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Conserved domains on  [gi|918586415|ref|XP_013366875|]
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PREDICTED: adenylosuccinate lyase isoform X2 [Chinchilla lanigera]

Protein Classification

adenylosuccinate lyase( domain architecture ID 10129463)

adenylosuccinate lyase catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 20-455 0e+00

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: 896.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLDNIDFKMAAEEEKKLRHDVMAHVHTFG 99
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 100 HCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWI 179
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 180 QDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLQLFEGDHDKVEKLDRMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 259
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 260 SLGASVHKICTDIRLLANLKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTASVQWFERTLDDSAN 339
Cdd:cd03302  241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 340 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKQ 419
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 918586415 420 EGGDNDLIERIQADAYFSPIHSQLEHLLDPSSFTGR 455
Cdd:cd03302  401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 20-455 0e+00

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: 896.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLDNIDFKMAAEEEKKLRHDVMAHVHTFG 99
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 100 HCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWI 179
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 180 QDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLQLFEGDHDKVEKLDRMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 259
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 260 SLGASVHKICTDIRLLANLKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTASVQWFERTLDDSAN 339
Cdd:cd03302  241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 340 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKQ 419
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 918586415 420 EGGDNDLIERIQADAYFSPIHSQLEHLLDPSSFTGR 455
Cdd:cd03302  401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 20-460 3.45e-167

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: 478.04  E-value: 3.45e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLDN--IDFKMAAEEEKKLRHDVMAHVHT 97
Cdd:COG0015    2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  98 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSC 176
Cdd:COG0015   81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 177 LWIQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLqlfegdhDKVEKLDRMVTEKAGFKRAFiITGQTYTRKVDIEVLS 256
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHG-------EAWPEVEERVAEKLGLKPNP-VTTQIEPRDRHAELFS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 257 VLASLGASVHKICTDIRLLAN--LKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMdPLQTASVQWFERTL 334
Cdd:COG0015  233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 335 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 414
Cdd:COG0015  312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 918586415 415 AvvkqegGDNDLIERIQADAYFSPIHS--QLEHLLDPSSFTGRASQQV 460
Cdd:COG0015  392 E------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIV 433
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 20-461 1.66e-156

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: 450.65  E-value: 1.66e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLDNIDFKMAAEEEKKLRHDVMAHVHTF 98
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   99 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLW 178
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  179 IQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLqlfegdhDKVEKLDRMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 258
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAY-------PLVEEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  259 ASLGASVHKICTDIRLLANL--KEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTAsVQWFERTLDD 336
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  337 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAV 416
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEV 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 918586415  417 vkqegGDNDLIERIQADAYFSPIHSQLE--HLLDPSSFTGRASQQVS 461
Cdd:TIGR00928 392 -----DEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVE 433
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 251-454 4.29e-75

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 234.54  E-value: 4.29e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 251 DIEVLsVLASLGASVHKICTDIRLLANLK--EVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTAsVQ 328
Cdd:PRK08937  17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 329 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 408
Cdd:PRK08937  95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 918586415 409 LSQQAAAVVkqeggdNDLIERIQADAYFSPIHSQ--LEHLLDPSSFTG 454
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 381-460 5.25e-24

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: 95.17  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  381 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAAAVVKqeggdNDLIERIQADAYFS-PIHSQLEHLLDPSSFTGRASQQ 459
Cdd:pfam10397   1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74


                  .
gi 918586415  460 V 460
Cdd:pfam10397  75 V 75
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 380-460 5.24e-19

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: 81.34  E-value: 5.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   380 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKqeggdnDLIERIQADAYFSPIHS--QLEHLLDPSSFTGRAS 457
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74


                   ...
gi 918586415   458 QQV 460
Cdd:smart00998  75 AIV 77
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 20-455 0e+00

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: 896.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLDNIDFKMAAEEEKKLRHDVMAHVHTFG 99
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 100 HCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWI 179
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 180 QDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLQLFEGDHDKVEKLDRMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 259
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 260 SLGASVHKICTDIRLLANLKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTASVQWFERTLDDSAN 339
Cdd:cd03302  241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 340 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKQ 419
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 918586415 420 EGGDNDLIERIQADAYFSPIHSQLEHLLDPSSFTGR 455
Cdd:cd03302  401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 29-408 3.34e-176

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: 498.57  E-value: 3.34e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  29 MCFLFSDRNKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLDN--IDFKMAAEEEKKLRHDVMAHVHTFGHCCPK-A 105
Cdd:cd01595    1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADVfeIDAERIAEIEKETGHDVIAFVYALAEKCGEdA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 106 AGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCID 185
Cdd:cd01595   80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 186 LQNLTRVRDDLRFRGVKGTTGTQASFLqlfegdhDKVEKLDRMVTEKAGFKrAFIITGQTYTRKVDIEVLSVLASLGASV 265
Cdd:cd01595  160 LERLEEARERVLVGGISGAVGTHASLG-------PKGPEVEERVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 266 HKICTDIRLLAN--LKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTAsVQWFERTLDDSANRRIC 343
Cdd:cd01595  232 EKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDSSVERNI 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918586415 344 LAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 408
Cdd:cd01595  311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 20-460 3.45e-167

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: 478.04  E-value: 3.45e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLDN--IDFKMAAEEEKKLRHDVMAHVHT 97
Cdd:COG0015    2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  98 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSC 176
Cdd:COG0015   81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 177 LWIQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLqlfegdhDKVEKLDRMVTEKAGFKRAFiITGQTYTRKVDIEVLS 256
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHG-------EAWPEVEERVAEKLGLKPNP-VTTQIEPRDRHAELFS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 257 VLASLGASVHKICTDIRLLAN--LKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMdPLQTASVQWFERTL 334
Cdd:COG0015  233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 335 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 414
Cdd:COG0015  312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 918586415 415 AvvkqegGDNDLIERIQADAYFSPIHS--QLEHLLDPSSFTGRASQQV 460
Cdd:COG0015  392 E------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIV 433
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 20-461 1.66e-156

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: 450.65  E-value: 1.66e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLDNIDFKMAAEEEKKLRHDVMAHVHTF 98
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   99 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLW 178
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  179 IQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLqlfegdhDKVEKLDRMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 258
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAY-------PLVEEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  259 ASLGASVHKICTDIRLLANL--KEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTAsVQWFERTLDD 336
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  337 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAV 416
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEV 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 918586415  417 vkqegGDNDLIERIQADAYFSPIHSQLE--HLLDPSSFTGRASQQVS 461
Cdd:TIGR00928 392 -----DEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVE 433
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 39-368 4.01e-100

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: 302.88  E-value: 4.01e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  39 FRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLDNIDFKMAA---EEEKKLRHDVMAHVHTFGHCCPKA-AGIIHLGAT 114
Cdd:cd01334    1 IRADLQVEKAHAKALAELGL-LPKEAAEAILAALDEILEGIAAdqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 115 SCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRD 194
Cdd:cd01334   80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 195 DLRFRGVKGTT-GTQASFlqlfegdhdkVEKLDRMVTEKAGFKRAFIITGQ-TYTRKVDIEVLSVLASLGASVHKICTDI 272
Cdd:cd01334  160 RLNVLPLGGGAvGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 273 RLLAN--LKEVEEPFEKQqIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTASvQWFERTLDDSANRRICLAEAFLT 350
Cdd:cd01334  230 RLLSSgeFGEVELPDAKQ-PGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDL 307

                        330
                 ....*....|....*...
gi 918586415 351 ADTILNTLQNISEGLVVY 368
Cdd:cd01334  308 LDAALRLLTGVLEGLEVN 325
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 23-407 5.26e-80

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: 253.24  E-value: 5.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  23 RYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLDnIDFKMAAEEEKKLRHDVMAHVHTFGHCC 102
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGV-IPAEAAEEIRKKAK-FDVERVKEIEAETKHDVIAFVTAIAEYC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 103 PKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDL 182
Cdd:cd01360   79 GEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 183 CIDLQNLTRVRDDLRFRGVKGTTGTQASFlqlfegdHDKVEKLdrmVTEKAGFKRAFIITgQTYTRKVDIEVLSVLASLG 262
Cdd:cd01360  159 KRHLERLKEARERILVGKISGAVGTYANL-------GPEVEER---VAEKLGLKPEPIST-QVIQRDRHAEYLSTLALIA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 263 ASVHKICTDIRLL--ANLKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVmDPLQTASVQWFERTLDDSANR 340
Cdd:cd01360  228 STLEKIATEIRHLqrTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNV-IPALENVALWHERDISHSSVE 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 918586415 341 RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIR 407
Cdd:cd01360  307 RVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQ 373
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 251-454 4.29e-75

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 234.54  E-value: 4.29e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 251 DIEVLsVLASLGASVHKICTDIRLLANLK--EVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTAsVQ 328
Cdd:PRK08937  17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 329 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 408
Cdd:PRK08937  95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 918586415 409 LSQQAAAVVkqeggdNDLIERIQADAYFSPIHSQ--LEHLLDPSSFTG 454
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 20-460 2.54e-55

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: 190.15  E-value: 2.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  20 LASRYASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGL--PITDEQIQEmKSNLDNIDFKMAAEEEKKLRHDVMAHVHT 97
Cdd:cd01597    2 LGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVipKEAAAEIAA-AADVERLDLEALAEATARTGHPAIPLVKQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  98 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSC 176
Cdd:cd01597   81 LTAACGDAAGeYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 177 LWIQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFlqlfeGDHDkvekldrMVTEKAGFKR----AFIITGQTyTRKVDI 252
Cdd:cd01597  161 VWLSELLRHRERLDELRPRVLVVQFGGAAGTLASL-----GDQG-------LAVQEALAAElglgVPAIPWHT-ARDRIA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 253 EVLSVLASLGASVHKICTDIRLL--ANLKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLAR---HLMGLVMDplqtASV 327
Cdd:cd01597  228 ELASFLALLTGTLGKIARDVYLLmqTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARrvpGLAALLLD----AMV 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 328 QWFERtlDDSANR--RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGsRQDCHEK 405
Cdd:cd01597  304 QEHER--DAGAWHaeWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLG-RQEAHDL 380

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 918586415 406 IRVLSQQAAAvvkqEGGdnDLIERIQAD----AYFSPihSQLEHLLDPSSFTGRASQQV 460
Cdd:cd01597  381 VYEACMRAVE----EGR--PLREVLLEDpevaAYLSD--EELDALLDPANYLGSAPALV 431
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 99-359 1.64e-44

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: 155.46  E-value: 1.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  99 GHCCPKAAGII-----HLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGK 173
Cdd:cd01594   22 GRAGELAGGLHgsalvHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGY 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 174 RSCLWIQDLCIDLQNLTRVRDdlrfrgvkgttgtqasflqlfegdhdkvekldrmvtekagfkrafiitgqtytrkvdIE 253
Cdd:cd01594  102 ELRAWAQVLGRDLERLEEAAV---------------------------------------------------------AE 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 254 VLSVLASLGASVHKICTDIRLLANLK--EVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLqTASVQWFE 331
Cdd:cd01594  125 ALDALALAAAHLSKIAEDLRLLLSGEfgELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVL-TALKGGPE 203

                        250       260
                 ....*....|....*....|....*...
gi 918586415 332 RTLDDSANRRICLAEAFLTADTILNTLQ 359
Cdd:cd01594  204 RDNEDSPSMREILADSLLLLIDALRLLL 231
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 20-334 1.80e-29

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: 117.92  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   20 LASRYAS-PEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLDNIDFKMAAEEE-------------K 85
Cdd:TIGR02426   1 LLDGLFGdPAALELFSDRAFLRAMLDFEAALARAQADAGL-IPAEAAAAIEAACAAAAPDLEALAHaaatagnpviplvK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   86 KLRHDVMAhvhtfghccpKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQP 165
Cdd:TIGR02426  80 ALRKAVAG----------EAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  166 AQLTTVGKRSCLWIQDLCIDLQNLTRVRDD---LRFRGVKGTtgtqasflqlfegdHDKVEKLDRMVTEKAGFKRAFIIT 242
Cdd:TIGR02426 150 AVPTTFGLKAAGWLAAVLRARDRLAALRTRalpLQFGGAAGT--------------LAALGTRGGAVAAALAARLGLPLP 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  243 GQTY--TRKVDIEVLSVLASLGASVHKICTDIRLLANLkEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMd 320
Cdd:TIGR02426 216 ALPWhtQRDRIAEFGSALALVAGALGKIAGDIALLSQT-EVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAA- 293

                         330
                  ....*....|....
gi 918586415  321 PLQTASVQWFERTL 334
Cdd:TIGR02426 294 TLHAALPQEHERSL 307
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 381-460 5.25e-24

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: 95.17  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  381 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAAAVVKqeggdNDLIERIQADAYFS-PIHSQLEHLLDPSSFTGRASQQ 459
Cdd:pfam10397   1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74


                  .
gi 918586415  460 V 460
Cdd:pfam10397  75 V 75
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 18-460 1.48e-20

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


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 93.93  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  18 SPLASRY-ASPEMCFLFSDRNKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLDNIDFKMAAEEE----------- 84
Cdd:PRK09053   5 ARLTDLYfGSPAMRAIFSDRATVQRMLDFEAALARAEAACGViPAAAVAPIEAACDAERLDLDALAQAAalagnlaiplv 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  85 KKLRHDVMAHVhtfghccPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQ 164
Cdd:PRK09053  85 KQLTAQVAARD-------AEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 165 PAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFlqlfeGDHdkveklDRMVTEKAGFKRAFIITGQ 244
Cdd:PRK09053 158 QALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASL-----GEQ------ALPVAQALAAELQLALPAL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 245 TYTRKVD--IEVLSVLASLGASVHKICTDIRLL--ANLKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMGLVMD 320
Cdd:PRK09053 227 PWHTQRDriAEFASALGLLAGTLGKIARDVSLLmqTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVAT 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 321 pLQTASVQWFERTLD------DSANRRICLAEAFLTAdtilntLQNISEGLVVYPKvierRIRQELPfmATENIIMA--- 391
Cdd:PRK09053 307 -LFAAMPQEHERALGgwhaewDTLPELACLAAGALAQ------MAQIVEGLEVDAA----RMRANLD--LTHGLILAeav 373

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918586415 392 MVKAGGS--RQDCHEKIRVLSQQAAAvvKQEGGDNDLIERIQADAYFSPihSQLEHLLDPSSFTGRASQQV 460
Cdd:PRK09053 374 MLALADRigRLDAHHLVEQASKRAVA--EGRHLRDVLAEDPQVSAHLSP--AALDRLLDPAHYLGQAHAWV 440
Lyase_1 pfam00206
Lyase;
25-316 1.68e-20

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 91.66  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   25 ASPEMCFLFSDRN--KFRTWRQLWLW---LAEAEQTLGLPIT----------DEQIQEMKSNLDNI----------DFKM 79
Cdd:pfam00206   6 PADALMGIFTDRSrfNFRLGEEDIKGlaaLKKAAAKANVILKeeaaaiikalDEVAEEGKLDDQFPlkvwqegsgtAVNM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   80 AAEEekKLRHDVMAHVHTFGHccpkaagiIHLGATScyvGD--NTDL-IILRNA-FDLLLPKLARVISRLADFAKEHANL 155
Cdd:pfam00206  86 NLNE--VIGELLGQLVHPNDH--------VHTGQSS---NDqvPTALrLALKDAlSEVLLPALRQLIDALKEKAKEFADI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  156 PTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGTTGTQASFLQLFEGDHDKVEKLDRMvtEKAGF 235
Cdd:pfam00206 153 VKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--TGLPV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  236 KRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEVEEPFEKQQIGSSAMPYKRNPMRSERCCSLARH 313
Cdd:pfam00206 231 KAPNSFE-ATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGR 309


                  ...
gi 918586415  314 LMG 316
Cdd:pfam00206 310 VMG 312
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 380-460 5.24e-19

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: 81.34  E-value: 5.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415   380 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKqeggdnDLIERIQADAYFSPIHS--QLEHLLDPSSFTGRAS 457
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74


                   ...
gi 918586415   458 QQV 460
Cdd:smart00998  75 AIV 77
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 46-380 3.28e-18

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: 86.52  E-value: 3.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  46 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLDNIDFKMA---AEEEKKLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 113
Cdd:cd01598   21 WLiALSNLEEIPEVPpLTKEELKFLRAIIENFSEEDAlriKEIEATTNHDVKAveyflkeKFETLGLL-KKIKEFIHFAC 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 114 TScyvGDNTDLII---LRNAF-DLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNL 189
Cdd:cd01598  100 TS---EDINNLAYalmIKEARnEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 190 TRVRDDLRFrgvKGTTGT----QASFLQLfegDHDKVEKLdrmvtekagFKRAFIITGQTYTRKVD-----IEVLSVLAS 260
Cdd:cd01598  177 KQIEILGKF---NGAVGNfnahLVAYPDV---DWRKFSEF---------FVTSLGLTWNPYTTQIEphdyiAELFDALAR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 261 LGASVHKICTDIRLLANLKEVEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHL-MGLVMDPLQtasvqwfeR 332
Cdd:cd01598  242 INTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAegnlglsNALLNHLsAKLPISRLQ--------R 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 918586415 333 TLDDSANRR---ICLAEAFLTADTILNTLQNISeglvvypkVIERRIRQEL 380
Cdd:cd01598  314 DLTDSTVLRnigVAFGHSLIAYKSLLRGLDKLE--------LNEARLLEDL 356
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 103-312 8.17e-16

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 78.56  E-value: 8.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 103 PKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDL 182
Cdd:PRK05975  96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 183 CIDLQNLTRVRDD---LRFRGVKGTtgtqasfLQLFEGDHDKV-----EKLDRMVTEKAGFKRAFIitgqtytrkVDIEV 254
Cdd:PRK05975 176 LRHRDRLEALRADvfpLQFGGAAGT-------LEKLGGKAAAVrarlaKRLGLEDAPQWHSQRDFI---------ADFAH 239

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918586415 255 LsvLASLGASVHKICTDIRLLANLKEveepfEKQQIG---SSAMPYKRNPMRSERCCSLAR 312
Cdd:PRK05975 240 L--LSLVTGSLGKFGQDIALMAQAGD-----EISLSGgggSSAMPHKQNPVAAETLVTLAR 293
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 18-173 3.63e-11

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 64.77  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  18 SPLASRYAS------PemcfLFSDR--NKFRTWRQL-WL-WLAEAEQTLGLP-ITDEQIQEMKSNLDNIDFKMAA---EE 83
Cdd:PRK09285  10 SPLDGRYASktaalrP----IFSEFglIRYRVQVEVeWLiALAAHPGIPEVPpFSAEANAFLRAIVENFSEEDAArikEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  84 EKKLRHDVMA-------HVHTFGHCcPKAAGIIHLGATScyvGDNTDL---IILRNAFD-LLLPKLARVISRLADFAKEH 152
Cdd:PRK09285  86 ERTTNHDVKAveyflkeKLAGLPEL-EAVSEFIHFACTS---EDINNLshaLMLKEAREeVLLPALRELIDALKELAHEY 161

                        170       180
                 ....*....|....*....|.
gi 918586415 153 ANLPTLGFTHFQPAQLTTVGK 173
Cdd:PRK09285 162 ADVPMLSRTHGQPATPTTLGK 182
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 127-317 5.51e-10

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 61.32  E-value: 5.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 127 LRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQnltRVRDDLR--------- 197
Cdd:PRK00855 123 LRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLE---RLRDARKrvnrsplgs 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 198 --FRGVkgttgtqaSFlqlfegdhdkveKLDR-MVTEKAGFKRAFI--ITGQTyTRKVDIEVLSVLASLGASVHKICTDI 272
Cdd:PRK00855 200 aaLAGT--------TF------------PIDReRTAELLGFDGVTEnsLDAVS-DRDFALEFLSAASLLMVHLSRLAEEL 258

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918586415 273 RLLANlkeveepfekQQI-----------GSSAMPYKRNP-----MRSeRCCSLARHLMGL 317
Cdd:PRK00855 259 ILWSS----------QEFgfvelpdafstGSSIMPQKKNPdvaelIRG-KTGRVYGNLTGL 308
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 134-301 7.41e-09

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: 57.53  E-value: 7.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 134 LLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGT---TGTQAS 210
Cdd:cd01357  155 LLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTaigTGINAP 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 211 flqlfEGDHDKVEKLDRMVTeKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLL-----ANLKEVEEPf 285
Cdd:cd01357  235 -----PGYIELVVEKLSEIT-GLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLssgprAGLGEINLP- 307

                        170
                 ....*....|....*.
gi 918586415 286 eKQQIGSSAMPYKRNP 301
Cdd:cd01357  308 -AVQPGSSIMPGKVNP 322
PLN02848 PLN02848
adenylosuccinate lyase
 18-173 2.51e-08

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 55.90  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  18 SPLASRYAS--PEMCFLFSDRN--KFRTWRQLwLWLAEAEQTLGL----PITDEQIQEMKSNLDNIDFKMAAEE---EKK 86
Cdd:PLN02848  13 SPLDGRYWSkvKDLRPIFSEFGliRYRVLVEV-KWLLKLSQIPEVtevpPFSDEANSFLEGIIAGFSVDDALEVkkiERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415  87 LRHDVMAhVHTF--GHCC--PKAAGI---IHLGATSCYVGDNTDLIILRNAFD-LLLPKLARVISRLADFAKEHANLPTL 158
Cdd:PLN02848  92 TNHDVKA-VEYFlkQKCKshPELAKVlefFHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHEFAYVPML 170

                        170
                 ....*....|....*
gi 918586415 159 GFTHFQPAQLTTVGK 173
Cdd:PLN02848 171 SRTHGQPASPTTLGK 185
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 134-301 3.51e-08

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: 55.51  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 134 LLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGT---TG--TQ 208
Cdd:cd01596  155 LLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTavgTGlnAP 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 209 ASFLQLFegdhdkVEKLDRmvtekagfkrafiITGQTYTR---KVD--------IEVLSVLASLGASVHKICTDIRLLAN 277
Cdd:cd01596  235 PGYAEKV------AAELAE-------------LTGLPFVTapnLFEataahdalVEVSGALKTLAVSLSKIANDLRLLSS 295

                        170       180
                 ....*....|....*....|....*....
gi 918586415 278 -----LKEVEEPfEKQQiGSSAMPYKRNP 301
Cdd:cd01596  296 gpragLGEINLP-ANQP-GSSIMPGKVNP 322
aspA PRK12273
aspartate ammonia-lyase; Provisional
 127-301 5.68e-08

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 54.75  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 127 LRNAFDLLLPKLARVISRLAD-F---AKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVK 202
Cdd:PRK12273 151 IRIALLLSLRKLLDALEQLQEaFeakAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLG 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 203 GT---TG--TQASFLQLFegdhdkVEKLDRmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 266
Cdd:PRK12273 231 ATaigTGlnAPPGYIELV------VEKLAE-------------ITGLPLVPAEDlieatqdtgafVEVSGALKRLAVKLS 291

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 918586415 267 KICTDIRLL-----ANLKEVEEPfeKQQIGSSAMPYKRNP 301
Cdd:PRK12273 292 KICNDLRLLssgprAGLNEINLP--AVQAGSSIMPGKVNP 329
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 122-386 1.25e-07

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: 53.70  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 122 TDL-IILRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFR- 199
Cdd:cd01359   93 TDLrLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVSp 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 200 -GVKGTTGTqaSFlqlfegdhdkveKLDR-MVTEKAGFKRafiITGQTY----TRKVDIEVLSVLASLGASVHKICTDIR 273
Cdd:cd01359  173 lGAGALAGT--TF------------PIDReRTAELLGFDG---PTENSLdavsDRDFVLEFLSAAALLMVHLSRLAEDLI 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 274 LLA----NLKEVEEPFEKqqiGSSAMPYKRNPMRSERCCSLARHLMGLVMDPLQTAsvqwfeRTLDDSANRriCLAEA-- 347
Cdd:cd01359  236 LWStqefGFVELPDAYST---GSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTL------KGLPLAYNK--DLQEDke 304

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 918586415 348 --FLTADTILNTLQnISEGLVVYPKVIERRIRQEL--PFM-ATE 386
Cdd:cd01359  305 plFDAVDTLIASLR-LLTGVISTLTVNPERMREAAeaGFStATD 347
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
127-301 1.20e-06

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


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 50.82  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 127 LRNAFDLLLPKLARVISRLAD-F---AKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVK 202
Cdd:COG1027  146 IRLALLLLLRELLEALERLQEaFaakAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLG 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 203 GT---TGTQASflqlfEGDHDKV-EKLDRmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHK 267
Cdd:COG1027  226 GTaigTGLNAP-----PGYIELVvEHLAE-------------ITGLPLVRAENlieatqdtdafVEVSGALKRLAVKLSK 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 918586415 268 ICTDIRLLA----------NLKEVeepfekqQIGSSAMPYKRNP 301
Cdd:COG1027  288 ICNDLRLLSsgpraglgeiNLPAV-------QPGSSIMPGKVNP 324
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 134-305 3.11e-06

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 49.60  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 134 LLPKLARVISRLADF----AKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGT---TG 206
Cdd:PRK13353 156 LLEGLLAAMGALQDVfeekAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTavgTG 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 207 TQAsflqlfegDHDKVEKLDRMVTEKAG--FKRAF-IITGqtyTRKVD--IEVLSVLASLGASVHKICTDIRLLAN---- 277
Cdd:PRK13353 236 LNA--------DPEYIERVVKHLAAITGlpLVGAEdLVDA---TQNTDafVEVSGALKVCAVNLSKIANDLRLLSSgprt 304

                        170       180
                 ....*....|....*....|....*....
gi 918586415 278 -LKEVEEPfeKQQIGSSAMPYKRNPMRSE 305
Cdd:PRK13353 305 gLGEINLP--AVQPGSSIMPGKVNPVMPE 331
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 134-316 2.30e-05

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: 46.72  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 134 LLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGT---TGTQAs 210
Cdd:cd01362  156 LLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTavgTGLNA- 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 211 flqlfegdhdkvekldrmvteKAGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 274
Cdd:cd01362  235 ---------------------HPGFAEKVAaelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 293

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 918586415 275 LAN-----LKEVEEPfeKQQIGSSAMPYKRNPMRSERCCSLARHLMG 316
Cdd:cd01362  294 LGSgprcgLGELSLP--ENEPGSSIMPGKVNPTQCEALTMVAAQVMG 338
fumC PRK00485
fumarate hydratase; Reviewed
 134-317 1.28e-04

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 44.31  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 134 LLPKLARVISRLADFAKEHANLPTLGFTHFQPAQLTTVGKRSCLWIQDLCIDLQNLTRVRDDLRFRGVKGT---TGTQAs 210
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTavgTGLNA- 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918586415 211 flqlfegdhdkvekldrmvteKAGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 274
Cdd:PRK00485 239 ---------------------HPGFAERVAeelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 297

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 918586415 275 LAN-----LKEVEEPfeKQQIGSSAMPYKRNPMRSERCCSLARHLMGL 317
Cdd:PRK00485 298 LASgprcgLGEISLP--ENEPGSSIMPGKVNPTQCEALTMVCAQVMGN 343
PLN02646 PLN02646
argininosuccinate lyase
 127-167 8.78e-03

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 38.55  E-value: 8.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 918586415 127 LRNAFDLLLPKLARVISRLADFAKEHANLPTLGFTHFQPAQ 167
Cdd:PLN02646 135 CRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQ 175
 
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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