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Conserved domains on  [gi|5822224]
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Protein Classification

similar to phosphoenolpyruvate phosphomutase (domain architecture ID 10798011)

protein similar to phosphoenolpyruvate phosphomutase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PEP_mutase TIGR02320
phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate ...
11-283 2.00e-158

phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model.


:

Pssm-ID: 274077  Cd Length: 284  Bit Score: 442.53  E-value: 2.00e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     11 LKQ*LNSKDLEFI*EAHNGLSARIVQEA--------GFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPI 82
Cdd:TIGR02320   1 LRQLLHSKPLERLMEAHNGLSALIAEEArvevgdslGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVEFMFDVTTKPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     83 LLDADTGyGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGR-AQPLADIEEFALKIKACKDSQTDPDFCIVARVE 161
Cdd:TIGR02320  81 ILDGDTG-GNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFGNDvAQPQASVEEFCGKIRAGKDAQTTEDFMIIARVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    162 AFIAGWGLDEALKRAEAYRNAGADAIL*HSKKADPSDIEAF*KAWNN---QGPVVIVPTKYYKTPTDHFRD*GVS*VIWA 238
Cdd:TIGR02320 160 SLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNhypRTPLVIVPTSYYTTPTDEFRDAGISVVIYA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 5822224    239 NHNLRASVSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDE 283
Cdd:TIGR02320 240 NHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLIPGTE 284
 
Name Accession Description Interval E-value
PEP_mutase TIGR02320
phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate ...
11-283 2.00e-158

phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model.


Pssm-ID: 274077  Cd Length: 284  Bit Score: 442.53  E-value: 2.00e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     11 LKQ*LNSKDLEFI*EAHNGLSARIVQEA--------GFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPI 82
Cdd:TIGR02320   1 LRQLLHSKPLERLMEAHNGLSALIAEEArvevgdslGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVEFMFDVTTKPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     83 LLDADTGyGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGR-AQPLADIEEFALKIKACKDSQTDPDFCIVARVE 161
Cdd:TIGR02320  81 ILDGDTG-GNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFGNDvAQPQASVEEFCGKIRAGKDAQTTEDFMIIARVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    162 AFIAGWGLDEALKRAEAYRNAGADAIL*HSKKADPSDIEAF*KAWNN---QGPVVIVPTKYYKTPTDHFRD*GVS*VIWA 238
Cdd:TIGR02320 160 SLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNhypRTPLVIVPTSYYTTPTDEFRDAGISVVIYA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 5822224    239 NHNLRASVSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDE 283
Cdd:TIGR02320 240 NHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLIPGTE 284
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
11-255 1.32e-88

Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. Known members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), and 2-methylisocitrate lyase (MICL). Isocitrate lyase (ICL) catalyzes the conversion of isocitrate to succinate and glyoxylate, the first committed step in the glyoxylate pathway. This carbon-conserving pathway is present in most prokaryotes, lower eukaryotes and plants, but has not been observed in vertebrates. PEP mutase (PEPM) turns phosphoenolpyruvate (PEP) into phosphonopyruvate (P-pyr), an important intermediate in the formation of organophosphonates, which function as antibiotics or play a role in pathogenesis or signaling. P-pyr can be hydrolyzed by phosphonopyruvate hydrolase (PPH) to from pyruvate and phosphate. Oxaloacetate acetylhydrolase (OAH) catalyzes the hydrolytic cleavage of oxaloacetate to form acetate and oxalate, an important pathway to produce oxalate in filamentous fungi. 2-methylisocitrate lyase (MICL) cleaves 2-methylisocitrate to pyruvate and succinate, part of the methylcitrate cycle for the alpha-oxidation of propionate.


Pssm-ID: 119340  Cd Length: 243  Bit Score: 263.97  E-value: 1.32e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   11 LKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGY 90
Cdd:cd00377   1 LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAASLGLPDGGLLTLDEVLAAVRRIARAVDLPVIADADTGY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   91 GNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGraQPLADIEEFALKIKACKDSQTD-PDFCIVARVEAFIAG-WG 168
Cdd:cd00377  81 GNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGG--KVLVPIEEFVAKIKAARDARDDlPDFVIIARTDALLAGeEG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224  169 LDEALKRAEAYRNAGADAIL*HSKKaDPSDIEAF*KAwnNQGPVVIVPTKYYKTPT-DHFRD*GVS*VIWANHNLRASVS 247
Cdd:cd00377 159 LDEAIERAKAYAEAGADGIFVEGLK-DPEEIRAFAEA--PDVPLNVNMTPGGNLLTvAELAELGVRRVSYGLALLRAAAK 235

                ....*...
gi 5822224  248 AIQQTTKQ 255
Cdd:cd00377 236 AMREAARE 243
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
9-293 8.02e-83

2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and metabolism];


Pssm-ID: 225311  Cd Length: 289  Bit Score: 251.05  E-value: 8.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    9 TQLKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADT 88
Cdd:COG2513   8 AAFRALHASGDPLVLPGAWDAGSALLAERAGFKALYLSGAGVAASLGLPDLGITTLDEVLADARRITDAVDLPVLVDIDT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   89 GYGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGRaqPLADIEEFALKIKACKDSQTDPDFCIVARVEAFIAGwG 168
Cdd:COG2513  88 GFGEALNVARTVRELEQAGAAGIHIEDQVGPKRCGHLPGK--ELVSIDEMVDRIKAAVEARRDPDFVIIARTDALLVE-G 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224  169 LDEALKRAEAYRNAGADAIL*HSKKaDPSDIEAF*KAWnnQGPVVIVPTKYYKTP---TDHFRD*GVS*VIWANHNLRAS 245
Cdd:COG2513 165 LDDAIERAQAYVEAGADAIFPEALT-DLEEIRAFAEAV--PVPLPANITEFGKTPlltVAELAELGVKRVSYGLTAFRAA 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 5822224  246 VSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYLP 293
Cdd:COG2513 242 LKAAEQAAREIRREGTQANVLDKMQTRKELYDLINYYDYEAKDDELFP 289
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
25-256 2.61e-68

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein has been characterized as catalyzing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 316253  Cd Length: 239  Bit Score: 212.04  E-value: 2.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     25 EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGYG-NFNNARRLVRKL 103
Cdd:pfam13714  15 NAWDAASARIVEAAGFPAIATSSAGVAASLGYPDGELLPLDELLAAVRRIAAAVDLPVSVDLEDGYGdSPEEVAETVRRL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    104 EDRGVAGACLEDKlfpKTNSLhdgraqPLADIEEFALKIKACKDSQ--TDPDFCIVARVEAFI--AGWGLDEALKRAEAY 179
Cdd:pfam13714  95 IAAGVVGVNIEDS---KKGSL------NLADPEEFAAKIAAARAAAraAGVPFVINARTDAFLlgAGDGLEEAIERARAY 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5822224    180 RNAGADAIL*HSKKaDPSDIEAF*KAWnnQGPVVIVPTKYYkTPTDHFRD*GVS*VIWANHNLRASVSAIQQTTKQI 256
Cdd:pfam13714 166 AEAGADGIFVPGLL-DPADIAALVAAV--PGPVNVVPGPGT-LSVAELAALGVARISYGPHLARAAYAALRRAAEEI 238
prpB PRK11320
2-methylisocitrate lyase; Provisional
28-237 4.84e-28

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 109.22  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    28 NGLSARIVQEAGFKGIWGSGLSVS-AQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGYGNFNNARRLVRKLEDR 106
Cdd:PRK11320  26 NAYHALLAERAGFKAIYLSGGGVAaASLGLPDLGITTLDDVLIDVRRITDACDLPLLVDIDTGFGGAFNIARTVKSMIKA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   107 GVAGACLEDKLFPKTNSLHDGRAqpLADIEEFALKIKACKDSQTDPDFCIVARVEAFiAGWGLDEALKRAEAYRNAGADA 186
Cdd:PRK11320 106 GAAAVHIEDQVGAKRCGHRPNKE--IVSQEEMVDRIKAAVDARTDPDFVIMARTDAL-AVEGLDAAIERAQAYVEAGADM 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5822224   187 IL*HSKKaDPSDIEAF*KAWnnQGPVVIVPTKYYKTP---TDHFRD*GVS*VIW 237
Cdd:PRK11320 183 IFPEAMT-ELEMYRRFADAV--KVPILANITEFGATPlftTEELASAGVAMVLY 233
 
Name Accession Description Interval E-value
PEP_mutase TIGR02320
phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate ...
11-283 2.00e-158

phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model.


Pssm-ID: 274077  Cd Length: 284  Bit Score: 442.53  E-value: 2.00e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     11 LKQ*LNSKDLEFI*EAHNGLSARIVQEA--------GFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPI 82
Cdd:TIGR02320   1 LRQLLHSKPLERLMEAHNGLSALIAEEArvevgdslGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVEFMFDVTTKPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     83 LLDADTGyGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGR-AQPLADIEEFALKIKACKDSQTDPDFCIVARVE 161
Cdd:TIGR02320  81 ILDGDTG-GNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFGNDvAQPQASVEEFCGKIRAGKDAQTTEDFMIIARVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    162 AFIAGWGLDEALKRAEAYRNAGADAIL*HSKKADPSDIEAF*KAWNN---QGPVVIVPTKYYKTPTDHFRD*GVS*VIWA 238
Cdd:TIGR02320 160 SLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNhypRTPLVIVPTSYYTTPTDEFRDAGISVVIYA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 5822224    239 NHNLRASVSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDE 283
Cdd:TIGR02320 240 NHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLIPGTE 284
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
11-255 1.32e-88

Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. Known members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), and 2-methylisocitrate lyase (MICL). Isocitrate lyase (ICL) catalyzes the conversion of isocitrate to succinate and glyoxylate, the first committed step in the glyoxylate pathway. This carbon-conserving pathway is present in most prokaryotes, lower eukaryotes and plants, but has not been observed in vertebrates. PEP mutase (PEPM) turns phosphoenolpyruvate (PEP) into phosphonopyruvate (P-pyr), an important intermediate in the formation of organophosphonates, which function as antibiotics or play a role in pathogenesis or signaling. P-pyr can be hydrolyzed by phosphonopyruvate hydrolase (PPH) to from pyruvate and phosphate. Oxaloacetate acetylhydrolase (OAH) catalyzes the hydrolytic cleavage of oxaloacetate to form acetate and oxalate, an important pathway to produce oxalate in filamentous fungi. 2-methylisocitrate lyase (MICL) cleaves 2-methylisocitrate to pyruvate and succinate, part of the methylcitrate cycle for the alpha-oxidation of propionate.


Pssm-ID: 119340  Cd Length: 243  Bit Score: 263.97  E-value: 1.32e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   11 LKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGY 90
Cdd:cd00377   1 LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAASLGLPDGGLLTLDEVLAAVRRIARAVDLPVIADADTGY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   91 GNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGraQPLADIEEFALKIKACKDSQTD-PDFCIVARVEAFIAG-WG 168
Cdd:cd00377  81 GNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGG--KVLVPIEEFVAKIKAARDARDDlPDFVIIARTDALLAGeEG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224  169 LDEALKRAEAYRNAGADAIL*HSKKaDPSDIEAF*KAwnNQGPVVIVPTKYYKTPT-DHFRD*GVS*VIWANHNLRASVS 247
Cdd:cd00377 159 LDEAIERAKAYAEAGADGIFVEGLK-DPEEIRAFAEA--PDVPLNVNMTPGGNLLTvAELAELGVRRVSYGLALLRAAAK 235

                ....*...
gi 5822224  248 AIQQTTKQ 255
Cdd:cd00377 236 AMREAARE 243
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
9-293 8.02e-83

2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and metabolism];


Pssm-ID: 225311  Cd Length: 289  Bit Score: 251.05  E-value: 8.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    9 TQLKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADT 88
Cdd:COG2513   8 AAFRALHASGDPLVLPGAWDAGSALLAERAGFKALYLSGAGVAASLGLPDLGITTLDEVLADARRITDAVDLPVLVDIDT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   89 GYGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGRaqPLADIEEFALKIKACKDSQTDPDFCIVARVEAFIAGwG 168
Cdd:COG2513  88 GFGEALNVARTVRELEQAGAAGIHIEDQVGPKRCGHLPGK--ELVSIDEMVDRIKAAVEARRDPDFVIIARTDALLVE-G 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224  169 LDEALKRAEAYRNAGADAIL*HSKKaDPSDIEAF*KAWnnQGPVVIVPTKYYKTP---TDHFRD*GVS*VIWANHNLRAS 245
Cdd:COG2513 165 LDDAIERAQAYVEAGADAIFPEALT-DLEEIRAFAEAV--PVPLPANITEFGKTPlltVAELAELGVKRVSYGLTAFRAA 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 5822224  246 VSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYLP 293
Cdd:COG2513 242 LKAAEQAAREIRREGTQANVLDKMQTRKELYDLINYYDYEAKDDELFP 289
Pphn_pyruv_hyd TIGR02321
phosphonopyruvate hydrolase; This family consists of phosphonopyruvate hydrolase, an enzyme ...
7-292 4.83e-69

phosphonopyruvate hydrolase; This family consists of phosphonopyruvate hydrolase, an enzyme closely related to phosphoenolpyruvate phosphomutase. It cleaves the direct C-P bond of phosphonopyruvate. The characterized example is from Variovorax sp. Pal2.


Pssm-ID: 131374  Cd Length: 290  Bit Score: 215.74  E-value: 4.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224      7 KTTQLKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDA 86
Cdd:TIGR02321   3 KNQALRAALDSGRLFTAMAAHNPLVAKLAEQAGFGGIWGSGFELSASYAVPDANILSMSTHLEMMRAIASTVSIPLIADI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     87 DTGYGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGRAQPLADIEEFALKIKACKDSQTDPDFCIVARVEAFIAG 166
Cdd:TIGR02321  83 DTGFGNAVNVHYVVPQYEAAGASAIVMEDKTFPKDTSLRTDGRQELVRIEEFQGKIAAATAARADRDFVVIARVEALIAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    167 WGLDEALKRAEAYRNAGADAIL*HSKKADPSDIEAF*KAWNNQGPVVIVPTKYYKTPTDHFRD*G-VS*VIWANHNLRAS 245
Cdd:TIGR02321 163 LGQQEAVRRGQAYEEAGADAILIHSRQKTPDEILAFVKSWPGKVPLVLVPTAYPQLTEADIAALSkVGIVIYGNHAIRAA 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 5822224    246 VSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYL 292
Cdd:TIGR02321 243 VGAVREVFARIRRDGGIREVDAALPSVKEIIELQGDERMRAVEARYL 289
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
25-256 2.61e-68

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein has been characterized as catalyzing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 316253  Cd Length: 239  Bit Score: 212.04  E-value: 2.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     25 EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGYG-NFNNARRLVRKL 103
Cdd:pfam13714  15 NAWDAASARIVEAAGFPAIATSSAGVAASLGYPDGELLPLDELLAAVRRIAAAVDLPVSVDLEDGYGdSPEEVAETVRRL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    104 EDRGVAGACLEDKlfpKTNSLhdgraqPLADIEEFALKIKACKDSQ--TDPDFCIVARVEAFI--AGWGLDEALKRAEAY 179
Cdd:pfam13714  95 IAAGVVGVNIEDS---KKGSL------NLADPEEFAAKIAAARAAAraAGVPFVINARTDAFLlgAGDGLEEAIERARAY 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5822224    180 RNAGADAIL*HSKKaDPSDIEAF*KAWnnQGPVVIVPTKYYkTPTDHFRD*GVS*VIWANHNLRASVSAIQQTTKQI 256
Cdd:pfam13714 166 AEAGADGIFVPGLL-DPADIAALVAAV--PGPVNVVPGPGT-LSVAELAALGVARISYGPHLARAAYAALRRAAEEI 238
prpB TIGR02317
methylisocitrate lyase; Members of this family are methylisocitrate lyase, also called (2S,3R) ...
11-283 8.48e-49

methylisocitrate lyase; Members of this family are methylisocitrate lyase, also called (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase. This enzyme acts in propionate metabolism. It cleaves a carbon-carbon bond to convert 2-methylisocitrate to pyruvate plus succinate. Some members of this family have been annotated, incorrectly it seems, as the related protein carboxyphosphoenolpyruvate phosphomutase, which is involved in synthesizing the antibiotic bialaphos in Streptomyces hygroscopicus.


Pssm-ID: 131370  Cd Length: 285  Bit Score: 163.72  E-value: 8.48e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     11 LKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGY 90
Cdd:TIGR02317   5 FRAALAKEDILQIPGAINAMAALLAERAGFEAIYLSGAAVAASLGLPDLGITTLDEVAEDARRITRVTDLPLLVDADTGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     91 GNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGRAqpLADIEEFALKIKACKDSQTDPDFCIVARVEAFiAGWGLD 170
Cdd:TIGR02317  85 GEAFNVARTVREMEDAGAAAVHIEDQVLPKRCGHLPGKE--LVSREEMVDKIAAAVDAKRDEDFVIIARTDAR-AVEGLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    171 EALKRAEAYRNAGADAIL*HSKKADpSDIEAF*KAWnnQGPVVIVPTKYYKTP---TDHFRD*GVS*VIWANHNLRASVS 247
Cdd:TIGR02317 162 AAIERAKAYVEAGADMIFPEALTSL-EEFRQFAKAV--KVPLLANMTEFGKTPlftADELREAGYKMVIYPVTAFRAMNK 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 5822224    248 AIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDE 283
Cdd:TIGR02317 239 AAEAVYNEIKEHGTQKGSLDDMQTRKELYELIGYYD 274
CPEP_Pphonmut TIGR02319
carboxyvinyl-carboxyphosphonate phosphorylmutase; This family consists of ...
5-284 3.02e-28

carboxyvinyl-carboxyphosphonate phosphorylmutase; This family consists of carboxyvinyl-carboxyphosphonate phosphorylmutase (CPEP phosphonomutase), an unusual enzyme involved in the biosynthesis of the antibiotic bialaphos. So far, it is known only in that pathway and only in Streptomyces hygroscopicus. Some related proteins annotated as being functionally equivalent are likely misannotated examples of methylisocitrate lyase, an enzyme of priopionate utilization.


Pssm-ID: 131372  Cd Length: 294  Bit Score: 109.82  E-value: 3.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224      5 VKKTTQLKQ*LNSKDLEFI*EAHNGLSARIVQEAGFKGIWGSGLSVSAQ-LGVRDSNEASWTQVVEVLEF*SDASDVPIL 83
Cdd:TIGR02319   2 VTKARTFRELMNAPEILVVPSAYDALSAKVIQQAGFPAVHMTGSGTSASmLGLPDLGFTSVSEQAINAKNIVLAVDVPVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224     84 LDADTGYGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNSLHDGRAqpLADIEEFALKIKACKDSQTDPDFCIVARVEAF 163
Cdd:TIGR02319  82 MDADAGYGNAMSVWRATREFERVGIVGYHLEDQVNPKRCGHLEGKR--LISTEEMTGKIEAAVEAREDEDFTIIARTDAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    164 iAGWGLDEALKRAEAYRNAGADAIL*HSKkadpSDIEAF*KAWNN-QGPVVIVPTKYYKTP---TDHFRD*GVS*VIWAN 239
Cdd:TIGR02319 160 -ESFGLDEAIRRSREYVAAGADCIFLEAM----LDVEEMKRVRDEiDAPLLANMVEGGKTPwltTKELESIGYNLAIYPL 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 5822224    240 HNLRASVSAIQQ---------TTKQIYDDQSLvnvEDKIVSVKEIFRLQRDDEL 284
Cdd:TIGR02319 235 SGWMAAASVLRKlftelreagTTQKFWDDMGL---KMSFAELFEVFEYSKISEL 285
prpB PRK11320
2-methylisocitrate lyase; Provisional
28-237 4.84e-28

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 109.22  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224    28 NGLSARIVQEAGFKGIWGSGLSVS-AQLGVRDSNEASWTQVVEVLEF*SDASDVPILLDADTGYGNFNNARRLVRKLEDR 106
Cdd:PRK11320  26 NAYHALLAERAGFKAIYLSGGGVAaASLGLPDLGITTLDDVLIDVRRITDACDLPLLVDIDTGFGGAFNIARTVKSMIKA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822224   107 GVAGACLEDKLFPKTNSLHDGRAqpLADIEEFALKIKACKDSQTDPDFCIVARVEAFiAGWGLDEALKRAEAYRNAGADA 186
Cdd:PRK11320 106 GAAAVHIEDQVGAKRCGHRPNKE--IVSQEEMVDRIKAAVDARTDPDFVIMARTDAL-AVEGLDAAIERAQAYVEAGADM 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5822224   187 IL*HSKKaDPSDIEAF*KAWnnQGPVVIVPTKYYKTP---TDHFRD*GVS*VIW 237
Cdd:PRK11320 183 IFPEAMT-ELEMYRRFADAV--KVPILANITEFGATPlftTEELASAGVAMVLY 233
AceA COG2224
Isocitrate lyase [Energy production and conversion];
80-117 6.07e-04

Isocitrate lyase [Energy production and conversion];


Pssm-ID: 225134  Cd Length: 433  Bit Score: 40.79  E-value: 6.07e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 5822224   80 VPILLDADTGYGNFNNARRLVRKLEDRGVAGACLEDKL 117
Cdd:COG2224 153 LPIVADAEAGFGGPLNAFELMKAMIEAGAAGVHFEDQL 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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