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Conserved domains on  [gi|961652663|ref|NP_001304852|]
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adenylosuccinate lyase isoform c [Homo sapiens]

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 ...
 1-388 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: 791.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   1 MKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:cd03302   49 MKANVENIDFEIAAAEEKKLRHDVMAHVHAFGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDK 160
Cdd:cd03302  129 FALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC 240
Cdd:cd03302  209 LVTKKAGFKKVYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERC 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 241 CSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATEN 320
Cdd:cd03302  289 CSLARHLMNLASNAAQTASTQWFERTLDDSANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATEN 368

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961652663 321 IIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 388
Cdd:cd03302  369 IIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQEGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 1-388 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: 791.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   1 MKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:cd03302   49 MKANVENIDFEIAAAEEKKLRHDVMAHVHAFGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDK 160
Cdd:cd03302  129 FALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC 240
Cdd:cd03302  209 LVTKKAGFKKVYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERC 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 241 CSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATEN 320
Cdd:cd03302  289 CSLARHLMNLASNAAQTASTQWFERTLDDSANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATEN 368

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961652663 321 IIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 388
Cdd:cd03302  369 IIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQEGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 2-396 1.99e-144

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: 418.33  E-value: 1.99e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   2 KSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:COG0015   52 AADDFEIDAERIKEIEKETRHDVKAFVYALKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDK 160
Cdd:COG0015  132 LAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEE 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKRAFiITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:COG0015  205 RVAEKLGLKPNP-VTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSE 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 239 RCCSLARHLMTLVMdPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMAT 318
Cdd:COG0015  284 NIEGLARLARALAA-ALLEALASWHERDLSDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLS 362

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 319 ENIIMAMVKAGGSRQDCHEKIRVLSQQAASvvkqegGDNDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRASQQVQRF 396
Cdd:COG0015  363 EAVLMALVRRGLGREEAYELVKELARGAWE------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 1-396 2.62e-134

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: 392.48  E-value: 2.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663    1 MKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:TIGR00928  50 EKANFTEVDLERIKEIEAVTRHDVKAVVYALKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFegddhkvEQLDK 160
Cdd:TIGR00928 130 LAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  161 MVTEKAGFKRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:TIGR00928 203 RVTEFLGLKPVPIST-QIEPRDRHAELLDALALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFE 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  239 RCCSLARHLMTLVMDPLQTAsVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMAT 318
Cdd:TIGR00928 282 NVCGLARVIRGYASPALENA-PLWHERDLTDSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIAS 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  319 ENIIMAMVKAGGSRQDCHEKIRVLSQQAAsvvkqEGGDNDLIERIQVDAYFSPIHSQLD--HLLDPSSFTGRASQQVQRF 396
Cdd:TIGR00928 361 ERVLIALVERGMGREEAYEIVRELAMGAA-----EVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 184-387 5.44e-73

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 227.60  E-value: 5.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 184 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 261
Cdd:PRK08937  17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 262 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 341
Cdd:PRK08937  95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 961652663 342 LSQQAASVVkqeggdNDLIERIQVDAYFSPIHSQ--LDHLLDPSSFTG 387
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 314-396 5.09e-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: 94.79  E-value: 5.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  314 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAASVVKqeggdNDLIERIQVDAYFS-PIHSQLDHLLDPSSFTGRASQQ 392
Cdd:pfam10397   1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74


                  ....
gi 961652663  393 VQRF 396
Cdd:pfam10397  75 VDRV 78
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 313-397 1.75e-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: 82.11  E-value: 1.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   313 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKqeggdnDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRAS 390
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74


                   ....*..
gi 961652663   391 QQVQRFL 397
Cdd:smart00998  75 AIVDRVL 81
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 1-388 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: 791.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   1 MKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:cd03302   49 MKANVENIDFEIAAAEEKKLRHDVMAHVHAFGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDK 160
Cdd:cd03302  129 FALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC 240
Cdd:cd03302  209 LVTKKAGFKKVYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERC 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 241 CSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATEN 320
Cdd:cd03302  289 CSLARHLMNLASNAAQTASTQWFERTLDDSANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATEN 368

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961652663 321 IIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 388
Cdd:cd03302  369 IIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQEGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 2-341 5.08e-155

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: 443.10  E-value: 5.08e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   2 KSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPK-AAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:cd01595   42 AADVFEIDAERIAEIEKETGHDVIAFVYALAEKCGEdAGEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQlfegddhKVEQLDK 160
Cdd:cd01595  122 LALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKrAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:cd01595  195 RVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSE 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 239 RCCSLARHLMTLVMDPLQTAsVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMAT 318
Cdd:cd01595  274 NIEGLARLVRALAAPALENL-VQWHERDLSDSSVERNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILS 352

                        330       340
                 ....*....|....*....|...
gi 961652663 319 ENIIMAMVKAGGSRQDCHEKIRV 341
Cdd:cd01595  353 EAVMMALAKKGLGRQEAYELVKE 375
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 2-396 1.99e-144

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: 418.33  E-value: 1.99e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   2 KSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:COG0015   52 AADDFEIDAERIKEIEKETRHDVKAFVYALKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDK 160
Cdd:COG0015  132 LAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEE 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKRAFiITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:COG0015  205 RVAEKLGLKPNP-VTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSE 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 239 RCCSLARHLMTLVMdPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMAT 318
Cdd:COG0015  284 NIEGLARLARALAA-ALLEALASWHERDLSDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLS 362

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 319 ENIIMAMVKAGGSRQDCHEKIRVLSQQAASvvkqegGDNDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRASQQVQRF 396
Cdd:COG0015  363 EAVLMALVRRGLGREEAYELVKELARGAWE------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 1-396 2.62e-134

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: 392.48  E-value: 2.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663    1 MKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:TIGR00928  50 EKANFTEVDLERIKEIEAVTRHDVKAVVYALKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFegddhkvEQLDK 160
Cdd:TIGR00928 130 LAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  161 MVTEKAGFKRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:TIGR00928 203 RVTEFLGLKPVPIST-QIEPRDRHAELLDALALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFE 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  239 RCCSLARHLMTLVMDPLQTAsVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMAT 318
Cdd:TIGR00928 282 NVCGLARVIRGYASPALENA-PLWHERDLTDSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIAS 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  319 ENIIMAMVKAGGSRQDCHEKIRVLSQQAAsvvkqEGGDNDLIERIQVDAYFSPIHSQLD--HLLDPSSFTGRASQQVQRF 396
Cdd:TIGR00928 361 ERVLIALVERGMGREEAYEIVRELAMGAA-----EVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 1-301 2.19e-88

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: 271.30  E-value: 2.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   1 MKSNLENIDFKMAA---EEEKRLRHDVMAHVHTFGHCCPKA-AGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVIS 76
Cdd:cd01334   29 ILAALDEILEGIAAdqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALID 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  77 RLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTT-GTQASFlqlfegddhkV 155
Cdd:cd01334  109 ALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLNVLPLGGGAvGTGANA----------P 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 156 EQLDKMVTEKAGFKRAFIITGQ-TYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQqIGSSAMPYKR 232
Cdd:cd01334  179 PIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDLRLLSSgeFGEVELPDAKQ-PGSSIMPQKV 257

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961652663 233 NPMRSERCCSLARHLMTLVMDPLQTASvQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVY 301
Cdd:cd01334  258 NPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGLEVN 325
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 184-387 5.44e-73

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 227.60  E-value: 5.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 184 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 261
Cdd:PRK08937  17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 262 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 341
Cdd:PRK08937  95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 961652663 342 LSQQAASVVkqeggdNDLIERIQVDAYFSPIHSQ--LDHLLDPSSFTG 387
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 1-340 3.09e-65

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: 213.57  E-value: 3.09e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   1 MKSNLENIDfkmaaEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:cd01360   49 AKFDVERVK-----EIEAETKHDVIAFVTAIAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfegdDHKVEqldK 160
Cdd:cd01360  124 KALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKISGAVGTYANL-------GPEVE---E 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:cd01360  194 RVAEKLGLKPEPIST-QVIQRDRHAEYLSTLALIASTLEKIATEIRHLqrTEVLEVEEPFSKGQKGSSAMPHKRNPILSE 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 239 RCCSLARHLMTLVmDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMAT 318
Cdd:cd01360  273 NICGLARVIRSNV-IPALENVALWHERDISHSSVERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFS 351

                        330       340
                 ....*....|....*....|..
gi 961652663 319 ENIIMAMVKAGGSRQDCHEKIR 340
Cdd:cd01360  352 QRVLLALVEKGMSREEAYEIVQ 373
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 2-399 2.69e-48

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: 170.12  E-value: 2.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   2 KSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLAD 80
Cdd:cd01597   52 AADVERLDLEALAEATARTGHPAIPLVKQLTAACGDAAGeYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALAR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  81 FAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfeGDDhkveqldK 160
Cdd:cd01597  132 LAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGGAAGTLASL-----GDQ-------G 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 161 MVTEKAGFKR----AFIITGQTyTRKVDIEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNP 234
Cdd:cd01597  200 LAVQEALAAElglgVPAIPWHT-ARDRIAELASFLALLTGTLGKIARDVYLLmqTEIGEVAEPFAKGRGGSSTMPHKRNP 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 235 MRSERCCSLAR---HLMTLVMDplqtASVQWFERtlDDSANR--RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRI 309
Cdd:cd01597  279 VGCELIVALARrvpGLAALLLD----AMVQEHER--DAGAWHaeWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANL 352

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 310 RQELPFMATENIIMAMVKAGGsRQDCHEKIRVLSQQAAsvvkQEGGdnDLIERI----QVDAYFSPihSQLDHLLDPSSF 385
Cdd:cd01597  353 DLTGGLILSEAVMMALAPKLG-RQEAHDLVYEACMRAV----EEGR--PLREVLledpEVAAYLSD--EELDALLDPANY 423

                        410
                 ....*....|....
gi 961652663 386 TGRASQQVQRFLEE 399
Cdd:cd01597  424 LGSAPALVDRVLAR 437
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 32-292 9.81e-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: 152.38  E-value: 9.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  32 GHCCPKAAGII-----HLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGK 106
Cdd:cd01594   22 GRAGELAGGLHgsalvHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGY 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 107 RCCLWIQDLCMDLQNLKRVRDdlrfrgvkgttgtqasflqlfegddhkveqldkmvtekagfkrafiitgqtytrkvdIE 186
Cdd:cd01594  102 ELRAWAQVLGRDLERLEEAAV---------------------------------------------------------AE 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 187 VLSVLASLGASVHKICTDIRLLANLKEME--EPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLqTASVQWFE 264
Cdd:cd01594  125 ALDALALAAAHLSKIAEDLRLLLSGEFGElgEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVL-TALKGGPE 203

                        250       260
                 ....*....|....*....|....*...
gi 961652663 265 RTLDDSANRRICLAEAFLTADTILNTLQ 292
Cdd:cd01594  204 RDNEDSPSMREILADSLLLLIDALRLLL 231
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 37-267 1.49e-26

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: 109.07  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   37 KAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLC 116
Cdd:TIGR02426  88 EAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAAVL 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  117 MDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDkMVTEKAGF--KRAFIItgqtytrkvdiEVL 188
Cdd:TIGR02426 168 RARDRLAALRTRalpLQFGGAAGTlaaLGTRGGAVA-----AALAARLG-LPLPALPWhtQRDRIA-----------EFG 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961652663  189 SVLASLGASVHKICTDIRLLANLkEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 267
Cdd:TIGR02426 231 SALALVAGALGKIAGDIALLSQT-EVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAA-TLHAALPQEHERSL 307
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 314-396 5.09e-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: 94.79  E-value: 5.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  314 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAASVVKqeggdNDLIERIQVDAYFS-PIHSQLDHLLDPSSFTGRASQQ 392
Cdd:pfam10397   1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74


                  ....
gi 961652663  393 VQRF 396
Cdd:pfam10397  75 VDRV 78
Lyase_1 pfam00206
Lyase;
9-238 7.10e-21

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 92.43  E-value: 7.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663    9 DFKMAAEEekRLRHDVMAHVHTFGHccpkaagiIHLGATScyvGD--NTDL-IILRNAL-DLLLPKLARVISRLADFAKE 84
Cdd:pfam00206  82 AVNMNLNE--VIGELLGQLVHPNDH--------VHTGQSS---NDqvPTALrLALKDALsEVLLPALRQLIDALKEKAKE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   85 RASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMvtE 164
Cdd:pfam00206 149 FADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--T 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961652663  165 KAGFKRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 238
Cdd:pfam00206 227 GLPVKAPNSFE-ATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 36-399 9.57e-20

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


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 90.85  E-value: 9.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  36 PKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDL 115
Cdd:PRK09053  96 AEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDAL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 116 CMDLQNLKRVRDDLRFRGVKGTTGTQASF----------------LQLFEGDDHKveQLDKMVtekagfkrafiitgqty 179
Cdd:PRK09053 176 LRHRQRLAALRPRALVLQFGGAAGTLASLgeqalpvaqalaaelqLALPALPWHT--QRDRIA----------------- 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 180 trkvdiEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDpLQT 257
Cdd:PRK09053 237 ------EFASALGLLAGTLGKIARDVSLLmqTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVAT-LFA 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 258 ASVQWFERTLD------DSANRRICLAEAFLTAdtilntLQNISEGLVVYPKvierRIRQELPfmATENIIMA---MVKA 328
Cdd:PRK09053 310 AMPQEHERALGgwhaewDTLPELACLAAGALAQ------MAQIVEGLEVDAA----RMRANLD--LTHGLILAeavMLAL 377

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961652663 329 GGS--RQDCHEKIRVLSQQAasVVKQEGGDNDLIERIQVDAYFSPihSQLDHLLDPSSFTGRASQQVQRFLEE 399
Cdd:PRK09053 378 ADRigRLDAHHLVEQASKRA--VAEGRHLRDVLAEDPQVSAHLSP--AALDRLLDPAHYLGQAHAWVDRVLAE 446
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 313-397 1.75e-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: 82.11  E-value: 1.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   313 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKqeggdnDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRAS 390
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74


                   ....*..
gi 961652663   391 QQVQRFL 397
Cdd:smart00998  75 AIVDRVL 81
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 9-313 1.26e-16

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: 81.13  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   9 DFKMAAEEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGATScyvGDNTDLII---LRNAL-DLLLPKLARVISR 77
Cdd:cd01598   56 DALRIKEIEATTNHDVKAveyflkeKFETLGLL-KKIKEFIHFACTS---EDINNLAYalmIKEARnEVILPLLKEIIDS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  78 LADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFrgvKGTTGTQASflqlfegddHKVE- 156
Cdd:cd01598  132 LKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQIEILGKF---NGAVGNFNA---------HLVAy 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 157 -QLDKMVTEKAgFKRAFIITGQTYTRKVD-----IEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPY 230
Cdd:cd01598  200 pDVDWRKFSEF-FVTSLGLTWNPYTTQIEphdyiAELFDALARINTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPH 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 231 KRNPMRSERC-------CSLARHL-MTLVMDPLQtasvqwfeRTLDDSANRR---ICLAEAFLTADTILNTLQNISeglv 299
Cdd:cd01598  279 KVNPIDFENAegnlglsNALLNHLsAKLPISRLQ--------RDLTDSTVLRnigVAFGHSLIAYKSLLRGLDKLE---- 346

                        330
                 ....*....|....
gi 961652663 300 vypkVIERRIRQEL 313
Cdd:cd01598  347 ----LNEARLLEDL 356
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 36-266 7.92e-15

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 75.09  E-value: 7.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  36 PKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDL 115
Cdd:PRK05975  96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 116 CMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDKMVTEKAGFKRAFIitgqtytrkVDIEVLs 189
Cdd:PRK05975 176 LRHRDRLEALRADvfpLQFGGAAGTlekLGGKAAAVR-----ARLAKRLGLEDAPQWHSQRDFI---------ADFAHL- 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 190 vLASLGASVHKICTDIRLLAnlkEMEEpfEKQQIG---SSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERT 266
Cdd:PRK05975 241 -LSLVTGSLGKFGQDIALMA---QAGD--EISLSGgggSSAMPHKQNPVAAETLVTLARFNATQV-SGLHQALVHEQERS 313
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 60-234 2.85e-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: 58.69  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  60 LRNALDLLLPKLARVISRLAD--FAKER--ASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 135
Cdd:cd01357  144 LRLALILLLRKLLDALAALQEafQAKARefADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLG 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 136 GT---TGTQASFlqlfEGDDHKVEQLDKMVteKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLA--- 209
Cdd:cd01357  224 GTaigTGINAPP----GYIELVVEKLSEIT--GLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSsgp 297

                        170       180       190
                 ....*....|....*....|....*....|..
gi 961652663 210 -------NLKEMeepfekqQIGSSAMPYKRNP 234
Cdd:cd01357  298 raglgeiNLPAV-------QPGSSIMPGKVNP 322
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 17-247 2.46e-08

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 55.91  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  17 EKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGATScyvGDNTDL---IILRNALD-LLLPKLARVISRLADFAKER 85
Cdd:PRK09285  86 ERTTNHDVKAveyflkeKLAGLPEL-EAVSEFIHFACTS---EDINNLshaLMLKEAREeVLLPALRELIDALKELAHEY 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  86 ASLPTLGFTHFQPAQLTTVGKrcclwiqdlcmDLQN----LKRVRDdlRFRGVK------GTTGTQASFLQLF-EGDDHK 154
Cdd:PRK09285 162 ADVPMLSRTHGQPATPTTLGK-----------EMANvayrLERQLK--QLEAVEilgkinGAVGNYNAHLAAYpEVDWHA 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 155 veqldkmvtekagFKRAFI----ITGQTYTRKV----DI-EVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGS 225
Cdd:PRK09285 229 -------------FSREFVeslgLTWNPYTTQIephdYIaELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGS 295

                        250       260
                 ....*....|....*....|....*....
gi 961652663 226 SAMPYKRNPMRSERC-------CSLARHL 247
Cdd:PRK09285 296 STMPHKVNPIDFENSegnlglaNALLEHL 324
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 60-250 7.36e-08

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 54.39  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  60 LRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQnlkRVRDDLRfRgVK---- 135
Cdd:PRK00855 123 LRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLE---RLRDARK-R-VNrspl 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 136 ------GTTgtqasflqlFEgddhkveqLD-KMVTEKAGFKRAFI--ITGQTyTRKVDIEVLSVLASLGASVHKICTDIR 206
Cdd:PRK00855 198 gsaalaGTT---------FP--------IDrERTAELLGFDGVTEnsLDAVS-DRDFALEFLSAASLLMVHLSRLAEELI 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 207 LLANlkemeepfekQQI-----------GSSAMPYKRNP-----MRSeRCCSLARHLMTL 250
Cdd:PRK00855 260 LWSS----------QEFgfvelpdafstGSSIMPQKKNPdvaelIRG-KTGRVYGNLTGL 308
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 64-234 1.27e-07

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: 53.58  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  64 LDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG- 139
Cdd:cd01596  152 LERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTavgTGl 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 140 -TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTR---KVD--------IEVLSVLASLGASVHKICTDIRL 207
Cdd:cd01596  232 nAPPGYAEKV------AAELAE-------------LTGLPFVTapnLFEataahdalVEVSGALKTLAVSLSKIANDLRL 292

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 961652663 208 LA----------NLKEMeEPfekqqiGSSAMPYKRNP 234
Cdd:cd01596  293 LSsgpraglgeiNLPAN-QP------GSSIMPGKVNP 322
aspA PRK12273
aspartate ammonia-lyase; Provisional
 60-234 1.65e-07

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 53.21  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  60 LRNALDLLLPKLARVISRLAD-F---AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 135
Cdd:PRK12273 151 IRIALLLSLRKLLDALEQLQEaFeakAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLG 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 136 GT---TG--TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 199
Cdd:PRK12273 231 ATaigTGlnAPPGYIELV------VEKLAE-------------ITGLPLVPAEDlieatqdtgafVEVSGALKRLAVKLS 291

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 961652663 200 KICTDIRLL-----ANLKEMEEPfeKQQIGSSAMPYKRNP 234
Cdd:PRK12273 292 KICNDLRLLssgprAGLNEINLP--AVQAGSSIMPGKVNP 329
PLN02848 PLN02848
adenylosuccinate lyase
 5-106 1.99e-07

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 52.82  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663   5 LENI--DFKMA-AEE----EKRLRHDVMAhVHTF--GHCC--PKAAGI---IHLGATSCYVGDNTDLIILRNALD-LLLP 69
Cdd:PLN02848  70 LEGIiaGFSVDdALEvkkiERVTNHDVKA-VEYFlkQKCKshPELAKVlefFHFACTSEDINNLSHALMLKEGVNsVVLP 148

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 961652663  70 KLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGK 106
Cdd:PLN02848 149 TMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGK 185
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
60-234 3.90e-07

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


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 51.98  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  60 LRNALDLLLPKLARVISRLAD-F---AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 135
Cdd:COG1027  146 IRLALLLLLRELLEALERLQEaFaakAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLG 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 136 GT---TG--TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 199
Cdd:COG1027  226 GTaigTGlnAPPGYIELV------VEHLAE-------------ITGLPLVRAENlieatqdtdafVEVSGALKRLAVKLS 286

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 961652663 200 KICTDIRLLA----------NLKEMeepfekqQIGSSAMPYKRNP 234
Cdd:COG1027  287 KICNDLRLLSsgpraglgeiNLPAV-------QPGSSIMPGKVNP 324
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 55-234 1.95e-06

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: 49.85  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  55 TDL-IILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFR- 132
Cdd:cd01359   93 TDLrLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVSp 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 133 -GVKGTTGTqaSFLqlfegddhkveqLD-KMVTEKAGFKRafiITGQTY----TRKVDIEVLSVLASLGASVHKICTDIR 206
Cdd:cd01359  173 lGAGALAGT--TFP------------IDrERTAELLGFDG---PTENSLdavsDRDFVLEFLSAAALLMVHLSRLAEDLI 235

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 961652663 207 LLANlkemeepFEKQQI--------GSSAMPYKRNP 234
Cdd:cd01359  236 LWST-------QEFGFVelpdaystGSSIMPQKKNP 264
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 60-238 1.06e-05

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 47.67  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  60 LRNALDLLLPKLARVISRLADF----AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 135
Cdd:PRK13353 149 IRIAALNLLEGLLAAMGALQDVfeekAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 136 GT---TGTQASflqlfegddhkVEQLDKMVTEKAGfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHKI 201
Cdd:PRK13353 229 GTavgTGLNAD-----------PEYIERVVKHLAA------ITGLPLVGAEDlvdatqntdafVEVSGALKVCAVNLSKI 291

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 961652663 202 CTDIRLLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 238
Cdd:PRK13353 292 ANDLRLLSSgprtgLGEINLP--AVQPGSSIMPGKVNPVMPE 331
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 67-238 1.37e-04

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: 44.03  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  67 LLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG--TQ 141
Cdd:cd01362  156 LLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTavgTGlnAH 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 142 ASFLQL------------FEGDDHKVEQL---DKMVtekagfkrafiitgqtytrkvdiEVLSVLASLGASVHKICTDIR 206
Cdd:cd01362  236 PGFAEKvaaelaeltglpFVTAPNKFEALaahDALV-----------------------EASGALKTLAVSLMKIANDIR 292

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 961652663 207 LLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 238
Cdd:cd01362  293 WLGSgprcgLGELSLP--ENEPGSSIMPGKVNPTQCE 327
fumC PRK00485
fumarate hydratase; Reviewed
 67-238 1.77e-04

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 43.54  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  67 LLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TGTQAs 143
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTavgTGLNA- 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 144 flqlfegddHKveqldkmvtekaGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 207
Cdd:PRK00485 239 ---------HP------------GFAERVAeelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 297

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 961652663 208 LAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 238
Cdd:PRK00485 298 LASgprcgLGEISLP--ENEPGSSIMPGKVNPTQCE 331
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 62-238 1.43e-03

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 40.75  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663  62 NALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---T 138
Cdd:PRK14515 161 NALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATavgT 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961652663 139 GTQAsflqlfegDDHKVEQLDKMVTEKAGF--KRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN-----L 211
Cdd:PRK14515 241 GLNA--------DPEYIEAVVKHLAAISELplVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASgprvgL 312

                        170       180
                 ....*....|....*....|....*..
gi 961652663 212 KEMEEPfeKQQIGSSAMPYKRNPMRSE 238
Cdd:PRK14515 313 AEIMLP--ARQPGSSIMPGKVNPVMPE 337
 
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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