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Conserved domains on  [gi|1892709055|ref|WP_184826609|]
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3-carboxy-cis,cis-muconate cycloisomerase [Streptomyces griseomycini]

Protein Classification

adenylosuccinate lyase family protein( domain architecture ID 10107773)

adenylosuccinate lyase family protein similar to Acinetobacter sp. 3-carboxy-cis,cis-muconate cycloisomerase, which catalyzes the cyclization of 3-carboxy-cis,cis-muconate to 4-carboxy-muconolactone in the beta-ketoadipate pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 30-443 4.56e-155

prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.


:

Pssm-ID: 176469 [Multi-domain]  Cd Length: 437  Bit Score: 446.31  E-value: 4.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  30 YLRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATS 109
Cdd:cd01597    20 RVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATARTGHPAIPLVKQLTAACGDAAGEYVHWGATT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 110 QDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVR-D 188
Cdd:cd01597   100 QDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRpR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 189 GLPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:cd01597   180 VLVVQFGGAAGTLASLGDQGLA----VQEALAAELGLGVPAIPWHTARDRIAELASFLALLTGTLGKIARDVYLLMQTEI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:cd01597   256 GEVAEPFAkgrGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQAE 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDV----ALD 421
Cdd:cd01597   336 FLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLLEDPEVAAYlsdeELD 415

                         410       420
                  ....*....|....*....|..
gi 1892709055 422 ELTDPARYTGSAGVLTDRALER 443
Cdd:cd01597   416 ALLDPANYLGSAPALVDRVLAR 437
 
Name Accession Description Interval E-value
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 30-443 4.56e-155

prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.


Pssm-ID: 176469 [Multi-domain]  Cd Length: 437  Bit Score: 446.31  E-value: 4.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  30 YLRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATS 109
Cdd:cd01597    20 RVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATARTGHPAIPLVKQLTAACGDAAGEYVHWGATT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 110 QDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVR-D 188
Cdd:cd01597   100 QDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRpR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 189 GLPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:cd01597   180 VLVVQFGGAAGTLASLGDQGLA----VQEALAAELGLGVPAIPWHTARDRIAELASFLALLTGTLGKIARDVYLLMQTEI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:cd01597   256 GEVAEPFAkgrGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQAE 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDV----ALD 421
Cdd:cd01597   336 FLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLLEDPEVAAYlsdeELD 415

                         410       420
                  ....*....|....*....|..
gi 1892709055 422 ELTDPARYTGSAGVLTDRALER 443
Cdd:cd01597   416 ALLDPANYLGSAPALVDRVLAR 437
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 31-440 1.56e-129

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 380.97  E-value: 1.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATSQ 110
Cdd:COG0015    21 IRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKETRHDVKAFVYALKEKVGAEAGEYIHFGATSQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 111 DIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDG- 189
Cdd:COG0015   101 DINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERv 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 LPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLR-EPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:COG0015   181 LVGKIGGAVGTYAAHGEAWPE----VEERVAEKLGLKpNPVTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:COG0015   257 GEVEEPFAkgqVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNILPDAFLLLDGALERLL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPL-LGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDVA----L 420
Cdd:COG0015   337 KLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRgLGREEAYELVKELARGAWEEGNDLRELLAADPEIPAELskeeL 416

                         410       420
                  ....*....|....*....|
gi 1892709055 421 DELTDPARYTGSAGVLTDRA 440
Cdd:COG0015   417 EALFDPANYLGAADEIVDRV 436
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 30-351 1.87e-120

3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 274128 [Multi-domain]  Cd Length: 338  Bit Score: 354.44  E-value: 1.87e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  30 YLRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATS 109
Cdd:TIGR02426  20 FLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAAAAPDLEALAHAAATAGNPVIPLVKALRKAVAGEAARYVHRGATS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 110 QDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDG 189
Cdd:TIGR02426 100 QDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAAVLRARDRLAALRTR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 -LPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:TIGR02426 180 aLPLQFGGAAGTLAALGTRGGA----VAAALAARLGLPLPALPWHTQRDRIAEFGSALALVAGALGKIAGDIALLSQTEV 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSGGGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAAELT 348
Cdd:TIGR02426 256 GEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPELVRLTGGALRQAQVLA 335


                  ...
gi 1892709055 349 EGL 351
Cdd:TIGR02426 336 EGL 338
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 31-441 3.22e-113

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 340.07  E-value: 3.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGA---EYGPYVHRGA 107
Cdd:PRK09053   27 VQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALAGNLAIPLVKQLTAQVAArdaEAARYVHWGA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 108 TSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVR 187
Cdd:PRK09053  107 TSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 188 DGLPA-QLGGAAGTLAAFtaygAEDATGLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRT 266
Cdd:PRK09053  187 PRALVlQFGGAAGTLASL----GEQALPVAQALAAELQLALPALPWHTQRDRIAEFASALGLLAGTLGKIARDVSLLMQT 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 267 EIAEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARD 343
Cdd:PRK09053  263 EVGEVFEPAAagkGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWHAEWDTLPELACLAAGALAQ 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 344 AAELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPA----LRDVA 419
Cdd:PRK09053  343 MAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADRIGRLDAHHLVEQASKRAVAEGRHLRDVLAEDPQvsahLSPAA 422

                         410       420
                  ....*....|....*....|..
gi 1892709055 420 LDELTDPARYTGSAGVLTDRAL 441
Cdd:PRK09053  423 LDRLLDPAHYLGQAHAWVDRVL 444
Lyase_1 pfam00206
Lyase;
102-302 2.43e-30

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 119.40  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 102 YVHRGATSQDIMDTATMLVAARTLDIVL-ADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDAR 180
Cdd:pfam00206 104 HVHTGQSSNDQVPTALRLALKDALSEVLlPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 181 DRVTAVRDGLPA-QLGGAAgtlAAFTAYGA--EDATGLPAAYARELGLREPLLPWHT---LRTPIADLAGCLAFTVGALG 254
Cdd:pfam00206 184 ERLQQLLPRLLVlPLGGGT---AVGTGLNAdpEFAELVAKELGFFTGLPVKAPNSFEatsDRDAVVELSGALALLATSLS 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1892709055 255 KLAADVLTLSRTEIAEV----AEGSgGGSSAMPHKANPVRSTLIAAAARRAP 302
Cdd:pfam00206 261 KFAEDLRLLSSGPAGLVelslAEGE-PGSSIMPGKVNPDQLELLTGKAGRVM 311
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 366-441 1.22e-12

Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.


Pssm-ID: 198066 [Multi-domain]  Cd Length: 81  Bit Score: 63.24  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  366 HGLIVSERLSAELA-PLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDV----ALDELTDPARYTGSAGVLTDRA 440
Cdd:smart00998   1 GGLIFSERVLLALVeKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYlseeELEELFDPEYYLGHADAIVDRV 80


                   .
gi 1892709055  441 L 441
Cdd:smart00998  81 L 81
 
Name Accession Description Interval E-value
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 30-443 4.56e-155

prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.


Pssm-ID: 176469 [Multi-domain]  Cd Length: 437  Bit Score: 446.31  E-value: 4.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  30 YLRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATS 109
Cdd:cd01597    20 RVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATARTGHPAIPLVKQLTAACGDAAGEYVHWGATT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 110 QDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVR-D 188
Cdd:cd01597   100 QDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRpR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 189 GLPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:cd01597   180 VLVVQFGGAAGTLASLGDQGLA----VQEALAAELGLGVPAIPWHTARDRIAELASFLALLTGTLGKIARDVYLLMQTEI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:cd01597   256 GEVAEPFAkgrGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQAE 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDV----ALD 421
Cdd:cd01597   336 FLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLLEDPEVAAYlsdeELD 415

                         410       420
                  ....*....|....*....|..
gi 1892709055 422 ELTDPARYTGSAGVLTDRALER 443
Cdd:cd01597   416 ALLDPANYLGSAPALVDRVLAR 437
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 31-440 1.56e-129

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 380.97  E-value: 1.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATSQ 110
Cdd:COG0015    21 IRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKETRHDVKAFVYALKEKVGAEAGEYIHFGATSQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 111 DIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDG- 189
Cdd:COG0015   101 DINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERv 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 LPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLR-EPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:COG0015   181 LVGKIGGAVGTYAAHGEAWPE----VEERVAEKLGLKpNPVTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:COG0015   257 GEVEEPFAkgqVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNILPDAFLLLDGALERLL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPL-LGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDVA----L 420
Cdd:COG0015   337 KLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRgLGREEAYELVKELARGAWEEGNDLRELLAADPEIPAELskeeL 416

                         410       420
                  ....*....|....*....|
gi 1892709055 421 DELTDPARYTGSAGVLTDRA 440
Cdd:COG0015   417 EALFDPANYLGAADEIVDRV 436
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 30-351 1.87e-120

3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 274128 [Multi-domain]  Cd Length: 338  Bit Score: 354.44  E-value: 1.87e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  30 YLRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATS 109
Cdd:TIGR02426  20 FLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAAAAPDLEALAHAAATAGNPVIPLVKALRKAVAGEAARYVHRGATS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 110 QDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDG 189
Cdd:TIGR02426 100 QDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAAVLRARDRLAALRTR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 -LPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:TIGR02426 180 aLPLQFGGAAGTLAALGTRGGA----VAAALAARLGLPLPALPWHTQRDRIAEFGSALALVAGALGKIAGDIALLSQTEV 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSGGGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAAELT 348
Cdd:TIGR02426 256 GEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPELVRLTGGALRQAQVLA 335


                  ...
gi 1892709055 349 EGL 351
Cdd:TIGR02426 336 EGL 338
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 31-441 3.22e-113

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 340.07  E-value: 3.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGA---EYGPYVHRGA 107
Cdd:PRK09053   27 VQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALAGNLAIPLVKQLTAQVAArdaEAARYVHWGA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 108 TSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVR 187
Cdd:PRK09053  107 TSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 188 DGLPA-QLGGAAGTLAAFtaygAEDATGLPAAYARELGLREPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRT 266
Cdd:PRK09053  187 PRALVlQFGGAAGTLASL----GEQALPVAQALAAELQLALPALPWHTQRDRIAEFASALGLLAGTLGKIARDVSLLMQT 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 267 EIAEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARD 343
Cdd:PRK09053  263 EVGEVFEPAAagkGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWHAEWDTLPELACLAAGALAQ 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 344 AAELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPA----LRDVA 419
Cdd:PRK09053  343 MAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADRIGRLDAHHLVEQASKRAVAEGRHLRDVLAEDPQvsahLSPAA 422

                         410       420
                  ....*....|....*....|..
gi 1892709055 420 LDELTDPARYTGSAGVLTDRAL 441
Cdd:PRK09053  423 LDRLLDPAHYLGQAHAWVDRVL 444
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 31-393 1.04e-110

Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176467 [Multi-domain]  Cd Length: 381  Bit Score: 331.01  E-value: 1.04e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATSQ 110
Cdd:cd01595    11 LRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVFEIDAERIAEIEKETGHDVIAFVYALAEKCGEDAGEYVHFGATSQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 111 DIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRD-G 189
Cdd:cd01595    91 DINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARErV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 LPAQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTL-RTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:cd01595   171 LVGGISGAVGTHASLGPKGPE----VEERVAEKLGLKVPPITTQIEpRDRIAELLSALALIAGTLEKIATDIRLLQRTEI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:cd01595   247 GEVEEPFEkgqVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDAALSRLQ 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAP-LLGRTRAKELLTE 393
Cdd:cd01595   327 GLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKkGLGRQEAYELVKE 375
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 69-354 3.53e-66

Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.


Pssm-ID: 176461 [Multi-domain]  Cd Length: 325  Bit Score: 214.67  E-value: 3.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  69 DLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRD 148
Cdd:cd01334    40 IAADQVEQEGSGTHDVMAVEEVLAERAGELNGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 149 TPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDGL-PAQLG-GAAGTLAAFTAygaedatGLPAAYARELGLR 226
Cdd:cd01334   120 TVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLnVLPLGgGAVGTGANAPP-------IDRERVAELLGFF 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 227 EP---LLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEIAEVAEGSG--GGSSAMPHKANPVRSTLIAAAARRA 301
Cdd:cd01334   193 GPapnSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEVELPDAkqPGSSIMPQKVNPVILELVRGLAGRV 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1892709055 302 PQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAAELTEGLRVH 354
Cdd:cd01334   273 IGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGLEVN 325
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 31-352 9.51e-55

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 185.64  E-value: 9.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGPYVHRGATSQ 110
Cdd:PRK05975   30 IAAMLAFEAALAEAEAEHGIIPAEAAERIAAACETFEPDLAALRHATARDGVVVPALVRQLRAAVGEEAAAHVHFGATSQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 111 DIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVR-DG 189
Cdd:PRK05975  110 DVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRaDV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 LPAQLGGAAGTLAAFtaygAEDATGLPAAYARELGLrEPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEiA 269
Cdd:PRK05975  190 FPLQFGGAAGTLEKL----GGKAAAVRARLAKRLGL-EDAPQWHSQRDFIADFAHLLSLVTGSLGKFGQDIALMAQAG-D 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 270 EVAEGSGGGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAAELTE 349
Cdd:PRK05975  264 EISLSGGGGSSAMPHKQNPVAAETLVTLARFNATQVSGLHQALVHEQERSGAAWTLEWMILPQMVAATGAALRLALELAG 343


                  ...
gi 1892709055 350 GLR 352
Cdd:PRK05975  344 NIR 346
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 31-379 2.60e-52

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 180.44  E-value: 2.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAapaGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEyGPYVHRGATSQ 110
Cdd:cd01360    17 FRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKA---KFDVERVKEIEAETKHDVIAFVTAIAEYCGEA-GRYIHFGLTSS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 111 DIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRD-G 189
Cdd:cd01360    93 DVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARErI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 190 LPAQLGGAAGTLAAFTAYGAEDAtglpaayARELGLR-EPLLPWHTLRTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:cd01360   173 LVGKISGAVGTYANLGPEVEERV-------AEKLGLKpEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEV 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSG---GGSSAMPHKANPVRSTLIAAAAR--RAPQLAATLYGSLaaederpagaWH--------AEWEPLRDLLR 335
Cdd:cd01360   246 LEVEEPFSkgqKGSSAMPHKRNPILSENICGLARviRSNVIPALENVAL----------WHerdishssVERVILPDATI 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1892709055 336 LTGGAARDAAELTEGLRVHPDTMREHLGLTHGLIVSERLSAELA 379
Cdd:cd01360   316 LLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALV 359
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 31-439 4.75e-52

adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273345 [Multi-domain]  Cd Length: 435  Bit Score: 181.01  E-value: 4.75e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  31 LRALLDAEAALTRAQAALGLAPAQAAAAVDEAAAPAGFDLRSLAERTREGGNPVIPLVEDLTEAVGAEyGPYVHRGATSQ 110
Cdd:TIGR00928  20 FKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYALKEKCGAE-GEFIHFGATSN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 111 DIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDGL 190
Cdd:TIGR00928  99 DIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERI 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 191 P-AQLGGAAGTLAAFTAYGAEdatgLPAAYARELGLREPLLPWHTL-RTPIADLAGCLAFTVGALGKLAADVLTLSRTEI 268
Cdd:TIGR00928 179 KvGGISGAVGTHAAAYPLVEE----VEERVTEFLGLKPVPISTQIEpRDRHAELLDALALLATTLEKFAVDIRLLQRTEH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 269 AEVAEGSGG---GSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDERPAGAWHAEWEPLRDLLRLTGGAARDAA 345
Cdd:TIGR00928 255 FEVEEPFGKgqvGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILPDAFILADIMLKTTL 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 346 ELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPL-LGRTRAKELLTELARRTY-AEGQPLAGLLAGEPA----LRDVA 419
Cdd:TIGR00928 335 KVVKKLVVNPENILRNLDLTLGLIASERVLIALVERgMGREEAYEIVRELAMGAAeVDEPDLLEFLLEDERitkyLKEEE 414

                         410       420
                  ....*....|....*....|
gi 1892709055 420 LDELTDPARYTGSAGVLTDR 439
Cdd:TIGR00928 415 LAELLDPETYIGNAGEIVER 434
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 87-342 6.96e-34

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


Pssm-ID: 176466 [Multi-domain]  Cd Length: 231  Bit Score: 126.57  E-value: 6.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  87 LVEDLTEAVGAEYG-----PYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAV 161
Cdd:cd01594    16 VEEVLAGRAGELAGglhgsALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 162 PTTFGLKAAGWRSLVLDARDRVTAVrdglpaqlggaagtlaaftaygaedatglpaayarelglrepllpwhtlrtPIAD 241
Cdd:cd01594    96 PVTLGYELRAWAQVLGRDLERLEEA---------------------------------------------------AVAE 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 242 LAGCLAFTVGALGKLAADVLTLSRTEIAEVAEGSG---GGSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAEDER 318
Cdd:cd01594   125 ALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLpgqPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPER 204

                         250       260
                  ....*....|....*....|....
gi 1892709055 319 PAGAWHAEWEPLRDLLRLTGGAAR 342
Cdd:cd01594   205 DNEDSPSMREILADSLLLLIDALR 228
Lyase_1 pfam00206
Lyase;
102-302 2.43e-30

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 119.40  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 102 YVHRGATSQDIMDTATMLVAARTLDIVL-ADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDAR 180
Cdd:pfam00206 104 HVHTGQSSNDQVPTALRLALKDALSEVLlPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 181 DRVTAVRDGLPA-QLGGAAgtlAAFTAYGA--EDATGLPAAYARELGLREPLLPWHT---LRTPIADLAGCLAFTVGALG 254
Cdd:pfam00206 184 ERLQQLLPRLLVlPLGGGT---AVGTGLNAdpEFAELVAKELGFFTGLPVKAPNSFEatsDRDAVVELSGALALLATSLS 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1892709055 255 KLAADVLTLSRTEIAEV----AEGSgGGSSAMPHKANPVRSTLIAAAARRAP 302
Cdd:pfam00206 261 KFAEDLRLLSSGPAGLVelslAEGE-PGSSIMPGKVNPDQLELLTGKAGRVM 311
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 239-431 6.36e-22

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 93.55  E-value: 6.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 239 IADLAgcLAFTVGALGKLAADVLTLSRTEIAEVAEGSGG---GSSAMPHKANPVRSTLIAAAARRAPQLAATLYGSLAAE 315
Cdd:PRK08937   18 IAEIV--LALIATSLEKFANEIRLLQRSEIREVEEPFAKgqkGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLW 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 316 DERPAGAWHAEWEPLRDLLRLTGGAARDAAELTEGLRVHPDTMREHLGLTHGLIVSERLSAELAPL-LGRTRAKELLTEL 394
Cdd:PRK08937   96 HERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKgMGREEAHELIREK 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1892709055 395 ARRTYAEGQPLAGLLAGEPALRDV----ALDELTDPARYTG 431
Cdd:PRK08937  176 AMEAWKNQKDLRELLEADERFTKQltkeELDELFDPEAFVG 216
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 70-363 1.59e-21

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 96.08  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  70 LRSLAERTREGGNPVIPLVED--------LTEAVGaEYGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALAR 141
Cdd:cd01359    41 LAKIRAEIEAGAFELDPEDEDihmaierrLIERIG-DVGGKLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 142 LAAEHRDTPMPGRTLTQHAVPTTFG--LKAAGW-----RSLVLDARDRVtavrDGLPaqLGGAAGTlaaftaygaedATG 214
Cdd:cd01359   120 RAEEHADTIMPGYTHLQRAQPITFGhyLLAYAEmlerdLERLADAYKRV----NVSP--LGAGALA-----------GTT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 215 LP---AAYARELGLREPLlpWHTL-----RTPIADLAGCLAFTVGALGKLAADVLTLSRTE--IAEVAEGSGGGSSAMPH 284
Cdd:cd01359   183 FPidrERTAELLGFDGPT--ENSLdavsdRDFVLEFLSAAALLMVHLSRLAEDLILWSTQEfgFVELPDAYSTGSSIMPQ 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 285 KANPVRSTLIAAAARRAPQLAATL----------YGSLAAEDerpagawhaeWEPLRDLLRLTGGAARDAAELTEGLRVH 354
Cdd:cd01359   261 KKNPDVLELIRGKAGRVIGALAGLlttlkglplaYNKDLQED----------KEPLFDAVDTLIASLRLLTGVISTLTVN 330


                  ....*....
gi 1892709055 355 PDTMREHLG 363
Cdd:cd01359   331 PERMREAAE 339
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 68-310 4.13e-17

Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176471 [Multi-domain]  Cd Length: 436  Bit Score: 83.14  E-value: 4.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  68 FDLRSLAERTREGGNPVIPLVEDLTEAVGAEYGpYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHR 147
Cdd:cd03302    56 IDFEIAAAEEKKLRHDVMAHVHAFGLLCPAAAG-IIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 148 DTPMPGRTLTQHAVPTTFGLKAAGW-RSLVLDARdRVTAVRDGLPAQ-LGGAAGTLAAFTAYGAEDatglpAAYARELGL 225
Cdd:cd03302   135 DLPTLGFTHYQPAQLTTVGKRACLWiQDLLMDLR-NLERLRDDLRFRgVKGTTGTQASFLDLFEGD-----HDKVEALDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 226 RepllpwhtlrtpIADLAGC------------------LAFTVGALG----KLAADV-LTLSRTEIAEVAEGSGGGSSAM 282
Cdd:cd03302   209 L------------VTKKAGFkkvypvtgqtysrkvdidVLNALSSLGatahKIATDIrLLANLKEVEEPFEKGQIGSSAM 276

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1892709055 283 PHKANPVRSTLIAAAARR---APQLAATLYG 310
Cdd:cd03302   277 PYKRNPMRSERCCSLARHlmnLASNAAQTAS 307
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 70-363 2.86e-16

Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439935 [Multi-domain]  Cd Length: 462  Bit Score: 80.53  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  70 LRSLAERTREGGNPVIPLVED--------LTEAVGAEyGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALAR 141
Cdd:COG0165    64 LDEIEAEIEAGAFEFDPELEDihmnierrLIERIGDV-GGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLD 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 142 LAAEHRDTPMPGRTLTQHAVPTTFG--LKAAGW-----RSLVLDARDRVtavrDGLPaqLGGAAgtLAaftaygaedATG 214
Cdd:COG0165   143 LAEEHADTIMPGYTHLQRAQPVTFGhhLLAYAEmllrdRERLADAYKRL----NVSP--LGAAA--LA---------GTT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 215 LP---AAYARELGLREPLlpWHTL-----RTPIADLAGCLAFTVGALGKLAADVLTLSRTE--IAEVAEGSGGGSSAMPH 284
Cdd:COG0165   206 FPidrERTAELLGFDGPT--ENSLdavsdRDFALEFLSAASLIMVHLSRLAEELILWSSSEfgFVELPDAFSTGSSIMPQ 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 285 KANPVRSTLIaaaarRApqLAATLYGSLAA-----------------EDerpagawhaeWEPLRDLLRLTGGAARDAAEL 347
Cdd:COG0165   284 KKNPDVAELI-----RG--KTGRVIGNLTGllttmkglplaynkdlqED----------KEPLFDAVDTLKLCLRLFAGM 346

                         330
                  ....*....|....*.
gi 1892709055 348 TEGLRVHPDTMREHLG 363
Cdd:COG0165   347 IATLKVNRERMREAAG 362
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 101-290 9.16e-15

PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176470 [Multi-domain]  Cd Length: 425  Bit Score: 75.73  E-value: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 101 PYVHRGATSQDIMDTA--TMLVAARTlDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLD 178
Cdd:cd01598    93 EFIHFACTSEDINNLAyaLMIKEARN-EVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLER 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 179 ARDRVTAVRDglPAQLGGAAGTLAA-FTAYGAEDATGLPAAYARELGLRepllpWHTLRTPI------ADLAGCLAFTVG 251
Cdd:cd01598   172 QYKQLKQIEI--LGKFNGAVGNFNAhLVAYPDVDWRKFSEFFVTSLGLT-----WNPYTTQIephdyiAELFDALARINT 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1892709055 252 ALGKLAADV-LTLSRTEIAEVAEGSGGGSSAMPHKANPVR 290
Cdd:cd01598   245 ILIDLCRDIwGYISLGYFKQKVKKGEVGSSTMPHKVNPID 284
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 367-440 9.47e-14

Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.


Pssm-ID: 463073 [Multi-domain]  Cd Length: 78  Bit Score: 66.28  E-value: 9.47e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1892709055 367 GLIVSERLSAELAPLLGRTRAKELLTELARRTYAEGQ-PLAGLLAGEPA---LRDVALDELTDPARYTGSAGVLTDRA 440
Cdd:pfam10397   1 GLIFSERVLLALVKGLGREEAHELVQEAAMKAWEEGKnDLRELLAADPEvtyLSEEELDALFDPAYYLGRADEIVDRV 78
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 366-441 1.22e-12

Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.


Pssm-ID: 198066 [Multi-domain]  Cd Length: 81  Bit Score: 63.24  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  366 HGLIVSERLSAELA-PLLGRTRAKELLTELARRTYAEGQPLAGLLAGEPALRDV----ALDELTDPARYTGSAGVLTDRA 440
Cdd:smart00998   1 GGLIFSERVLLALVeKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYlseeELEELFDPEYYLGHADAIVDRV 80


                   .
gi 1892709055  441 L 441
Cdd:smart00998  81 L 81
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 117-425 7.33e-12

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 67.06  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 117 TMLVAA--RTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDGL-PAQ 193
Cdd:cd01596   142 AAHIAAalALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLrELN 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 194 LGG-AAGT-LAAFTAYGAEDAtglpAAYARELGlreplLPWHTLRTPIADLAGCLAFTV--GALGKLAADVLTLS----- 264
Cdd:cd01596   222 LGGtAVGTgLNAPPGYAEKVA----AELAELTG-----LPFVTAPNLFEATAAHDALVEvsGALKTLAVSLSKIAndlrl 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 265 -----RTEIAEV------AegsggGSSAMPHKANPVRSTLIAaaarrapQLAATLYG-----SLAAEderpAGawHAE-- 326
Cdd:cd01596   293 lssgpRAGLGEInlpanqP-----GSSIMPGKVNPVIPEAVN-------MVAAQVIGndtaiTMAGS----AG--QLEln 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 327 -WEPL--RDLLR----LTGGAARDAAELTEGLRVHPDTMREHLGLTHGLIVSerlsaeLAPLLGRTRAkellTELARRTY 399
Cdd:cd01596   355 vFKPViaYNLLQsirlLANACRSFRDKCVEGIEANEERCKEYVENSLMLVTA------LNPHIGYEKA----AEIAKEAL 424

                         330       340
                  ....*....|....*....|....*.
gi 1892709055 400 AEGQPLAGLLAGEPALRDVALDELTD 425
Cdd:cd01596   425 KEGRTLREAALELGLLTEEELDEILD 450
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 103-296 2.22e-11

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 65.60  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 103 VHRGATSQDIMDTATMLVAARTL-DIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARD 181
Cdd:cd01362   130 VNMSQSSNDTFPTAMHIAAALALqERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 182 RVTAVRDGLP--AQLGGAAGT-LAAFTAYGAEDAtglpAAYARELGlreplLPWHTLRTPIADLAGC--LAFTVGALGKL 256
Cdd:cd01362   210 RIEAALPRLYelALGGTAVGTgLNAHPGFAEKVA----AELAELTG-----LPFVTAPNKFEALAAHdaLVEASGALKTL 280

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1892709055 257 AADVLTLS----------RTEIAEVA-EGSGGGSSAMPHKANPVRS---TLIAA 296
Cdd:cd01362   281 AVSLMKIAndirwlgsgpRCGLGELSlPENEPGSSIMPGKVNPTQCealTMVAA 334
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 97-290 3.30e-11

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 64.77  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  97 AEYGPYVHRGATSQDIMDT--ATMLVAARTlDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGlK-----A 169
Cdd:PRK09285  111 EAVSEFIHFACTSEDINNLshALMLKEARE-EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLG-KemanvA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 170 AGWRSlvldARDRVTAVRdgLPAQLGGAAGTLAA-FTAYGAEDATGLPAAYARELGLRepllpWHTLRTPI------ADL 242
Cdd:PRK09285  189 YRLER----QLKQLEAVE--ILGKINGAVGNYNAhLAAYPEVDWHAFSREFVESLGLT-----WNPYTTQIephdyiAEL 257

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1892709055 243 AGCLAFTVGALGKLAADVLT-LS------RTEIAEVaegsggGSSAMPHKANPVR 290
Cdd:PRK09285  258 FDAVARFNTILIDLDRDVWGyISlgyfkqKTKAGEI------GSSTMPHKVNPID 306
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 70-360 4.56e-11

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 64.40  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  70 LRSLAERTREGGNPVIPLVED--------LTEAVGaEYGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALAR 141
Cdd:PRK00855   65 LDEILEEIEAGKFEFSPELEDihmaiearLTERIG-DVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLD 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 142 LAAEHRDTPMPGRTLTQHAVPTTFGLKAAGW-------RSLVLDARDRVtavrDGLPaqLGGAAGtlaaftaYGaedaTG 214
Cdd:PRK00855  144 LAEEHADTIMPGYTHLQRAQPVTFGHHLLAYaemlardLERLRDARKRV----NRSP--LGSAAL-------AG----TT 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 215 LP---AAYARELGLREPLLpwHTL-----RTPIADLAGCLAFTVGALGKLAADVLTLSRTE--IAEVAEGSGGGSSAMPH 284
Cdd:PRK00855  207 FPidrERTAELLGFDGVTE--NSLdavsdRDFALEFLSAASLLMVHLSRLAEELILWSSQEfgFVELPDAFSTGSSIMPQ 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 285 KANPVRSTLIAAAARRapqlaatLYGSLAA-----------------EDERPagAWHAEwEPLRDLLRLtggaardAAEL 347
Cdd:PRK00855  285 KKNPDVAELIRGKTGR-------VYGNLTGlltvmkglplaynrdlqEDKEP--LFDAV-DTLKLSLEA-------MAGM 347

                         330
                  ....*....|...
gi 1892709055 348 TEGLRVHPDTMRE 360
Cdd:PRK00855  348 LETLTVNKERMRE 360
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 91-434 8.98e-11

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 64.10  E-value: 8.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  91 LTEAVGAEYGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAA 170
Cdd:PRK02186  498 LIERLGEDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLL 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 171 GWRSLVLDARDRVTAVRDGLP-AQLGGAAGtlaaftayGAEDATGLPAAYARELGLREPL---LPWHTLRTPIADLAGCL 246
Cdd:PRK02186  578 AVDGALARETHALFALFEHIDvCPLGAGAG--------GGTTFPIDPEFVARLLGFEQPApnsLDAVASRDGVLHFLSAM 649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 247 AFTVGALGKLAADVLTLSRTEIAEVA--EGSGGGSSAMPHKANPVrstLIAAAARRAPQLAATLYGSLAAEDERPAGAWH 324
Cdd:PRK02186  650 AAISTVLSRLAQDLQLWTTREFALVSlpDALTGGSSMLPQKKNPF---LLEFVKGRAGVVAGALASASAALGKTPFSNSF 726

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 325 AEWEPLRDLLRLTGGAARDAAELT----EGLRVHPDTMREHL--GLTHGLIVSERLSAE--LAPLLGRTRAKELLTELAR 396
Cdd:PRK02186  727 EAGSPMNGPIAQACAAIEDAAAVLvlliDGLEADQARMRAHLedGGVSATAVAESLVVRrsISFRSAHTQVGQAIRQSLD 806

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1892709055 397 RTYAEGQPLAGLlagEPALRDVALDELTDPARYTGSAG 434
Cdd:PRK02186  807 QGRSSADALAAL---DPQFVSRAPLEWARSHRFGGGPG 841
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 93-430 2.74e-10

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 61.92  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  93 EAVGAEYGPY--------VHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTT 164
Cdd:PRK13353  117 ELLGGEKGDYhyvspndhVNMAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPIT 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 165 FGLKAAGWRSLVLDARDRVTAVRDGL-PAQLGGAA-GT-LAAFTAYGA------EDATGLPAAyarelglREPLLPWHTL 235
Cdd:PRK13353  197 LGQEFSAYARALKRDRKRIQQAREHLyEVNLGGTAvGTgLNADPEYIErvvkhlAAITGLPLV-------GAEDLVDATQ 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 236 RT-PIADLAGCLAFTVGALGKLAADVLTLS---RTEIAEVA-EGSGGGSSAMPHKANPVRSTLIAAAARRAPQLAATLyg 310
Cdd:PRK13353  270 NTdAFVEVSGALKVCAVNLSKIANDLRLLSsgpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTI-- 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 311 SLAAEderpAGAWHAE-WEPL--RDLLR----LTGGAARDAAELTEGLRVHPDTMREHLGLTHGLIVSerlsaeLAPLLG 383
Cdd:PRK13353  348 TLAAE----AGQLELNvMEPViaFNLLEsisiLTNACRAFTDNCVKGIEANEERCKEYVEKSVGIATA------LNPHIG 417

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1892709055 384 RTRAkellTELARRTYAEGQPLAGLLAGEPALRDVALDELTDPARYT 430
Cdd:PRK13353  418 YEAA----ARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
PLN02848 PLN02848
adenylosuccinate lyase
 102-289 3.50e-10

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 61.68  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 102 YVHRGATSQDI--MDTATMLVAARTlDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDA 179
Cdd:PLN02848  119 FFHFACTSEDInnLSHALMLKEGVN-SVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQ 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 180 RDRVTAVRdgLPAQLGGAAGTLAA-FTAYGAEDATGLPAAYARELGLRepLLPWHTLRTP---IADLAGCLAFTVGALGK 255
Cdd:PLN02848  198 RKQLSEVK--IKGKFAGAVGNYNAhMSAYPEVDWPAVAEEFVTSLGLT--FNPYVTQIEPhdyMAELFNAVSRFNNILID 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1892709055 256 LAADVLTL-------SRTEIAEVaegsggGSSAMPHKANPV 289
Cdd:PLN02848  274 FDRDIWSYislgyfkQITKAGEV------GSSTMPHKVNPI 308
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 93-423 9.85e-10

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 60.23  E-value: 9.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  93 EAVGAEYGPY--------VHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTT 164
Cdd:cd01357   112 ELLGHEKGEYqyvhpndhVNMSQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMT 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 165 FGLKAAGWRSLVLDARDRVTAVRDGLPA-QLGGaagtlaafTAYGaedaTGL--PAAY--------ARELGLrePLLPWH 233
Cdd:cd01357   192 LGQEFGAYATALKRDRARIYKARERLREvNLGG--------TAIG----TGInaPPGYielvveklSEITGL--PLKRAE 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 234 TL------RTPIADLAGCLAFTVGALGKLAADVLTLS---RTEIAEV------AegsggGSSAMPHKANPVRSTLIAAAA 298
Cdd:cd01357   258 NLidatqnTDAFVEVSGALKRLAVKLSKIANDLRLLSsgpRAGLGEInlpavqP-----GSSIMPGKVNPVIPEVVNQVA 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 299 RR--APQLAATlygsLAAEderpAGawHAE---WEPL--RDLLR----LTGGAARDAAELTEGLRVHPDTMREHLGLTHG 367
Cdd:cd01357   333 FQviGNDLTIT----MAAE----AG--QLElnvFEPViaYNLLEsidiLTNAVRTLRERCIDGITANEERCREYVENSIG 402

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1892709055 368 LIvserlsAELAPLLGRTRAkellTELARRTYAEGQPLAGLLAGEPALRDVALDEL 423
Cdd:cd01357   403 IV------TALNPYIGYEAA----AEIAKEALETGRSVRELVLEEGLLTEEELDEI 448
fumC PRK00485
fumarate hydratase; Reviewed
 103-432 1.69e-09

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 59.72  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 103 VHRGATSQDIMDTAtMLVAArTLDIV---LADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDA 179
Cdd:PRK00485  134 VNMSQSSNDTFPTA-MHIAA-VLAIVerlLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHG 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 180 RDRVTAVRDGLP--AQLGGAAGT-LAAFTAYGAE------DATGLPAAYAR----ELGLREPLLPWH-TLRTpiadLAgc 245
Cdd:PRK00485  212 IERIEAALPHLYelALGGTAVGTgLNAHPGFAERvaeelaELTGLPFVTAPnkfeALAAHDALVEASgALKT----LA-- 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 246 laftvGALGKLAADVLTLS---RTEIAEVA-EGSGGGSSAMPHKANPVrstlIAAAARrapQLAATLYGSLAAEDerpAG 321
Cdd:PRK00485  286 -----VSLMKIANDIRWLAsgpRCGLGEISlPENEPGSSIMPGKVNPT----QCEALT---MVCAQVMGNDAAVT---FA 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 322 AWHAEWE-----PL--RDLL---RLTGGAARDAAELT-EGLRVHPDTMREHLGltHGLIvserLSAELAPLLGRTRAkel 390
Cdd:PRK00485  351 GSQGNFElnvfkPViaYNFLqsiRLLADAMRSFADHCvVGIEPNRERIKELLE--RSLM----LVTALNPHIGYDKA--- 421

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1892709055 391 lTELARRTYAEGQPL------AGLLAGEpalrdvALDELTDPARYTGS 432
Cdd:PRK00485  422 -AKIAKKAHKEGLTLkeaaleLGYLTEE------EFDRWVDPEKMTGP 462
PRK12425 PRK12425
class II fumarate hydratase;
73-405 1.72e-09

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 59.55  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  73 LAERTREGGNPVIPlvedlteavgaeyGPYVHRGATSQDIMDTATMLVAARTL-DIVLADLGRTERALARLAAEHRDTPM 151
Cdd:PRK12425  115 LAGNGRGGKSPVHP-------------NDHVNRSQSSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVK 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 152 PGRTLTQHAVPTTFGLKAAGWRSLvLDARDRvtAVRDGLP-----AQLGGAAGT-LAAFTAYGAEDA------TGLPAAY 219
Cdd:PRK12425  182 TGRTHMMDATPITFGQELSAFVAQ-LDYAER--AIRAALPavcelAQGGTAVGTgLNAPHGFAEAIAaelaalSGLPFVT 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 220 ARElglREPLLPWHtlrTPIADLAGCLAFTVGALGKLAADVLTLS---RTEIAEVA-EGSGGGSSAMPHKANPVRSTLIA 295
Cdd:PRK12425  259 APN---KFAALAGH---EPLVSLSGALKTLAVALMKIANDLRLLGsgpRAGLAEVRlPANEPGSSIMPGKVNPTQCEALS 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 296 AAARRAPQLAATL-----YGSLAAEDERPAGAWHAewepLRDLLRLTGGAARDAAELTEGLRVHPDTMREHlgLTHGLIv 370
Cdd:PRK12425  333 MLACQVMGNDATIgfaasQGHLQLNVFKPVIIHNL----LQSIRLLADGCRNFQQHCVAGLEPDAEQMAAH--LERGLM- 405

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1892709055 371 serLSAELAPLLGRTRAkellTELARRTYAEGQPL 405
Cdd:PRK12425  406 ---LVTALNPHIGYDKA----AEIAKKAYAEGTTL 433
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 70-360 1.45e-07

argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129918 [Multi-domain]  Cd Length: 455  Bit Score: 53.51  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  70 LRSLAERTREGGNPVIPLVED--------LTEAVGAEYGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALAR 141
Cdd:TIGR00838  60 LNELKEEGREGPFILDPDDEDihmaiereLIDRVGEDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 142 LAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVL-------DARDRVtavrDGLPAQLGGAAGT-LAAFTAYGAEDaT 213
Cdd:TIGR00838 140 LAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLrdyerlqDALKRV----NVSPLGSGALAGTgFPIDREYLAEL-L 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 214 GLPAAYAREL-GLREpllpwhtlRTPIADLAGCLAFTVGALGKLAADVLTLSRTE--IAEVAEGSGGGSSAMPHKANPVR 290
Cdd:TIGR00838 215 GFDAVTENSLdAVSD--------RDFILELLFVAALIMVHLSRFAEDLILWSTGEfgFVELPDEFSSGSSIMPQKKNPDV 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 291 STLIAAAARRAPQLAATLYGSLAA----------EDErpagawhaewEPLRDLLRLTGGAARDAAELTEGLRVHPDTMRE 360
Cdd:TIGR00838 287 AELIRGKTGRVQGNLTGMLMTLKAlplaynrdlqEDK----------EPLFDALKTVELSLEMATGMLDTITVNKERMEE 356
PRK12308 PRK12308
argininosuccinate lyase;
91-314 1.75e-06

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 50.17  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055  91 LTEAVGaEYGPYVHRGATSQDIMDTATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFglkaA 170
Cdd:PRK12308   92 LIGKVG-DLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTF----A 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 171 GW-----------RSLVLDARDRVtavrDGLPAQLGGAAGtlaafTAYgAEDATGLpaayARELGLREPL---LPWHTLR 236
Cdd:PRK12308  167 HWclayvemferdYSRLEDALTRL----DTCPLGSGALAG-----TAY-PIDREAL----AHNLGFRRATrnsLDSVSDR 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 237 TPIADLAGCLAFTVGALGKLAADVLTLSRTE--IAEVAEGSGGGSSAMPHKANPVRSTLIAAAARRapqlaatLYGSLAA 314
Cdd:PRK12308  233 DHVMELMSVASISMLHLSRLAEDLIFYNSGEsgFIELADTVTSGSSLMPQKKNPDALELIRGKTGR-------VYGALAG 305
PLN00134 PLN00134
fumarate hydratase; Provisional
 102-431 2.54e-06

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 49.69  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 102 YVHRGATSQDIMDTATMLVAARTL-DIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDAR 180
Cdd:PLN00134  125 HVNRSQSSNDTFPTAMHIAAATEIhSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 181 DRVTAVRDGLP--AQLGGAAGT-LAAFTAYGAEDAtglpAAYARELGlreplLPWHTLRTPIADLAGCLAF--TVGALG- 254
Cdd:PLN00134  205 NRVQCTLPRLYelAQGGTAVGTgLNTKKGFDEKIA----AAVAEETG-----LPFVTAPNKFEALAAHDAFveLSGALNt 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 255 ------KLAADVLTLS---RTEIAEVA-EGSGGGSSAMPHKANPVR--STLIAAAARRAPQLAATLYGSlaaederpagA 322
Cdd:PLN00134  276 vavslmKIANDIRLLGsgpRCGLGELNlPENEPGSSIMPGKVNPTQceALTMVCAQVMGNHVAITVGGS----------A 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 323 WHAE---WEPL--RDLLR----LTGGAARDAAELTEGLRVHPDTMREHLGLTHGLIVSerlsaeLAPLLGRTRAkellTE 393
Cdd:PLN00134  346 GHFElnvFKPLiaYNLLHsirlLGDASASFRKNCVRGIEANRERISKLLHESLMLVTA------LNPKIGYDKA----AA 415

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1892709055 394 LARRTYAEGQPLAGLLAGEPALRDVALDELTDPARYTG 431
Cdd:PLN00134  416 VAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTG 453
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
115-431 5.49e-06

Aspartate ammonia-lyase [Amino acid transport and metabolism];


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 48.51  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 115 TATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDGL-PAQ 193
Cdd:COG1027   144 TAIRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLrEVN 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 194 LGG-AAGT-LAAFTAYGAE------DATGLPaaYARELGLREPLlpWHTlrTPIADLAGCLAFTVGALGKLAADVLTLS- 264
Cdd:COG1027   224 LGGtAIGTgLNAPPGYIELvvehlaEITGLP--LVRAENLIEAT--QDT--DAFVEVSGALKRLAVKLSKICNDLRLLSs 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 265 --RTEIAEV------AegsggGSSAMPHKANPVrstlIAAAARrapQLAATLYG-----SLAAEderpAG-----Awhae 326
Cdd:COG1027   298 gpRAGLGEInlpavqP-----GSSIMPGKVNPV----IPEVVN---QVAFQVIGndltvTMAAE----AGqlelnV---- 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 327 WEPL--RDLLR----LTGGAARDAAELTEGLRVHPDTMREHLGLTHGLIvserlsAELAPLLGRTRAkellTELARRTYA 400
Cdd:COG1027   358 FEPViaYNLLEsielLTNACRTLREKCIDGITANEERCREYVENSIGLV------TALNPYIGYEKA----AEIAKEALA 427

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1892709055 401 EGQPLAGLLAGEPALRDVALDELTDPARYTG 431
Cdd:COG1027   428 TGKSVRELVLEKGLLTEEELDEILDPENMTG 458
FumC COG0114
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 103-289 7.27e-06

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 48.10  E-value: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 103 VHRGATSQDIMDTAtMLVAARTL--DIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDAR 180
Cdd:COG0114   134 VNMSQSSNDTFPTA-MHIAAALAleERLLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGI 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 181 DRVTAVRDGLpAQL--GG-AAGT-LAAFTAYGAEDATGLpaayARELGlreplLPWHTLRTPIADLAGC--LAFTVGALG 254
Cdd:COG0114   213 ERIEAALPRL-YELalGGtAVGTgLNAHPGFAERVAAEL----AELTG-----LPFVSAPNKFEALAAHdaLVELSGALK 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1892709055 255 KLAADVLTLS----------RTEIAEVA----EgsgGGSSAMPHKANPV 289
Cdd:COG0114   283 TLAVSLMKIAndirwlasgpRCGLGEIRlpanE---PGSSIMPGKVNPT 328
aspA PRK12273
aspartate ammonia-lyase; Provisional
 115-289 5.87e-04

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 42.03  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 115 TATMLVAARTLDIVLADLGRTERALARLAAEHRDTPMPGRTLTQHAVPTTFGLKAAGWRSLVLDARDRVTAVRDGLPA-Q 193
Cdd:PRK12273  149 TAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREvN 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892709055 194 LGGaagtlaafTAYGaedaTGL--PAAYA-------REL-GLrePLlpwhtlrTPIADL------AGCLAFTVGA----- 252
Cdd:PRK12273  229 LGA--------TAIG----TGLnaPPGYIelvveklAEItGL--PL-------VPAEDLieatqdTGAFVEVSGAlkrla 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1892709055 253 --LGKLAADVLTLS---RTEIAEV------AegsggGSSAMPHKANPV 289
Cdd:PRK12273  288 vkLSKICNDLRLLSsgpRAGLNEInlpavqA-----GSSIMPGKVNPV 330
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 136-166 3.37e-03

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 39.58  E-value: 3.37e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1892709055 136 ERALARLAAEHRDTPMPGRTLTQHAVPTTFG 166
Cdd:PRK06705  143 QESILQLAADHKETIMPAYTHTQPAQPTTFG 173
 
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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