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Conserved domains on  [gi|1308472039|gb|PKL03431|]
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carboxyvinyl-carboxyphosphonate phosphorylmutase [Synergistetes bacterium HGW-Synergistetes-2]

Protein Classification

oxaloacetate decarboxylase( domain architecture ID 10789410)

oxaloacetate decarboxylase catalyzes the decarboxylation of oxaloacetate into pyruvate; belongs to the isocitrate lyase/PEP mutase (ICL/PEPM) superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
 3-290 6.13e-149

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


:

Pssm-ID: 442003  Cd Length: 288  Bit Score: 418.77  E-value: 6.13e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   3 KRGAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVPVIA 82
Cdd:COG2513     1 SKRARFRALLASGGILVLPGAWDALSARLAEQAGFEALYLSGAGVAASLLGLPDLGLLTLTEVLEHARRIARAVDLPVIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  83 DGDTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTH 162
Cdd:COG2513    81 DADTGFGNALNVARTVRELERAGVAGIHIEDQVGPKRCGHLPGKEVVPAEEMVERIRAAVDARRDPDFVIIARTDARAVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 163 GIDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAK 242
Cdd:COG2513   161 GLDEAIERAKAYAEAGADVIFVEALTSLEEIRRVAAAVDVPLLANMTEGGKTPLLTAAELAELGVRRVSYPVSLLRAAAK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1308472039 243 AVGAVLETLKRAGTTADCIKDMIPFAEFNALMGLDGIRDMEKKYATGR 290
Cdd:COG2513   241 AAERALRELREDGTQAALLDAMQTFAELYELLGYDEYEALEKRYFKFK 288
 
Name Accession Description Interval E-value
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
 3-290 6.13e-149

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


Pssm-ID: 442003  Cd Length: 288  Bit Score: 418.77  E-value: 6.13e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   3 KRGAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVPVIA 82
Cdd:COG2513     1 SKRARFRALLASGGILVLPGAWDALSARLAEQAGFEALYLSGAGVAASLLGLPDLGLLTLTEVLEHARRIARAVDLPVIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  83 DGDTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTH 162
Cdd:COG2513    81 DADTGFGNALNVARTVRELERAGVAGIHIEDQVGPKRCGHLPGKEVVPAEEMVERIRAAVDARRDPDFVIIARTDARAVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 163 GIDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAK 242
Cdd:COG2513   161 GLDEAIERAKAYAEAGADVIFVEALTSLEEIRRVAAAVDVPLLANMTEGGKTPLLTAAELAELGVRRVSYPVSLLRAAAK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1308472039 243 AVGAVLETLKRAGTTADCIKDMIPFAEFNALMGLDGIRDMEKKYATGR 290
Cdd:COG2513   241 AAERALRELREDGTQAALLDAMQTFAELYELLGYDEYEALEKRYFKFK 288
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
 8-250 9.62e-108

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 [Multi-domain]  Cd Length: 243  Bit Score: 312.89  E-value: 9.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   8 LRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASvLGKPDTGLLSLTEMASRVSAIAETVSVPVIADGDTG 87
Cdd:cd00377     1 LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAAS-LGLPDGGLLTLDEVLAAVRRIARAVDLPVIADADTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  88 YGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRD-DDFLVMARTDAR--TTHGI 164
Cdd:cd00377    80 YGNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGGKVLVPIEEFVAKIKAARDARDDlPDFVIIARTDALlaGEEGL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 165 DEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKtsELEEIGYDIVIFPVGPLYAAAKAV 244
Cdd:cd00377   160 DEAIERAKAYAEAGADGIFVEGLKDPEEIRAFAEAPDVPLNVNMTPGGNLLTVA--ELAELGVRRVSYGLALLRAAAKAM 237


                  ....*.
gi 1308472039 245 GAVLET 250
Cdd:cd00377   238 REAARE 243
prpB TIGR02317
methylisocitrate lyase; Members of this family are methylisocitrate lyase, also called (2S,3R) ...
 4-285 3.59e-106

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: 310.48  E-value: 3.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   4 RGAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASvLGKPDTGLLSLTEMASRVSAIAETVSVPVIAD 83
Cdd:TIGR02317   1 PGKAFRAALAKEDILQIPGAINAMAALLAERAGFEAIYLSGAAVAAS-LGLPDLGITTLDEVAEDARRITRVTDLPLLVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  84 GDTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTHG 163
Cdd:TIGR02317  80 ADTGFGEAFNVARTVREMEDAGAAAVHIEDQVLPKRCGHLPGKELVSREEMVDKIAAAVDAKRDEDFVIIARTDARAVEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 164 IDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAKA 243
Cdd:TIGR02317 160 LDAAIERAKAYVEAGADMIFPEALTSLEEFRQFAKAVKVPLLANMTEFGKTPLFTADELREAGYKMVIYPVTAFRAMNKA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1308472039 244 VGAVLETLKRAGTTADCIKDMIPFAEFNALMGLDgirDMEKK 285
Cdd:TIGR02317 240 AEAVYNEIKEHGTQKGSLDDMQTRKELYELIGYY---DYEKK 278
prpB PRK11320
2-methylisocitrate lyase; Provisional
 5-264 2.52e-78

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 239.80  E-value: 2.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   5 GAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVPVIADG 84
Cdd:PRK11320    6 GARFRAALAAEKPLQIVGTINAYHALLAERAGFKAIYLSGGGVAAASLGLPDLGITTLDDVLIDVRRITDACDLPLLVDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  85 DTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTHGI 164
Cdd:PRK11320   86 DTGFGGAFNIARTVKSMIKAGAAAVHIEDQVGAKRCGHRPNKEIVSQEEMVDRIKAAVDARTDPDFVIMARTDALAVEGL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 165 DEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAKAV 244
Cdd:PRK11320  166 DAAIERAQAYVEAGADMIFPEAMTELEMYRRFADAVKVPILANITEFGATPLFTTEELASAGVAMVLYPLSAFRAMNKAA 245

                         250       260
                  ....*....|....*....|
gi 1308472039 245 GAVLETLKRAGTTADCIKDM 264
Cdd:PRK11320  246 ENVYEAIRRDGTQKAVVDTM 265
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
 8-252 9.51e-56

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterized as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 433424  Cd Length: 241  Bit Score: 180.48  E-value: 9.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   8 LRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASvLGKPDTGLLSLTEMASRVSAIAETVSVPVIADGDTG 87
Cdd:pfam13714   1 FRALHRPGGPLVLPNAWDAASARIVEAAGFPAIATSSAGVAAS-LGYPDGELLPRDELLAAARRIAAAVDLPVSADLETG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  88 YGNAV-NVARTVREYEKAGAACIQLEDQVAPKKCGHMLgreviPAAEMAGKIRAACDARRDD--DFLVMARTDA-RTTHG 163
Cdd:pfam13714  80 YGDSPeEVAETVRRLIAAGVVGVNIEDSKTGRPGGQLL-----DVEEAAARIRAARAAARAAgvPFVINARTDAfLLGRG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 164 --IDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIAnMVEHGRTPFlktSELEEIGYDIVIFPVGPLYAAA 241
Cdd:pfam13714 155 daLEEAIRRARAYAEAGADGIFVPGLLDPADIAALVAAVPGPVNV-LAGPGTLSV---AELAALGVARISYGNHLARAAL 230

                         250
                  ....*....|.
gi 1308472039 242 KAVGAVLETLK 252
Cdd:pfam13714 231 AALRRAAEEIL 241
 
Name Accession Description Interval E-value
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
 3-290 6.13e-149

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


Pssm-ID: 442003  Cd Length: 288  Bit Score: 418.77  E-value: 6.13e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   3 KRGAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVPVIA 82
Cdd:COG2513     1 SKRARFRALLASGGILVLPGAWDALSARLAEQAGFEALYLSGAGVAASLLGLPDLGLLTLTEVLEHARRIARAVDLPVIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  83 DGDTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTH 162
Cdd:COG2513    81 DADTGFGNALNVARTVRELERAGVAGIHIEDQVGPKRCGHLPGKEVVPAEEMVERIRAAVDARRDPDFVIIARTDARAVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 163 GIDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAK 242
Cdd:COG2513   161 GLDEAIERAKAYAEAGADVIFVEALTSLEEIRRVAAAVDVPLLANMTEGGKTPLLTAAELAELGVRRVSYPVSLLRAAAK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1308472039 243 AVGAVLETLKRAGTTADCIKDMIPFAEFNALMGLDGIRDMEKKYATGR 290
Cdd:COG2513   241 AAERALRELREDGTQAALLDAMQTFAELYELLGYDEYEALEKRYFKFK 288
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
 8-250 9.62e-108

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 [Multi-domain]  Cd Length: 243  Bit Score: 312.89  E-value: 9.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   8 LRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASvLGKPDTGLLSLTEMASRVSAIAETVSVPVIADGDTG 87
Cdd:cd00377     1 LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAAS-LGLPDGGLLTLDEVLAAVRRIARAVDLPVIADADTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  88 YGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRD-DDFLVMARTDAR--TTHGI 164
Cdd:cd00377    80 YGNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGGKVLVPIEEFVAKIKAARDARDDlPDFVIIARTDALlaGEEGL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 165 DEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKtsELEEIGYDIVIFPVGPLYAAAKAV 244
Cdd:cd00377   160 DEAIERAKAYAEAGADGIFVEGLKDPEEIRAFAEAPDVPLNVNMTPGGNLLTVA--ELAELGVRRVSYGLALLRAAAKAM 237


                  ....*.
gi 1308472039 245 GAVLET 250
Cdd:cd00377   238 REAARE 243
prpB TIGR02317
methylisocitrate lyase; Members of this family are methylisocitrate lyase, also called (2S,3R) ...
 4-285 3.59e-106

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: 310.48  E-value: 3.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   4 RGAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASvLGKPDTGLLSLTEMASRVSAIAETVSVPVIAD 83
Cdd:TIGR02317   1 PGKAFRAALAKEDILQIPGAINAMAALLAERAGFEAIYLSGAAVAAS-LGLPDLGITTLDEVAEDARRITRVTDLPLLVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  84 GDTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTHG 163
Cdd:TIGR02317  80 ADTGFGEAFNVARTVREMEDAGAAAVHIEDQVLPKRCGHLPGKELVSREEMVDKIAAAVDAKRDEDFVIIARTDARAVEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 164 IDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAKA 243
Cdd:TIGR02317 160 LDAAIERAKAYVEAGADMIFPEALTSLEEFRQFAKAVKVPLLANMTEFGKTPLFTADELREAGYKMVIYPVTAFRAMNKA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1308472039 244 VGAVLETLKRAGTTADCIKDMIPFAEFNALMGLDgirDMEKK 285
Cdd:TIGR02317 240 AEAVYNEIKEHGTQKGSLDDMQTRKELYELIGYY---DYEKK 278
prpB PRK11320
2-methylisocitrate lyase; Provisional
 5-264 2.52e-78

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 239.80  E-value: 2.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   5 GAQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVPVIADG 84
Cdd:PRK11320    6 GARFRAALAAEKPLQIVGTINAYHALLAERAGFKAIYLSGGGVAAASLGLPDLGITTLDDVLIDVRRITDACDLPLLVDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  85 DTGYGNAVNVARTVREYEKAGAACIQLEDQVAPKKCGHMLGREVIPAAEMAGKIRAACDARRDDDFLVMARTDARTTHGI 164
Cdd:PRK11320   86 DTGFGGAFNIARTVKSMIKAGAAAVHIEDQVGAKRCGHRPNKEIVSQEEMVDRIKAAVDARTDPDFVIMARTDALAVEGL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 165 DEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTSELEEIGYDIVIFPVGPLYAAAKAV 244
Cdd:PRK11320  166 DAAIERAQAYVEAGADMIFPEAMTELEMYRRFADAVKVPILANITEFGATPLFTTEELASAGVAMVLYPLSAFRAMNKAA 245

                         250       260
                  ....*....|....*....|
gi 1308472039 245 GAVLETLKRAGTTADCIKDM 264
Cdd:PRK11320  246 ENVYEAIRRDGTQKAVVDTM 265
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
 8-252 9.51e-56

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterized as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 433424  Cd Length: 241  Bit Score: 180.48  E-value: 9.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   8 LRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGYGLSASvLGKPDTGLLSLTEMASRVSAIAETVSVPVIADGDTG 87
Cdd:pfam13714   1 FRALHRPGGPLVLPNAWDAASARIVEAAGFPAIATSSAGVAAS-LGYPDGELLPRDELLAAARRIAAAVDLPVSADLETG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  88 YGNAV-NVARTVREYEKAGAACIQLEDQVAPKKCGHMLgreviPAAEMAGKIRAACDARRDD--DFLVMARTDA-RTTHG 163
Cdd:pfam13714  80 YGDSPeEVAETVRRLIAAGVVGVNIEDSKTGRPGGQLL-----DVEEAAARIRAARAAARAAgvPFVINARTDAfLLGRG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 164 --IDEAVERGALYEEAGADILFIESPESLEEMRRITSSFGVPVIAnMVEHGRTPFlktSELEEIGYDIVIFPVGPLYAAA 241
Cdd:pfam13714 155 daLEEAIRRARAYAEAGADGIFVPGLLDPADIAALVAAVPGPVNV-LAGPGTLSV---AELAALGVARISYGNHLARAAL 230

                         250
                  ....*....|.
gi 1308472039 242 KAVGAVLETLK 252
Cdd:pfam13714 231 AALRRAAEEIL 241
isocit_lyase TIGR01346
isocitrate lyase; Isocitrate lyase and malate synthase are the enzymes of the glyoxylate shunt, ...
 78-158 3.62e-15

isocitrate lyase; Isocitrate lyase and malate synthase are the enzymes of the glyoxylate shunt, a pathway associated with the TCA cycle. [Energy metabolism, TCA cycle]


Pssm-ID: 273564 [Multi-domain]  Cd Length: 527  Bit Score: 75.49  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  78 VPVIADGDTGYGNAVNVARTVREYEKAGAACIQLEDQVAP-KKCGHMLGREVIPAAEMAGKIRAA--CDARRDDDFLVMA 154
Cdd:TIGR01346 151 VPIVADGDAGFGGATAVFKLQKAFIERGAAGVHWEDQLSSeKKCGHMAGKVLIPVQEHVNRLVAArlAADIMGVPTLVVA 230


                  ....
gi 1308472039 155 RTDA 158
Cdd:TIGR01346 231 RTDA 234
ICL_KPHMT cd06556
Members of the ICL/PEPM_KPHMT enzyme superfamily catalyze the formation and cleavage of either ...
 22-207 7.99e-15

Members of the ICL/PEPM_KPHMT enzyme superfamily catalyze the formation and cleavage of either P-C or C-C bonds. Typical members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), 2-methylisocitrate lyase (MICL), and ketopantoate hydroxymethyltransferase (KPHMT).


Pssm-ID: 119341 [Multi-domain]  Cd Length: 240  Bit Score: 72.26  E-value: 7.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  22 GAYDGLSARLVESAGFEAVYVTGYgLSASVLGKPDTGLLSLTEMASRVSAIAETVSV-PVIADGDTG-YGNAVNVARTVR 99
Cdd:cd06556    18 TAYDYSMAKQFADAGLNVMLVGDS-QGMTVAGYDDTLPYPVNDVPYHVRAVRRGAPLaLIVADLPFGaYGAPTAAFELAK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 100 EYEKAGAACIQLEDQvapkkcghmlgrevipaAEMAGKIRAAcdarRDDDFLVMARTDA---------------RTTHGI 164
Cdd:cd06556    97 TFMRAGAAGVKIEGG-----------------EWHIETLQML----TAAAVPVIAHTGLtpqsvntsggdegqyRGDEAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1308472039 165 DEAVERGALYEEAGADILFIESPEsLEEMRRITSSFGVPVIAN 207
Cdd:cd06556   156 EQLIADALAYAPAGADLIVMECVP-VELAKQITEALAIPLAGI 197
PRK15063 PRK15063
isocitrate lyase; Provisional
 3-195 3.34e-14

isocitrate lyase; Provisional


Pssm-ID: 237893  Cd Length: 428  Bit Score: 72.19  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   3 KRGAQ-LRKLLARREILVAPGAYDGLSARLVESAGFEAVYVTGY------GLSASVLgkPDTGLL---SLTEMASRVS-- 70
Cdd:PRK15063   49 RRGAEkLWELLHGEPYVNALGALTGNQAVQQVKAGLKAIYLSGWqvaadaNLAGQMY--PDQSLYpanSVPAVVKRINna 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  71 -------AIAETVS------VPVIADGDTGYGNAVNVARTVREYEKAGAACIQLEDQVAP-KKCGHMLGREVIPAAEMAG 136
Cdd:PRK15063  127 lrradqiQWSEGDKgyidyfAPIVADAEAGFGGVLNAFELMKAMIEAGAAGVHFEDQLASeKKCGHMGGKVLVPTQEAIR 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 137 KIRAacdARRDDDF-----LVMARTDA----------------------------RTTHGIDEAVERGALYEEAgADILF 183
Cdd:PRK15063  207 KLVA---ARLAADVmgvptLVIARTDAeaadlltsdvderdrpfitgertaegfyRVKAGIEQAIARGLAYAPY-ADLIW 282

                         250
                  ....*....|...
gi 1308472039 184 IESPE-SLEEMRR 195
Cdd:PRK15063  283 CETSTpDLEEARR 295
PRK06498 PRK06498
isocitrate lyase; Provisional
 74-157 2.46e-13

isocitrate lyase; Provisional


Pssm-ID: 180592 [Multi-domain]  Cd Length: 531  Bit Score: 70.07  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  74 ETVSVPVIADGDTGYGNAVNVARTVREYEKAGAACIQLEDQVA-PKKCGHMLGREVIPAAEMAGKIRAACDARRD---DD 149
Cdd:PRK06498  175 ETHVVPIIADIDAGFGNEEATYLLAKKMIEAGACCIQIENQVSdEKQCGHQDGKVTVPHEDFLAKIRAVRYAFLElgvDD 254


                  ....*...
gi 1308472039 150 FLVMARTD 157
Cdd:PRK06498  255 GVIVARTD 262
ICL pfam00463
Isocitrate lyase family;
79-158 5.75e-13

Isocitrate lyase family;


Pssm-ID: 278869 [Multi-domain]  Cd Length: 526  Bit Score: 68.71  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  79 PVIADGDTGYGNAVNVARTVREYEKAGAACIQLEDQvAP--KKCGHMLGREVIPAAEMAGK---IRAACDArRDDDFLVM 153
Cdd:pfam00463 151 PIIADADTGHGGLTAVVKLTKLFIERGAAGIHIEDQ-APgtKKCGHMAGKVLVPIQEHINRlvaIRAQADI-MGSDLLAV 228


                  ....*
gi 1308472039 154 ARTDA 158
Cdd:pfam00463 229 ARTDS 233
AceA COG2224
Isocitrate lyase [Energy production and conversion]; Isocitrate lyase is part of the Pathway ...
 78-195 8.56e-13

Isocitrate lyase [Energy production and conversion]; Isocitrate lyase is part of the Pathway/BioSystem: TCA cycle, glyoxylate bypass


Pssm-ID: 441826  Cd Length: 425  Bit Score: 67.94  E-value: 8.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  78 VPVIADGDTGYGNAVNVARTVREYEKAGAACIQLEDQVAP-KKCGHMLGREVIPAAEMAGKIRAacdARRDDDF-----L 151
Cdd:COG2224   145 APIVADAEAGFGGPLNAFELMKAMIEAGAAGVHFEDQLASeKKCGHLGGKVLVPTQEAIRKLNA---ARLAADVmgvptL 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308472039 152 VMARTDA----------------------------RTTHGIDEAVERGALYEEAgADILFIE-SPESLEEMRR 195
Cdd:COG2224   222 IIARTDAeaatlltsdiderdrpfltgertaegfyRVKNGIEQAIARGLAYAPY-ADLIWCEtSTPDLEEARR 293
PLN02892 PLN02892
isocitrate lyase
 79-169 5.10e-11

isocitrate lyase


Pssm-ID: 215482 [Multi-domain]  Cd Length: 570  Bit Score: 62.92  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  79 PVIADGDTGYGNAVNVARTVREYEKAGAACIQLEDQVA-PKKCGHMLGREVIPAAEMAGKIRAacdARRDDDFL-----V 152
Cdd:PLN02892  171 PIIADGDTGFGGTTATVKLCKLFVERGAAGVHIEDQSSvTKKCGHMGGKVLVATSEHINRLVA---ARLQFDVMgvetvL 247

                          90
                  ....*....|....*..
gi 1308472039 153 MARTDARTTHGIDEAVE 169
Cdd:PLN02892  248 VARTDAVAATLIQSNID 264
Pantoate_transf pfam02548
Ketopantoate hydroxymethyltransferase; Ketopantoate hydroxymethyltransferase (EC:2.1.2.11) is ...
 6-205 1.37e-05

Ketopantoate hydroxymethyltransferase; Ketopantoate hydroxymethyltransferase (EC:2.1.2.11) is the first enzyme in the pantothenate biosynthesis pathway.


Pssm-ID: 460588  Cd Length: 259  Bit Score: 45.40  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   6 AQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVtGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVP-VIAD- 83
Cdd:pfam02548   5 PDLQKMKARGEKITMLTAYDYPTARLADEAGVDIILV-GDSLGMVVLGYESTLPVTLDEMIYHTKAVRRGAKRAlVVADm 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  84 --------GDTGYGNAvnvARTVREyekAGAACIQLEdqvapkkcghmlGrevipAAEMAGKIRAACDArrddDFLVMA- 154
Cdd:pfam02548  84 pfgsyqasPEQAVRNA---GRLMKE---GGADAVKLE------------G-----GAEVAETIKALVDA----GIPVMGh 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308472039 155 --------------RTDARTTHGIDEAVERGALYEEAGADILFIE-SPESLeeMRRITSSFGVPVI 205
Cdd:pfam02548 137 igltpqsvnqlggyKVQGKTEEAAEKLLEDAKALEEAGAFALVLEcVPAEL--AAEITEALSIPTI 200
KPHMT-like cd06557
Ketopantoate hydroxymethyltransferase (KPHMT) is the first enzyme in the pantothenate ...
 6-205 3.38e-05

Ketopantoate hydroxymethyltransferase (KPHMT) is the first enzyme in the pantothenate biosynthesis pathway. Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first committed step in the biosynthesis of pantothenate (vitamin B5), which is a precursor to coenzyme A and is required for penicillin biosynthesis.


Pssm-ID: 119342  Cd Length: 254  Bit Score: 44.33  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039   6 AQLRKLLARREILVAPGAYDGLSARLVESAGFEAVYVtGYGLSASVLGKPDTGLLSLTEMASRVSAIAETVSVP-VIAD- 83
Cdd:cd06557     2 PDLQKMKKAGEKIVMLTAYDYPTAKLADEAGVDVILV-GDSLGMVVLGYDSTLPVTLDEMIYHTRAVRRGAPRAlVVADm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  84 ----GDTGYGNAV-NVARTVREyekAGAACIQLEdqvapkkcghmlgreviPAAEMAGKIRAACDArrddDFLVMA---- 154
Cdd:cd06557    81 pfgsYQTSPEQALrNAARLMKE---AGADAVKLE-----------------GGAEVAETIRALVDA----GIPVMGhigl 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308472039 155 -----------RTDARTTHGIDEAVERGALYEEAGADILFIE-SPESLEemRRITSSFGVPVI 205
Cdd:cd06557   137 tpqsvnqlggyKVQGKTEEEAERLLEDALALEEAGAFALVLEcVPAELA--KEITEALSIPTI 197
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 138-216 3.36e-03

Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.


Pssm-ID: 463862 [Multi-domain]  Cd Length: 217  Bit Score: 37.93  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 138 IRAACDARRDDDFLvmaRTDARTTHGIDEAVERGALYEEAgaDILFIE---SPESLEEMRRITSSFGVPVIANMVEHGRT 214
Cdd:pfam13378  34 VRAVREAVGPGVDL---MVDANGAWSVAEAIRLARALEEL--GLLWIEepvPPDDLEGLARLRRATPVPIATGESLYSRE 108


                  ..
gi 1308472039 215 PF 216
Cdd:pfam13378 109 DF 110
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 79-230 3.90e-03

L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 443975 [Multi-domain]  Cd Length: 359  Bit Score: 38.26  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  79 PVIADGDTGYGNAVNVARTVREYEKAGAACIQLedqvapkKCGHMLGREVIpaaEMAGKIRAACDarrdDDFLVMArtDA 158
Cdd:COG4948   126 RVPVYATLGIDTPEEMAEEAREAVARGFRALKL-------KVGGPDPEEDV---ERVRAVREAVG----PDARLRV--DA 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308472039 159 RTTHGIDEAVERGALYEEAGadILFIE---SPESLEEMRRITSSFGVPVIANMVEHGRTPFLKTseLEEIGYDIV 230
Cdd:COG4948   190 NGAWTLEEAIRLLRALEDLG--LEWIEqplPAEDLEGLAELRRATPVPIAADESLTSRADFRRL--IEAGAVDIV 260
PRK08645 PRK08645
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ...
 79-259 8.93e-03

bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed


Pssm-ID: 236321 [Multi-domain]  Cd Length: 612  Bit Score: 37.52  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039  79 PVIADGDTG-----YGNAVN-------------VARTVREYEKAGAACIQ---------------LEDQVapkkcghmlg 125
Cdd:PRK08645   12 VLIADGAMGtllysRGVPLDrcfeelnlshpelILRIHREYIEAGADVIQtntfganriklkrygLEDKV---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 126 REVIPAAemagkIRAACDARRDDDFL--------VMARTDARTTHGIDEAVER--GALYEEaGADILFIESPESLEEM-- 193
Cdd:PRK08645   82 KEINRAA-----VRLAREAAGDDVYVagtigpigGRGPLGDISLEEIRREFREqiDALLEE-GVDGLLLETFYDLEELll 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308472039 194 -----RRITSsfgVPVIANMV--EHGRTPFLKT-----SELEEIGYDIVIF--PVGPLyaaakavgAVLETLKRAGTTAD 259
Cdd:PRK08645  156 aleaaREKTD---LPIIAQVAfhEDGVTQNGTSleealKELVAAGADVVGLncGLGPY--------HMLEALERIPIPEN 224
 
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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