NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495778828|ref|WP_008503407|]
View 

MULTISPECIES: isocitrate lyase [Enterobacter]

Protein Classification

isocitrate lyase( domain architecture ID 10794123)

isocitrate lyase catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates

EC:  4.1.3.1
Gene Ontology:  GO:0046872|GO:0004451

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK15063 PRK15063
isocitrate lyase; Provisional
1-434 0e+00

isocitrate lyase; Provisional


:

Pssm-ID: 237893  Cd Length: 428  Bit Score: 933.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   1 MKTRTQQIEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHGgskKGYINSLGALTGGQALQ 79
Cdd:PRK15063   2 MMTRTQQIEELEKDWaTNPRWKGITRPYSAEDVVRLRGSVQIEHTLARRGAEKLWELLHG---EPYVNALGALTGNQAVQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  80 QAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGiepnDPRFIDYFLPIVADAE 159
Cdd:PRK15063  79 QVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVKRINNALRRADQIQWSEG----DKGYIDYFAPIVADAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 160 AGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAAD 239
Cdd:PRK15063 155 AGFGGVLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHMGGKVLVPTQEAIRKLVAARLAADVMGVPTLVIARTDAEAAD 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 240 LITSDCDPYDSEFITGERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFADAIHAKYPGKLLAYNCS 319
Cdd:PRK15063 235 LLTSDVDERDRPFITGERTAEGFYRVKAGIEQAIARGLAYAPYADLIWCETSTPDLEEARRFAEAIHAKFPGKLLAYNCS 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 320 PSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEkVQQPEFAAGKDGYTFVSH 399
Cdd:PRK15063 315 PSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHSLNYSMFDLAHGYAR-EGMAAYVE-LQEAEFAAEERGYTAVKH 392
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495778828 400 QQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:PRK15063 393 QREVGTGYFDAVTTVIQGGQSSTTALTGSTEEEQF 427
 
Name Accession Description Interval E-value
PRK15063 PRK15063
isocitrate lyase; Provisional
1-434 0e+00

isocitrate lyase; Provisional


Pssm-ID: 237893  Cd Length: 428  Bit Score: 933.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   1 MKTRTQQIEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHGgskKGYINSLGALTGGQALQ 79
Cdd:PRK15063   2 MMTRTQQIEELEKDWaTNPRWKGITRPYSAEDVVRLRGSVQIEHTLARRGAEKLWELLHG---EPYVNALGALTGNQAVQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  80 QAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGiepnDPRFIDYFLPIVADAE 159
Cdd:PRK15063  79 QVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVKRINNALRRADQIQWSEG----DKGYIDYFAPIVADAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 160 AGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAAD 239
Cdd:PRK15063 155 AGFGGVLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHMGGKVLVPTQEAIRKLVAARLAADVMGVPTLVIARTDAEAAD 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 240 LITSDCDPYDSEFITGERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFADAIHAKYPGKLLAYNCS 319
Cdd:PRK15063 235 LLTSDVDERDRPFITGERTAEGFYRVKAGIEQAIARGLAYAPYADLIWCETSTPDLEEARRFAEAIHAKFPGKLLAYNCS 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 320 PSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEkVQQPEFAAGKDGYTFVSH 399
Cdd:PRK15063 315 PSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHSLNYSMFDLAHGYAR-EGMAAYVE-LQEAEFAAEERGYTAVKH 392
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495778828 400 QQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:PRK15063 393 QREVGTGYFDAVTTVIQGGQSSTTALTGSTEEEQF 427
AceA COG2224
Isocitrate lyase [Energy production and conversion]; Isocitrate lyase is part of the Pathway ...
1-434 0e+00

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: 898.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   1 MKTRTQQIEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHGgskKGYINSLGALTGGQALQ 79
Cdd:COG2224    1 MMTRQQTAAELEKDWaTNPRWKGIKRPYTAEDVVRLRGSVQIEHTLARRGAERLWELLHT---EDYVNALGALTGNQAVQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  80 QAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGiepndPRFIDYFLPIVADAE 159
Cdd:COG2224   78 QVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVRRINNALLRADQIQHAEG-----KDDIDWFAPIVADAE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 160 AGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAAD 239
Cdd:COG2224  153 AGFGGPLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHLGGKVLVPTQEAIRKLNAARLAADVMGVPTLIIARTDAEAAT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 240 LITSDCDPYDSEFITGERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFADAIHAKYPGKLLAYNCS 319
Cdd:COG2224  233 LLTSDIDERDRPFLTGERTAEGFYRVKNGIEQAIARGLAYAPYADLIWCETSTPDLEEARRFAEAIHAKFPGKLLAYNCS 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 320 PSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEkVQQPEFAAGKDGYTFVSH 399
Cdd:COG2224  313 PSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHALNYSMFELARGYAE-RGMAAYVE-LQEAEFAAEKRGYTATKH 390
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495778828 400 QQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:COG2224  391 QREVGTGYFDEVATAISGGQSSTTALKGSTEEEQF 425
isocit_lyase TIGR01346
isocitrate lyase; Isocitrate lyase and malate synthase are the enzymes of the glyoxylate shunt, ...
8-434 0e+00

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: 685.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828    8 IEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHG-GSKKGYINSLGALTGGQALQQAKAgI 85
Cdd:TIGR01346   1 AQEIQKWWdTNPRWNGTTRPYTARDVADLRGSVIPEHYLSRRMAEKLWRALTQhGDNKTYSNTFGALDPVQASQMAKY-L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   86 EAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGIEPNDPR-----FIDYFLPIVADAEA 160
Cdd:TIGR01346  80 DAIYLSGWQCSSTANTSNEPGPDLADYPADTVPNKVEHLFNAQLFHDRKQREARDTSVDNErsktpYIDYLVPIVADGDA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  161 GFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAADL 240
Cdd:TIGR01346 160 GFGGATAVFKLQKAFIERGAAGVHWEDQLSSEKKCGHMAGKVLIPVQEHVNRLVAARLAADIMGVPTLVVARTDAEAATL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  241 ITSDCDPYDSEFITG----------------------------------------------------------------- 255
Cdd:TIGR01346 240 ITSDVDERDHPFITGatnpnlkpladvlaramasgksgadlqavedewmamadlklfsdcvvdgikalnvsekgrrlgew 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  256 ---------------------------------ERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFA 302
Cdd:TIGR01346 320 mqqtntgnvlsyyqakelaeklgisnlfwdwdlPRTREGFYRVKGGLEPAIARAKAFAPYADLIWMETSTPDLELAKKFA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  303 DAIHAKYPGKLLAYNCSPSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEKV 382
Cdd:TIGR01346 400 EGVKSKFPDQLLAYNLSPSFNWSAHMEDDEIAKFIQELGDLGYKWQFITLAGFHSLALGMFDFAYDFAQ-EGMKAYVEKV 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495778828  383 QQPEFaagKDGYTFVSHQQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:TIGR01346 479 QQREM---EDGVDALKHQKWSGAGYFDQLLKTVQGGNSATAAMKGGVTEDQF 527
ICL pfam00463
Isocitrate lyase family;
7-434 9.35e-116

Isocitrate lyase family;


Pssm-ID: 278869 [Multi-domain]  Cd Length: 526  Bit Score: 348.75  E-value: 9.35e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828    7 QIEELKKEWTQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNgAAKMWKLLHGGSKKGYIN-SLGALTGGQALQQAKAgI 85
Cdd:pfam00463   1 EVAEVKKWWSDSRWRKTKRPYTAEDIVSKRGNLKIEYASNVQ-AKKLWKLLENHFANGTASfTFGALDPVQVTQMAKY-L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   86 EAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGIE-PNDPR----FIDYFLPIVADAEA 160
Cdd:pfam00463  79 DTIYVSGWQCSSTASTSNEPGPDLADYPMDTVPNKVEHLFFAQLFHDRKQREERLSmPKEERaktaYVDYLRPIIADADT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  161 GFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAADL 240
Cdd:pfam00463 159 GHGGLTAVVKLTKLFIERGAAGIHIEDQAPGTKKCGHMAGKVLVPIQEHINRLVAIRAQADIMGSDLLAVARTDSEAATL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  241 ITSDCDPYDSEFITG----------------------------------------------------------------- 255
Cdd:pfam00463 239 ITSTIDTRDHYFILGatnpdlepladlmvqaeaagkngaelqaiedewlrkaglklfheavvdeiergnlsnkkelikkf 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  256 ---------------------------------ERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFA 302
Cdd:pfam00463 319 thkvkplsctsnrearaiakellgkdiffdwelPRTREGYYRYQGGTQCSVNRGRAFAPYADLIWMESKLPDYAQAKEFA 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  303 DAIHAKYPGKLLAYNCSPSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEKV 382
Cdd:pfam00463 399 EGVKAKWPDQWLAYNLSPSFNWKKAMSRDEQETYIKRLAKLGYVWQFITLAGLHTNALISDTFAKAYAK-RGMRAYGELV 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495778828  383 QQPEFAAGKDgytFVSHQQEVGTGYFDNVTTIIQGGTSSVTAL-TGSTEEaQF 434
Cdd:pfam00463 478 QQPEIDNGVD---VVKHQKWSGANYIDGLLKMVTGGVSSTAAMgKGVTED-QF 526
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
53-368 1.16e-77

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: 241.24  E-value: 1.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  53 MWKLLHGGskkGYINSLGALTGGQALQQAKAGIEAIYLSGWQVAAdanlaSSMYPDQSLYPANSVPSVVDRINNTFRrad 132
Cdd:cd00377    1 LRALLESG---GPLVLPGAWDALSARLAERAGFKAIYTSGAGVAA-----SLGLPDGGLLTLDEVLAAVRRIARAVD--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 133 qiqwaagiepndprfidyfLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASvKKCGHMGGKVLVPTQEAVQK 212
Cdd:cd00377   70 -------------------LPVIADADTGYGNALNVARTVRELEEAGAAGIHIEDQVGP-KKCGHHGGKVLVPIEEFVAK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 213 LVAARLAADVLgVPTLVIARTDADAADlitsdcdpydsefitgertsegfyrtHAGIEQAISRGLAYAPY-ADLVWCETS 291
Cdd:cd00377  130 IKAARDARDDL-PDFVIIARTDALLAG--------------------------EEGLDEAIERAKAYAEAgADGIFVEGL 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778828 292 TpDLALAKRFADAihakyPGKLLAYNCSPSFNwqkklddktiASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHA 368
Cdd:cd00377  183 K-DPEEIRAFAEA-----PDVPLNVNMTPGGN----------LLTVAELAELGVRRVSYGLALLRAAAKAMREAARE 243
 
Name Accession Description Interval E-value
PRK15063 PRK15063
isocitrate lyase; Provisional
1-434 0e+00

isocitrate lyase; Provisional


Pssm-ID: 237893  Cd Length: 428  Bit Score: 933.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   1 MKTRTQQIEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHGgskKGYINSLGALTGGQALQ 79
Cdd:PRK15063   2 MMTRTQQIEELEKDWaTNPRWKGITRPYSAEDVVRLRGSVQIEHTLARRGAEKLWELLHG---EPYVNALGALTGNQAVQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  80 QAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGiepnDPRFIDYFLPIVADAE 159
Cdd:PRK15063  79 QVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVKRINNALRRADQIQWSEG----DKGYIDYFAPIVADAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 160 AGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAAD 239
Cdd:PRK15063 155 AGFGGVLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHMGGKVLVPTQEAIRKLVAARLAADVMGVPTLVIARTDAEAAD 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 240 LITSDCDPYDSEFITGERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFADAIHAKYPGKLLAYNCS 319
Cdd:PRK15063 235 LLTSDVDERDRPFITGERTAEGFYRVKAGIEQAIARGLAYAPYADLIWCETSTPDLEEARRFAEAIHAKFPGKLLAYNCS 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 320 PSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEkVQQPEFAAGKDGYTFVSH 399
Cdd:PRK15063 315 PSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHSLNYSMFDLAHGYAR-EGMAAYVE-LQEAEFAAEERGYTAVKH 392
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495778828 400 QQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:PRK15063 393 QREVGTGYFDAVTTVIQGGQSSTTALTGSTEEEQF 427
AceA COG2224
Isocitrate lyase [Energy production and conversion]; Isocitrate lyase is part of the Pathway ...
1-434 0e+00

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: 898.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   1 MKTRTQQIEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHGgskKGYINSLGALTGGQALQ 79
Cdd:COG2224    1 MMTRQQTAAELEKDWaTNPRWKGIKRPYTAEDVVRLRGSVQIEHTLARRGAERLWELLHT---EDYVNALGALTGNQAVQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  80 QAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGiepndPRFIDYFLPIVADAE 159
Cdd:COG2224   78 QVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVRRINNALLRADQIQHAEG-----KDDIDWFAPIVADAE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 160 AGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAAD 239
Cdd:COG2224  153 AGFGGPLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHLGGKVLVPTQEAIRKLNAARLAADVMGVPTLIIARTDAEAAT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 240 LITSDCDPYDSEFITGERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFADAIHAKYPGKLLAYNCS 319
Cdd:COG2224  233 LLTSDIDERDRPFLTGERTAEGFYRVKNGIEQAIARGLAYAPYADLIWCETSTPDLEEARRFAEAIHAKFPGKLLAYNCS 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 320 PSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEkVQQPEFAAGKDGYTFVSH 399
Cdd:COG2224  313 PSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHALNYSMFELARGYAE-RGMAAYVE-LQEAEFAAEKRGYTATKH 390
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495778828 400 QQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:COG2224  391 QREVGTGYFDEVATAISGGQSSTTALKGSTEEEQF 425
isocit_lyase TIGR01346
isocitrate lyase; Isocitrate lyase and malate synthase are the enzymes of the glyoxylate shunt, ...
8-434 0e+00

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: 685.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828    8 IEELKKEW-TQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNGAAKMWKLLHG-GSKKGYINSLGALTGGQALQQAKAgI 85
Cdd:TIGR01346   1 AQEIQKWWdTNPRWNGTTRPYTARDVADLRGSVIPEHYLSRRMAEKLWRALTQhGDNKTYSNTFGALDPVQASQMAKY-L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   86 EAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGIEPNDPR-----FIDYFLPIVADAEA 160
Cdd:TIGR01346  80 DAIYLSGWQCSSTANTSNEPGPDLADYPADTVPNKVEHLFNAQLFHDRKQREARDTSVDNErsktpYIDYLVPIVADGDA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  161 GFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAADL 240
Cdd:TIGR01346 160 GFGGATAVFKLQKAFIERGAAGVHWEDQLSSEKKCGHMAGKVLIPVQEHVNRLVAARLAADIMGVPTLVVARTDAEAATL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  241 ITSDCDPYDSEFITG----------------------------------------------------------------- 255
Cdd:TIGR01346 240 ITSDVDERDHPFITGatnpnlkpladvlaramasgksgadlqavedewmamadlklfsdcvvdgikalnvsekgrrlgew 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  256 ---------------------------------ERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFA 302
Cdd:TIGR01346 320 mqqtntgnvlsyyqakelaeklgisnlfwdwdlPRTREGFYRVKGGLEPAIARAKAFAPYADLIWMETSTPDLELAKKFA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  303 DAIHAKYPGKLLAYNCSPSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEKV 382
Cdd:TIGR01346 400 EGVKSKFPDQLLAYNLSPSFNWSAHMEDDEIAKFIQELGDLGYKWQFITLAGFHSLALGMFDFAYDFAQ-EGMKAYVEKV 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495778828  383 QQPEFaagKDGYTFVSHQQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:TIGR01346 479 QQREM---EDGVDALKHQKWSGAGYFDQLLKTVQGGNSATAAMKGGVTEDQF 527
PLN02892 PLN02892
isocitrate lyase
7-434 1.18e-116

isocitrate lyase


Pssm-ID: 215482 [Multi-domain]  Cd Length: 570  Bit Score: 352.59  E-value: 1.18e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   7 QIEELKKEWTQPRWEGIRRPYSAEDVVKLRGSVnPECTLAQNGAAKMWKLLHG-GSKKGYINSLGALTGGQALQQAKAgI 85
Cdd:PLN02892  21 EVAEVEAWWRSERFKLTRRPYSARDVAALRGTL-KQSYASNEMAKKLWRTLKThQANGTASRTFGALDPVQVAQMAKH-L 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  86 EAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRInntF-------RRADQIQWAAGIEPNDPR-FIDYFLPIVAD 157
Cdd:PLN02892  99 DTIYVSGWQCSSTATSTNEPGPDLADYPMDTVPNKVEHL---FfaqlyhdRKQREARMSMSREERARTpYVDYLKPIIAD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 158 AEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADA 237
Cdd:PLN02892 176 GDTGFGGTTATVKLCKLFVERGAAGVHIEDQSSVTKKCGHMGGKVLVATSEHINRLVAARLQFDVMGVETVLVARTDAVA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 238 ADLITSDCDPYDSEFITGE------------------------------------------------------------- 256
Cdd:PLN02892 256 ATLIQSNIDARDHQFILGAtnpalrgkplatllaeamaagksgaelqaiedewlaqaqlmtfseavadaiksmnisenek 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 257 ---------------------------------------RTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLAL 297
Cdd:PLN02892 336 rrrlnewmasvpkclsneqarriaaklgvanvfwdwdlpRTREGFYRFRGSVKACIVRGRAFAPYADLIWMETASPDLAE 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 298 AKRFADAIHAKYPGKLLAYNCSPSFNWQKK-LDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMK 376
Cdd:PLN02892 416 ATKFAEGVKAKHPEIMLAYNLSPSFNWDASgMTDEQMAEFIPRLARLGYCWQFITLAGFHANALVVDTFARDYAR-RGML 494
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495778828 377 HYVEKVQQPEfaaGKDGYTFVSHQQEVGTGYFDNVTTIIQGGTSSVTALTGSTEEAQF 434
Cdd:PLN02892 495 AYVERIQRQE---RTNGVETLAHQKWSGANYYDRYLKTVQGGISSTAAMGKGVTEEQF 549
ICL pfam00463
Isocitrate lyase family;
7-434 9.35e-116

Isocitrate lyase family;


Pssm-ID: 278869 [Multi-domain]  Cd Length: 526  Bit Score: 348.75  E-value: 9.35e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828    7 QIEELKKEWTQPRWEGIRRPYSAEDVVKLRGSVNPECTLAQNgAAKMWKLLHGGSKKGYIN-SLGALTGGQALQQAKAgI 85
Cdd:pfam00463   1 EVAEVKKWWSDSRWRKTKRPYTAEDIVSKRGNLKIEYASNVQ-AKKLWKLLENHFANGTASfTFGALDPVQVTQMAKY-L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   86 EAIYLSGWQVAADANLASSMYPDQSLYPANSVPSVVDRINNTFRRADQIQWAAGIE-PNDPR----FIDYFLPIVADAEA 160
Cdd:pfam00463  79 DTIYVSGWQCSSTASTSNEPGPDLADYPMDTVPNKVEHLFFAQLFHDRKQREERLSmPKEERaktaYVDYLRPIIADADT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  161 GFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDADAADL 240
Cdd:pfam00463 159 GHGGLTAVVKLTKLFIERGAAGIHIEDQAPGTKKCGHMAGKVLVPIQEHINRLVAIRAQADIMGSDLLAVARTDSEAATL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  241 ITSDCDPYDSEFITG----------------------------------------------------------------- 255
Cdd:pfam00463 239 ITSTIDTRDHYFILGatnpdlepladlmvqaeaagkngaelqaiedewlrkaglklfheavvdeiergnlsnkkelikkf 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  256 ---------------------------------ERTSEGFYRTHAGIEQAISRGLAYAPYADLVWCETSTPDLALAKRFA 302
Cdd:pfam00463 319 thkvkplsctsnrearaiakellgkdiffdwelPRTREGYYRYQGGTQCSVNRGRAFAPYADLIWMESKLPDYAQAKEFA 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  303 DAIHAKYPGKLLAYNCSPSFNWQKKLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQgEGMKHYVEKV 382
Cdd:pfam00463 399 EGVKAKWPDQWLAYNLSPSFNWKKAMSRDEQETYIKRLAKLGYVWQFITLAGLHTNALISDTFAKAYAK-RGMRAYGELV 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495778828  383 QQPEFAAGKDgytFVSHQQEVGTGYFDNVTTIIQGGTSSVTAL-TGSTEEaQF 434
Cdd:pfam00463 478 QQPEIDNGVD---VVKHQKWSGANYIDGLLKMVTGGVSSTAAMgKGVTED-QF 526
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
53-368 1.16e-77

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: 241.24  E-value: 1.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  53 MWKLLHGGskkGYINSLGALTGGQALQQAKAGIEAIYLSGWQVAAdanlaSSMYPDQSLYPANSVPSVVDRINNTFRrad 132
Cdd:cd00377    1 LRALLESG---GPLVLPGAWDALSARLAERAGFKAIYTSGAGVAA-----SLGLPDGGLLTLDEVLAAVRRIARAVD--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 133 qiqwaagiepndprfidyfLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASvKKCGHMGGKVLVPTQEAVQK 212
Cdd:cd00377   70 -------------------LPVIADADTGYGNALNVARTVRELEEAGAAGIHIEDQVGP-KKCGHHGGKVLVPIEEFVAK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 213 LVAARLAADVLgVPTLVIARTDADAADlitsdcdpydsefitgertsegfyrtHAGIEQAISRGLAYAPY-ADLVWCETS 291
Cdd:cd00377  130 IKAARDARDDL-PDFVIIARTDALLAG--------------------------EEGLDEAIERAKAYAEAgADGIFVEGL 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778828 292 TpDLALAKRFADAihakyPGKLLAYNCSPSFNwqkklddktiASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHA 368
Cdd:cd00377  183 K-DPEEIRAFAEA-----PDVPLNVNMTPGGN----------LLTVAELAELGVRRVSYGLALLRAAAKAMREAARE 243
ICL_KPHMT cd06556
Members of the ICL/PEPM_KPHMT enzyme superfamily catalyze the formation and cleavage of either ...
53-354 5.22e-49

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: 167.02  E-value: 5.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  53 MWKLLHGGSKKGYINSLGALTGGQALQQAKAGIEAIYLSGWQVAADANlassmYPDQSLYPANSVPSVVDRINNTFRRAd 132
Cdd:cd06556    1 LWLLQKYKQEKERFATLTAYDYSMAKQFADAGLNVMLVGDSQGMTVAG-----YDDTLPYPVNDVPYHVRAVRRGAPLA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 133 qiqwaagiepndprfidyflPIVADAEAGFGGV-LNAFELMKSMIEAGAAAVHFEDQLasvkkcghmggkvlvptqEAVQ 211
Cdd:cd06556   75 --------------------LIVADLPFGAYGApTAAFELAKTFMRAGAAGVKIEGGE------------------WHIE 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 212 KLVAARLAAdvlgvpTLVIARTDADAADLITSDCDpydsefitgertsEGFYRTHAGIEQAISRGLAYAPY-ADLVWCET 290
Cdd:cd06556  117 TLQMLTAAA------VPVIAHTGLTPQSVNTSGGD-------------EGQYRGDEAGEQLIADALAYAPAgADLIVMEC 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495778828 291 StpDLALAKRFADAihakyPGKLLAYNCSPSfnwqkklddktiasfqqqlsdmGYKYQFITLAG 354
Cdd:cd06556  178 V--PVELAKQITEA-----LAIPLAGIGAGS----------------------GTDGQFLVLAD 212
PRK06498 PRK06498
isocitrate lyase; Provisional
1-405 2.43e-45

isocitrate lyase; Provisional


Pssm-ID: 180592 [Multi-domain]  Cd Length: 531  Bit Score: 164.83  E-value: 2.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   1 MKTRTQQIEELK--KEWTQPRWEGIrrpySAEDVVKLR--GSVNPECTLAQNGAAKMWKLL--HGGSKKGYINSLGALTG 74
Cdd:PRK06498   1 MSTYQSDIDAVAalKEKQGSTWNAI----NPESAARMRlqNRFKTGLDIAKYTAKIMRADMaaYDADSSKYTQSLGCWHG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  75 GQAlQQAKAGIEA---------IYLSGWQVAAdanLASSM--YPDQSLYPANSVPSVVDRINNTFRRADQIQW------- 136
Cdd:PRK06498  77 FIA-QQKMISIKKhfgttkrryLYLSGWMVAA---LRSEFgpLPDQSMHEKTSVPALIEELYTFLRQADARELndlfrel 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 137 ----AAGIEPNDPRF---IDYF----LPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVP 205
Cdd:PRK06498 153 daarEAGDKAKEAAIqakIDNFethvVPIIADIDAGFGNEEATYLLAKKMIEAGACCIQIENQVSDEKQCGHQDGKVTVP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 206 TQEAVQKLVAARLAADVLGVPTLVI-ARTDA----------------DAADLITS--DCDPYDSE--------------F 252
Cdd:PRK06498 233 HEDFLAKIRAVRYAFLELGVDDGVIvARTDSlgagltqqiavsqepgDLGDQYNSflDCEEIDAAdlgngdvvikrdgkL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 253 ITGERTSEGFYRTHAGIEQ---------AISRGlayapyADLVWCETSTPDLALAKRFADAIHAKYPGKLLAYNCSPSFN 323
Cdd:PRK06498 313 LRPKRLPSGLFQFREGTGEdrcvldcitSLQNG------ADLLWIETEKPHVAQIAGMVNRIREVVPNAKLVYNNSPSFN 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 324 W-----QKKLD-------------------------------DKTIASFQQQLS-DMGYKYQFITLAGIHSMWFNMFDLA 366
Cdd:PRK06498 387 WtlnfrQQVYDawkaegkdvsaydraklmsaeyddtelaaeaDEKIRTFQADAArEAGIFHHLITLPTYHTAALSTDNLA 466
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 495778828 367 HAYAQGEGMKHYVEKVQQPEFaagKDGYTFVSHQQEVGT 405
Cdd:PRK06498 467 KGYFGDQGMLGYVAGVQRKEI---RQGIACVKHQNMAGS 502
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
70-383 9.49e-38

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


Pssm-ID: 442003  Cd Length: 288  Bit Score: 138.73  E-value: 9.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  70 GALTGGQALQQAKAGIEAIYLSGWQVAAdanlASSMYPDQSLYpanSVPSVVDRINNTFRRADqiqwaagiepndprfid 149
Cdd:COG2513   20 GAWDALSARLAEQAGFEALYLSGAGVAA----SLLGLPDLGLL---TLTEVLEHARRIARAVD----------------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 150 yfLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASvKKCGHMGGKVLVPTQEAVQKLVAARLAADvlGVPTLV 229
Cdd:COG2513   76 --LPVIADADTGFGNALNVARTVRELERAGVAGIHIEDQVGP-KRCGHLPGKEVVPAEEMVERIRAAVDARR--DPDFVI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 230 IARTDAdaadlitsdcdpydsefitgertsegfyRTHAGIEQAISRGLAYAPY-ADLVWCEtSTPDLALAKRFADAIhak 308
Cdd:COG2513  151 IARTDA----------------------------RAVEGLDEAIERAKAYAEAgADVIFVE-ALTSLEEIRRVAAAV--- 198
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495778828 309 yPGKLLAyNCSPSfnwqkkldDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQGEGMKHYVEKVQ 383
Cdd:COG2513  199 -DVPLLA-NMTEG--------GKTPLLTAAELAELGVRRVSYPVSLLRAAAKAAERALRELREDGTQAALLDAMQ 263
prpB TIGR02317
methylisocitrate lyase; Members of this family are methylisocitrate lyase, also called (2S,3R) ...
70-346 4.02e-29

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: 115.18  E-value: 4.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   70 GALTGGQALQQAKAGIEAIYLSGWQVAADANLassmyPDQSLypaNSVPSVVDRINNTFRRADqiqwaagiepndprfid 149
Cdd:TIGR02317  19 GAINAMAALLAERAGFEAIYLSGAAVAASLGL-----PDLGI---TTLDEVAEDARRITRVTD----------------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  150 yfLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASvKKCGHMGGKVLVPTQEAVQKLVAarlAADVLGVPTLV 229
Cdd:TIGR02317  74 --LPLLVDADTGFGEAFNVARTVREMEDAGAAAVHIEDQVLP-KRCGHLPGKELVSREEMVDKIAA---AVDAKRDEDFV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  230 -IARTDADAADlitsdcdpydsefitgertsegfyrthaGIEQAISRGLAYAPY-ADLVWCETSTpDLALAKRFADAIha 307
Cdd:TIGR02317 148 iIARTDARAVE----------------------------GLDAAIERAKAYVEAgADMIFPEALT-SLEEFRQFAKAV-- 196
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 495778828  308 kyPGKLLAyNCSPsfnwqkklDDKTIASFQQQLSDMGYK 346
Cdd:TIGR02317 197 --KVPLLA-NMTE--------FGKTPLFTADELREAGYK 224
prpB PRK11320
2-methylisocitrate lyase; Provisional
70-305 1.09e-24

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 103.06  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  70 GALTGGQALQQAKAGIEAIYLSGWQVAAdanlASSMYPDQSLYPANSVPSVVDRINNTFRradqiqwaagiepndprfid 149
Cdd:PRK11320  23 GTINAYHALLAERAGFKAIYLSGGGVAA----ASLGLPDLGITTLDDVLIDVRRITDACD-------------------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828 150 yfLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASvKKCGHMGGKVLVPTQEAVQKLVAarlAADVLGVPTLV 229
Cdd:PRK11320  79 --LPLLVDIDTGFGGAFNIARTVKSMIKAGAAAVHIEDQVGA-KRCGHRPNKEIVSQEEMVDRIKA---AVDARTDPDFV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495778828 230 I-ARTDADAADlitsdcdpydsefitgertsegfyrthaGIEQAISRGLAY-APYADLVWCETSTpDLALAKRFADAI 305
Cdd:PRK11320 153 ImARTDALAVE----------------------------GLDAAIERAQAYvEAGADMIFPEAMT-ELEMYRRFADAV 201
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
81-305 3.93e-16

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: 77.63  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828   81 AKAGIEAIYLSGWQVAAdanlaSSMYPDQSLYPANSVPSVVDRInntfrrADQIQwaagiepndprfidyfLPIVADAEA 160
Cdd:pfam13714  26 EAAGFPAIATSSAGVAA-----SLGYPDGELLPRDELLAAARRI------AAAVD----------------LPVSADLET 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778828  161 GFGGVLNAF-ELMKSMIEAGAAAVHFEDQLASVkkcghmGGKVLVPTQEAVQKLVAARLAADVLGVPTLVIARTDAdaad 239
Cdd:pfam13714  79 GYGDSPEEVaETVRRLIAAGVVGVNIEDSKTGR------PGGQLLDVEEAAARIRAARAAARAAGVPFVINARTDA---- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495778828  240 litsdcdpydseFITGErtsegfyrtHAGIEQAISRGLAYAPY-AD--LVWCETSTPDLAlakRFADAI 305
Cdd:pfam13714 149 ------------FLLGR---------GDALEEAIRRARAYAEAgADgiFVPGLLDPADIA---ALVAAV 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH