARHGLFDLTVKAKGDLHVDDHHTVEDVGIVLGQALAEALGDKKGIRRY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V      101 GNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSHHIIEATFKAFA 180
Cdd:COG0131  81 GHAYVPMDEALARVAVDLSGRPYLVFDVEFPREKIGDFDTELVEEFFRAFANNAGITLHIRVLYGENAHHIIEAIFKAFA 160
                       170       180
                ....*....|....*....|....
7OJ5_V      181 RALRQATEYDTRRRGtIPSSKGVL 204
Cdd:COG0131 161 RALREAVEIDPRRAG-VPSTKGVL 183
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
8-204 7.82e-94

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 277.83  E-value: 7.82e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V         8 SGARIGEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTAL 87
Cdd:PRK05446 163 KRDRYAHVVRNTKETDIDVEVWLDREGKSKINTGIGFFDHMLDQIATHGGFRLEIKVKGDLHIDDHHTVEDTALALGEAL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        88 LQALGDRKGINRFGnFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQfSGTN 167
Cdd:PRK05446 243 KQALGDKRGIGRFG-FVLPMDECLARCALDISGRPYLVFKAEFKRERVGDMSTEMVEHFFRSLSDAMGCTLHLKT-KGKN 320
                        170       180       190
                 ....*....|....*....|....*....|....*...
7OJ5_V       168 SHHIIEATFKAFARALRQAteydTRRRG-TIPSSKGVL 204
Cdd:PRK05446 321 DHHKVESLFKAFGRALRQA----IRVEGnTLPSSKGVL 354
IGPD pfam00475
Imidazoleglycerol-phosphate dehydratase;
44-183 1.31e-88

Imidazoleglycerol-phosphate dehydratase;


Pssm-ID: 459824  Cd Length: 140  Bit Score: 256.52  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V         44 FLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPH 123
Cdd:pfam00475   1 FLDHMLDQLAKHGGFDLTVKAKGDLHVDDHHTVEDVGIALGQALKEALGDKKGIRRYGSAIVPMDEALARVAVDLSGRPY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        124 LGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSHHIIEATFKAFARAL 183
Cdd:pfam00475  81 LVFDGEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVLYGENDHHIIEAIFKAFARAL 140
hisB PRK13598
imidazoleglycerol-phosphate dehydratase; Provisional
10-204 1.28e-51

imidazoleglycerol-phosphate dehydratase; Provisional


Pssm-ID: 184171  Cd Length: 193  Bit Score: 164.98  E-value: 1.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        10 ARIGEMKRVTKETNVSVKINLDGTGVADNSSGIPFLDHMLDQLASHGLFDVHVKATGDTHIDDHHTNEDVALAIGTALLQ 89
Cdd:PRK13598   2 SRNANITRETKETKIEVFLDIDRKGEIKVSTPVPFFNHMLITLLTYMNSTATVSATDKLPYDDHHIVEDVAITLGLAIKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7OJ5_V        90 ALGDRKGINRFGNFSAPLDEALVHVSLDLSGRPHLGYDLNIPTQRVGKYDTQLVEHFFQSLVNTSGMTLHIRQFSGTNSH 169
Cdd:PRK13598  82 ALGDKRGIKRFSHQIIPMDEALVLVSLDISGRGMAFVNLNLKRSEIGGLATENIPHFFQSFAYNSGVTLHISQLSGYNTH 161
                        170       180       190
                 ....*....|....*....|....*....|....*
7OJ5_V       170 HIIEATFKAFARALRQATEYDTRRrgtIPSSKGVL 204
Cdd:PRK13598 162 HIIEASFKGLGLALYEATRIVDNE---IRSTKGVL 193
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH