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Conserved domains on  [gi|1230362739|gb|OYJ38498|]
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bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB [Klebsiella pneumoniae subsp. pneumoniae]

Protein Classification

bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase( domain architecture ID 11481005)

bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate and the hydrolysis of L-histidinol phosphate to L-histidinol and phosphate

EC:  3.1.3.15|4.2.1.19
Gene Ontology:  GO:0005737|GO:0004401|GO:0004424|GO:0046872|GO:0000105
PubMed:  25848029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
3-355 0e+00

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


:

Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 763.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   3 QKYLFIDRDGTLISEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFAS 82
Cdd:PRK05446    2 QKILFIDRDGTLIEEPPTDFQVDSLDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMMQIFES 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  83 QGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRETLDWPTICEQL 162
Cdd:PRK05446   82 QGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIRYARETLNWDAIAEQL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 163 TRRDRYAHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEA 242
Cdd:PRK05446  162 TKRDRYAHVVRNTKETDIDVEVWLDREGKSKINTGIGFFDHMLDQIATHGGFRLEIKVKGDLHIDDHHTVEDTALALGEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 243 LKLALGDKRGINRFGFVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKTKGKND 322
Cdd:PRK05446  242 LKQALGDKRGIGRFGFVLPMDECLARCALDISGRPYLVFKAEFKRERVGDMSTEMVEHFFRSLSDAMGCTLHLKTKGKND 321

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1230362739 323 HHRVESLFKAFGRTLRQAIRVQGDALPSSKGVL 355
Cdd:PRK05446  322 HHKVESLFKAFGRALRQAIRVEGNTLPSSKGVL 354
 
Name Accession Description Interval E-value
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
3-355 0e+00

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 763.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   3 QKYLFIDRDGTLISEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFAS 82
Cdd:PRK05446    2 QKILFIDRDGTLIEEPPTDFQVDSLDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMMQIFES 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  83 QGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRETLDWPTICEQL 162
Cdd:PRK05446   82 QGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIRYARETLNWDAIAEQL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 163 TRRDRYAHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEA 242
Cdd:PRK05446  162 TKRDRYAHVVRNTKETDIDVEVWLDREGKSKINTGIGFFDHMLDQIATHGGFRLEIKVKGDLHIDDHHTVEDTALALGEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 243 LKLALGDKRGINRFGFVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKTKGKND 322
Cdd:PRK05446  242 LKQALGDKRGIGRFGFVLPMDECLARCALDISGRPYLVFKAEFKRERVGDMSTEMVEHFFRSLSDAMGCTLHLKTKGKND 321

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1230362739 323 HHRVESLFKAFGRTLRQAIRVQGDALPSSKGVL 355
Cdd:PRK05446  322 HHKVESLFKAFGRALRQAIRVEGNTLPSSKGVL 354
IGPD cd07914
Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2. ...
 169-355 1.13e-113

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: 328.21  E-value: 1.13e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 169 AHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALG 248
Cdd:cd07914     1 AEIERKTKETDIEVELNLDGTGKSKIDTGIGFFDHMLTLFARHGGFDLTVKAKGDLEVDDHHTVEDVGIVLGQALKKALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 249 DKRGINRFG-FVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDHHRV 326
Cdd:cd07914    81 DKKGIRRYGsALVPMDEALARVAVDLSGRPYLVFDAEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVlYGRNDHHII 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1230362739 327 ESLFKAFGRTLRQAIRVQGD-ALPSSKGVL 355
Cdd:cd07914   161 EAIFKAFARALRQAVAIDGRgGVPSTKGVL 190
HisB2 COG0131
Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; ...
 177-355 2.29e-103

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: 301.56  E-value: 2.29e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 177 ETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALGDKRGINRF 256
Cdd:COG0131     1 ETDISVELNLDGTGKSDISTGVGFFDHMLEQFARHGLFDLTVKAKGDLHVDDHHTVEDVGIVLGQALAEALGDKKGIRRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 257 GF-VLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDHHRVESLFKAFG 334
Cdd:COG0131    81 GHaYVPMDEALARVAVDLSGRPYLVFDVEFPREKIGDFDTELVEEFFRAFANNAGITLHIRVlYGENAHHIIEAIFKAFA 160

                         170       180
                  ....*....|....*....|...
gi 1230362739 335 RTLRQAIRVQGDA--LPSSKGVL 355
Cdd:COG0131   161 RALREAVEIDPRRagVPSTKGVL 183
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 3-163 5.14e-94

histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 130328 [Multi-domain]  Cd Length: 161  Bit Score: 276.98  E-value: 5.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   3 QKYLFIDRDGTLISEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFAS 82
Cdd:TIGR01261   1 QKILFIDRDGTLIEEPPSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  83 QGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRETLDWPTICEQL 162
Cdd:TIGR01261  81 QGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLGIRGIQYDEEELNWDMIAEEL 160


                  .
gi 1230362739 163 T 163
Cdd:TIGR01261 161 L 161
IGPD pfam00475
Imidazoleglycerol-phosphate dehydratase;
200-337 2.75e-85

Imidazoleglycerol-phosphate dehydratase;


Pssm-ID: 459824  Cd Length: 140  Bit Score: 254.21  E-value: 2.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 200 FFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALGDKRGINRFG-FVLPMDECLARCALDISGRPH 278
Cdd:pfam00475   1 FLDHMLDQLAKHGGFDLTVKAKGDLHVDDHHTVEDVGIALGQALKEALGDKKGIRRYGsAIVPMDEALARVAVDLSGRPY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 279 LEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDHHRVESLFKAFGRTL 337
Cdd:pfam00475  81 LVFDGEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVlYGENDHHIIEAIFKAFARAL 140
 
Name Accession Description Interval E-value
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
3-355 0e+00

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 763.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   3 QKYLFIDRDGTLISEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFAS 82
Cdd:PRK05446    2 QKILFIDRDGTLIEEPPTDFQVDSLDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMMQIFES 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  83 QGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRETLDWPTICEQL 162
Cdd:PRK05446   82 QGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIRYARETLNWDAIAEQL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 163 TRRDRYAHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEA 242
Cdd:PRK05446  162 TKRDRYAHVVRNTKETDIDVEVWLDREGKSKINTGIGFFDHMLDQIATHGGFRLEIKVKGDLHIDDHHTVEDTALALGEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 243 LKLALGDKRGINRFGFVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKTKGKND 322
Cdd:PRK05446  242 LKQALGDKRGIGRFGFVLPMDECLARCALDISGRPYLVFKAEFKRERVGDMSTEMVEHFFRSLSDAMGCTLHLKTKGKND 321

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1230362739 323 HHRVESLFKAFGRTLRQAIRVQGDALPSSKGVL 355
Cdd:PRK05446  322 HHKVESLFKAFGRALRQAIRVEGNTLPSSKGVL 354
IGPD cd07914
Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2. ...
 169-355 1.13e-113

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: 328.21  E-value: 1.13e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 169 AHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALG 248
Cdd:cd07914     1 AEIERKTKETDIEVELNLDGTGKSKIDTGIGFFDHMLTLFARHGGFDLTVKAKGDLEVDDHHTVEDVGIVLGQALKKALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 249 DKRGINRFG-FVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDHHRV 326
Cdd:cd07914    81 DKKGIRRYGsALVPMDEALARVAVDLSGRPYLVFDAEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVlYGRNDHHII 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1230362739 327 ESLFKAFGRTLRQAIRVQGD-ALPSSKGVL 355
Cdd:cd07914   161 EAIFKAFARALRQAVAIDGRgGVPSTKGVL 190
hisB PRK00951
imidazoleglycerol-phosphate dehydratase HisB;
166-355 3.81e-104

imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 234873  Cd Length: 195  Bit Score: 303.96  E-value: 3.81e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 166 DRYAHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKL 245
Cdd:PRK00951    2 MRTAEVERKTKETDISVELNLDGTGKSDIDTGVGFLDHMLDQFARHGLFDLTVKAKGDLHIDDHHTVEDVGIVLGQALKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 246 ALGDKRGINRFG-FVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDH 323
Cdd:PRK00951   82 ALGDKKGIRRYGhAYVPMDEALARVAVDLSGRPYLVFDVEFTREKIGTFDTELVREFFEAFANNAGITLHIRVlYGRNAH 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1230362739 324 HRVESLFKAFGRTLRQAIRVQGDA--LPSSKGVL 355
Cdd:PRK00951  162 HIIEALFKAFARALRMAVEIDPRVagVPSTKGVL 195
HisB2 COG0131
Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; ...
 177-355 2.29e-103

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: 301.56  E-value: 2.29e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 177 ETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALGDKRGINRF 256
Cdd:COG0131     1 ETDISVELNLDGTGKSDISTGVGFFDHMLEQFARHGLFDLTVKAKGDLHVDDHHTVEDVGIVLGQALAEALGDKKGIRRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 257 GF-VLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDHHRVESLFKAFG 334
Cdd:COG0131    81 GHaYVPMDEALARVAVDLSGRPYLVFDVEFPREKIGDFDTELVEEFFRAFANNAGITLHIRVlYGENAHHIIEAIFKAFA 160

                         170       180
                  ....*....|....*....|...
gi 1230362739 335 RTLRQAIRVQGDA--LPSSKGVL 355
Cdd:COG0131   161 RALREAVEIDPRRagVPSTKGVL 183
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 3-163 5.14e-94

histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 130328 [Multi-domain]  Cd Length: 161  Bit Score: 276.98  E-value: 5.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   3 QKYLFIDRDGTLISEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFAS 82
Cdd:TIGR01261   1 QKILFIDRDGTLIEEPPSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  83 QGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRETLDWPTICEQL 162
Cdd:TIGR01261  81 QGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLGIRGIQYDEEELNWDMIAEEL 160


                  .
gi 1230362739 163 T 163
Cdd:TIGR01261 161 L 161
IGPD pfam00475
Imidazoleglycerol-phosphate dehydratase;
200-337 2.75e-85

Imidazoleglycerol-phosphate dehydratase;


Pssm-ID: 459824  Cd Length: 140  Bit Score: 254.21  E-value: 2.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 200 FFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALGDKRGINRFG-FVLPMDECLARCALDISGRPH 278
Cdd:pfam00475   1 FLDHMLDQLAKHGGFDLTVKAKGDLHVDDHHTVEDVGIALGQALKEALGDKKGIRRYGsAIVPMDEALARVAVDLSGRPY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 279 LEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKT-KGKNDHHRVESLFKAFGRTL 337
Cdd:pfam00475  81 LVFDGEFPREKIGDFDTELVEEFFRSFANNAGITLHIRVlYGENDHHIIEAIFKAFARAL 140
PLN02800 PLN02800
imidazoleglycerol-phosphate dehydratase
 167-355 5.41e-82

imidazoleglycerol-phosphate dehydratase


Pssm-ID: 215430 [Multi-domain]  Cd Length: 261  Bit Score: 250.14  E-value: 5.41e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 167 RYAHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLA 246
Cdd:PLN02800   65 RIGEVKRVTKETNVSVKINLDGTGVADSSTGIPFLDHMLDQLASHGLFDVHVKATGDLWIDDHHTNEDVALAIGTALLKA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 247 LGDKRGINRFG-FVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHL--KTKGKNDH 323
Cdd:PLN02800  145 LGDRKGINRFGdFSAPLDEALIEVVLDLSGRPYLGYNLEIPTERVGDLDTEMVEHFFQSLVNNSGMTVHIrqLAAGKNSH 224

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1230362739 324 HRVESLFKAFGRTLRQAIRV---QGDALPSSKGVL 355
Cdd:PLN02800  225 HIIEATAKAFGRALRQCAEVdprRAGTVASSKGTL 259
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-151 4.59e-67

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 208.80  E-value: 4.59e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   1 MTQKYLFIDRDGTLISEPPEdfqVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVF 80
Cdd:COG0241     1 MMKKAVFLDRDGTINEDVGY---VKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1230362739  81 ASQGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRE 151
Cdd:COG0241    78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTG 148
hisB PRK13598
imidazoleglycerol-phosphate dehydratase; Provisional
 167-355 2.03e-55

imidazoleglycerol-phosphate dehydratase; Provisional


Pssm-ID: 184171  Cd Length: 193  Bit Score: 179.62  E-value: 2.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 167 RYAHVERITKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLA 246
Cdd:PRK13598    3 RNANITRETKETKIEVFLDIDRKGEIKVSTPVPFFNHMLITLLTYMNSTATVSATDKLPYDDHHIVEDVAITLGLAIKEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739 247 LGDKRGINRFGF-VLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHL-KTKGKNDHH 324
Cdd:PRK13598   83 LGDKRGIKRFSHqIIPMDEALVLVSLDISGRGMAFVNLNLKRSEIGGLATENIPHFFQSFAYNSGVTLHIsQLSGYNTHH 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1230362739 325 RVESLFKAFGRTLRQAIRVQGDALPSSKGVL 355
Cdd:PRK13598  163 IIEASFKGLGLALYEATRIVDNEIRSTKGVL 193
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 4-148 3.34e-54

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 174.64  E-value: 3.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   4 KYLFIDRDGTLISEPPEdfqVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFASQ 83
Cdd:cd07503     1 KALFLDRDGVINVDVPY---VHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQ 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1230362739  84 GVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRY 148
Cdd:cd07503    78 GVEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 4-143 3.54e-46

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.


Pssm-ID: 273737  Cd Length: 147  Bit Score: 154.09  E-value: 3.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   4 KYLFIDRDGTLISEPPEDFqVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFASQ 83
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSDY-PRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  84 GVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGI 143
Cdd:TIGR01656  80 GVAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGA 139
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-144 2.59e-24

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 97.97  E-value: 2.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   1 MTQKYLFIDRDGTL-------ISEPpEDFQvdrfdklaFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPH 73
Cdd:PRK08942    1 KSMKAIFLDRDGVInvdsdgyVKSP-DEWI--------PIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1230362739  74 NLMMQVFASQGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGIT 144
Cdd:PRK08942   72 EKMDWSLADRGGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVT 142
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 4-140 5.31e-21

D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD resembles the histidinol phosphatase domain of the bifunctional protein HisB. The member from E. coli has been characterized as D,D-heptose 1,7-bisphosphate phosphatase, GmhB, involved in inner core LPS assembly (). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129317 [Multi-domain]  Cd Length: 176  Bit Score: 88.83  E-value: 5.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   4 KYLFIDRDGTLISEPPEDFQVDRFDklaFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQVFASQ 83
Cdd:TIGR00213   2 KAIFLDRDGTINIDHGYVHEIDNFE---FIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAER 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1230362739  84 GVNFEEVLICPHFP------GDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADN 140
Cdd:TIGR00213  79 DVDLDGIYYCPHHPegveefRQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVA 141
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 4-150 3.63e-18

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 79.76  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   4 KYLFIDRDGTLISEppeDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAfdgpHNLMMQVFASQ 83
Cdd:TIGR01662   1 KAVVLDLDGTLTDD---VPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSF----SGRVARRLEEL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1230362739  84 GVNFEEVLICPHfpgdncaCRKPKTQLVLPWLEE-GVLDKSHSYVIGDRA-TDLELADNMGITGLRYDR 150
Cdd:TIGR01662  74 GVPIDILYACPG-------CRKPKPGMFLEALKRfNEIDPEESVYVGDQDlTDLQAAKRVGLATILVAP 135
PRK06769 PRK06769
HAD-IIIA family hydrolase;
1-172 6.51e-18

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 80.16  E-value: 6.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   1 MTQKYLFIDRDGTLISEP----PEDFQVDRFDKLAfepqvipaLLKLQQEGYKLVMITNQDGLGtdslpqeafDGPHNlm 76
Cdd:PRK06769    2 TNIQAIFIDRDGTIGGDTtihyPGSFTLFPFTKAS--------LQKLKANHIKIFSFTNQPGIA---------DGIAT-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  77 MQVFASQ--GVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMG------ITGLRY 148
Cdd:PRK06769   63 IADFVQElkGFGFDDIYLCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNattilvRTGAGY 142

                         170       180
                  ....*....|....*....|....
gi 1230362739 149 DreTLDwpticeqlTRRDRYAHVE 172
Cdd:PRK06769  143 D--ALH--------TYRDKWAHIE 156
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 9-143 1.76e-09

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319766  Cd Length: 154  Bit Score: 55.82  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   9 DRDGTLIS-EPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMM-------QVF 80
Cdd:cd01625     6 DLDGTLIKtKSGKVFPTNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTPEVFKGKIEAILeklgvpiQVY 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1230362739  81 ASQGVNFeevlicphfpgdncaCRKPKT---QLVLPWLEEGV-LDKSHSYVIGDRA--------TDLELADNMGI 143
Cdd:cd01625    86 AATKKGK---------------YRKPVTgmwDHLKEDLNSGIpINLKDSFYVGDAAgrpkdfsdSDRLFAENVGL 145
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 9-143 2.98e-06

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.


Pssm-ID: 370030  Cd Length: 161  Bit Score: 46.87  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   9 DRDGTLI-SEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGT---DSLPQ---------EAFDGPhnl 75
Cdd:pfam08645   6 DLDGTLIkTKSGKVFPRNPDDWKWLYPSVPEKLKKLHEDGYKIVIFTNQGGIGRkgkKSLEKfknkieailKKLGVP--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  76 mMQVFASqgvnfeevlicphfPGDNcACRKPKTQLvlpWLE-------EGVLDKSHSYVIGDRA--------------TD 134
Cdd:pfam08645  83 -LQVYAA--------------TKKD-IYRKPNTGM---WDEmkkdyndGVEIDLEKSFYVGDAAgrpydtrrkkdfsdSD 143


                  ....*....
gi 1230362739 135 LELADNMGI 143
Cdd:pfam08645 144 RKFALNVGI 152
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 6-148 4.41e-06

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 45.08  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   6 LFIDRDGTLIseppedfqvdrfdklafepqVIPALLKLQQEGYKLVMITNQDGLGTDSLpqeafdgphnlmmqVFASQGV 85
Cdd:cd01427     2 VLFDLDGTLL--------------------AVELLKRLRAAGIKLAIVTNRSREALRAL--------------LEKLGLG 47

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1230362739  86 NFEEVLICphfpGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRY 148
Cdd:cd01427    48 DLFDGIIG----SDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTVAV 106
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
20-143 8.26e-06

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 46.08  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  20 EDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNqdglgtdslpqeafdGPHNLMMQVFASQGVN-FEEVLICphfpG 98
Cdd:COG0546    73 ELYEEELLDETRLFPGVRELLEALKARGIKLAVVTN---------------KPREFAERLLEALGLDdYFDAIVG----G 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1230362739  99 DNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGI 143
Cdd:COG0546   134 DDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGV 178
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 9-156 7.24e-05

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 44.63  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739   9 DRDGTLIS--------EPPEDFQVdrfdklaFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPhnlMMQVF 80
Cdd:TIGR01663 174 DLDGTIIKtksgkvfpKGPDDWQI-------IFPEIPEKLKELEADGFKICIFTNQGGIARGKINADDFKAK---IEAIV 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362739  81 ASQGVNFeEVLICPHfpgdNCACRKPKT---QLVLPWLEEGV-LDKSHSYVIGD-------------RATDLELAD---- 139
Cdd:TIGR01663 244 AKLGVPF-QVFIAIG----AGFYRKPLTgmwDHLKEEANDGTeIQEDDCFFVGDaagrpangkaagkKKKDFSCADrlfa 318

                         170
                  ....*....|....*...
gi 1230362739 140 -NMGITGLRYDRETLDWP 156
Cdd:TIGR01663 319 aNLGIPFATPEEFFLGKP 336
Hydrolase_like pfam13242
HAD-hyrolase-like;
103-146 3.05e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 36.05  E-value: 3.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1230362739 103 CRKPKTQLVLPWLEEGVLDKSHSYVIGDR-ATDLELADNMGITGL 146
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRlDTDILGAREAGARTI 46
 
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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