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Conserved domains on  [gi|183227688|ref|NP_001116850|]
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adenylosuccinate lyase isoform b [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 ...
 17-397 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: 788.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 177 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302  241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183227688 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQ 381
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 17-397 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: 788.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 177 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302  241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183227688 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQ 381
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 17-397 6.87e-147

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: 424.50  E-value: 6.87e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015    2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:COG0015   81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 174 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDKMVTEKAGFKRAFiITGQTYTRKVDIEVLS 253
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNP-VTTQIEPRDRHAELFS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 254 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 331
Cdd:COG0015  233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183227688 332 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:COG0015  312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGRE 377
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 17-421 1.66e-135

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: 395.56  E-value: 1.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  176 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFegddhkvEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  256 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDD 333
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRqvqrfleEEVYPLLKpy 413
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGR-------EEAYEIVR-- 382


                  ....*...
gi 183227688  414 ESVMKVKA 421
Cdd:TIGR00928 383 ELAMGAAE 390
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 248-397 8.63e-60

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 194.09  E-value: 8.63e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 248 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 325
Cdd:PRK08937  17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183227688 326 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:PRK08937  95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGRE 166
Lyase_1 pfam00206
Lyase;
22-302 9.97e-23

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 97.82  E-value: 9.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   22 ASPEMCFVFSDR--YKFRTWRQLWLW---LAEAEQTLGLPIT----------DEQIQEMKSNLENI----------DFKM 76
Cdd:pfam00206   6 PADALMGIFTDRsrFNFRLGEEDIKGlaaLKKAAAKANVILKeeaaaiikalDEVAEEGKLDDQFPlkvwqegsgtAVNM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   77 AAEEekRLRHDVMAHVHTFGHccpkaagiIHLGATScyvGD--NTDL-IILRNAL-DLLLPKLARVISRLADFAKERASL 152
Cdd:pfam00206  86 NLNE--VIGELLGQLVHPNDH--------VHTGQSS---NDqvPTALrLALKDALsEVLLPALRQLIDALKEKAKEFADI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  153 PTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMvtEKAGF 232
Cdd:pfam00206 153 VKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--TGLPV 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183227688  233 KRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 302
Cdd:pfam00206 231 KAPNSFE-ATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 17-397 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: 788.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 177 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302  241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183227688 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQ 381
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 26-397 5.19e-168

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: 476.23  E-value: 5.19e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  26 MCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHTFGHCCPK-A 102
Cdd:cd01595    1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADVfeIDAERIAEIEKETGHDVIAFVYALAEKCGEdA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 103 AGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMD 182
Cdd:cd01595   80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 183 LQNLKRVRDDLRFRGVKGTTGTQASFLQlfegddhKVEQLDKMVTEKAGFKrAFIITGQTYTRKVDIEVLSVLASLGASV 262
Cdd:cd01595  160 LERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEERVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 263 HKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDDSANRRIC 340
Cdd:cd01595  232 EKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDSSVERNI 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 183227688 341 LAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:cd01595  311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQ 367
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 17-397 6.87e-147

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: 424.50  E-value: 6.87e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015    2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:COG0015   81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 174 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDKMVTEKAGFKRAFiITGQTYTRKVDIEVLS 253
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNP-VTTQIEPRDRHAELFS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 254 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 331
Cdd:COG0015  233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183227688 332 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:COG0015  312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGRE 377
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 17-421 1.66e-135

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: 395.56  E-value: 1.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  176 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFegddhkvEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  256 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDD 333
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRqvqrfleEEVYPLLKpy 413
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGR-------EEAYEIVR-- 382


                  ....*...
gi 183227688  414 ESVMKVKA 421
Cdd:TIGR00928 383 ELAMGAAE 390
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 36-365 6.13e-99

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: 298.26  E-value: 6.13e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  36 FRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLENIDFKMAA---EEEKRLRHDVMAHVHTFGHCCPKA-AGIIHLGAT 111
Cdd:cd01334    1 IRADLQVEKAHAKALAELGL-LPKEAAEAILAALDEILEGIAAdqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 112 SCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRD 191
Cdd:cd01334   80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 192 DLRFRGVKGTT-GTQASFlqlfegddhkVEQLDKMVTEKAGFKRAFIITGQ-TYTRKVDIEVLSVLASLGASVHKICTDI 269
Cdd:cd01334  160 RLNVLPLGGGAvGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 270 RLLAN--LKEMEEPFEKQqIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASvQWFERTLDDSANRRICLAEAFLT 347
Cdd:cd01334  230 RLLSSgeFGEVELPDAKQ-PGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDL 307

                        330
                 ....*....|....*...
gi 183227688 348 ADTILNTLQNISEGLVVY 365
Cdd:cd01334  308 LDAALRLLTGVLEGLEVN 325
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 20-400 1.60e-73

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: 235.14  E-value: 1.60e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  20 RYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQE----MKSNLENIDfkmaaEEEKRLRHDVMAHVHTF 95
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGV-IPAEAAEEirkkAKFDVERVK-----EIEAETKHDVIAFVTAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:cd01360   75 AEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 176 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfegdDHKVEqldKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:cd01360  155 YAEFKRHLERLKEARERILVGKISGAVGTYANL-------GPEVE---ERVAEKLGLKPEPIST-QVIQRDRHAEYLSTL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 256 ASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERTLDD 333
Cdd:cd01360  224 ALIASTLEKIATEIRHLqrTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNV-IPALENVALWHERDISH 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183227688 334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ-----VQR 400
Cdd:cd01360  303 SSVERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREeayeiVQR 374
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 248-397 8.63e-60

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 194.09  E-value: 8.63e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 248 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 325
Cdd:PRK08937  17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183227688 326 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQ 397
Cdd:PRK08937  95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGRE 166
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 96-356 7.55e-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: 152.76  E-value: 7.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  96 GHCCPKAAGII-----HLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGK 170
Cdd:cd01594   22 GRAGELAGGLHgsalvHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGY 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 171 RCCLWIQDLCMDLQNLKRVRDdlrfrgvkgttgtqasflqlfegddhkveqldkmvtekagfkrafiitgqtytrkvdIE 250
Cdd:cd01594  102 ELRAWAQVLGRDLERLEEAAV---------------------------------------------------------AE 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 251 VLSVLASLGASVHKICTDIRLLANLKEME--EPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLqTASVQWFE 328
Cdd:cd01594  125 ALDALALAAAHLSKIAEDLRLLLSGEFGElgEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVL-TALKGGPE 203

                        250       260
                 ....*....|....*....|....*...
gi 183227688 329 RTLDDSANRRICLAEAFLTADTILNTLQ 356
Cdd:cd01594  204 RDNEDSPSMREILADSLLLLIDALRLLL 231
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 17-404 5.26e-43

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: 156.25  E-value: 5.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL--PITDEQIQEmKSNLENIDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:cd01597    2 LGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVipKEAAAEIAA-AADVERLDLEALAEATARTGHPAIPLVKQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:cd01597   81 LTAACGDAAGeYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 174 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfeGDDhkveqldKMVTEKAGFKR----AFIITGQTyTRKVDI 249
Cdd:cd01597  161 VWLSELLRHRERLDELRPRVLVVQFGGAAGTLASL-----GDQ-------GLAVQEALAAElglgVPAIPWHT-ARDRIA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 250 EVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLAR---HLMTLVMDplqtASV 324
Cdd:cd01597  228 ELASFLALLTGTLGKIARDVYLLmqTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARrvpGLAALLLD----AMV 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 325 QWFERtlDDSANR--RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQVQRFL 402
Cdd:cd01597  304 QEHER--DAGAWHaeWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLGRQEAHDLV 381


                 ..
gi 183227688 403 EE 404
Cdd:cd01597  382 YE 383
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 17-331 4.62e-27

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: 110.61  E-value: 4.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   17 LASRYAS-PEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLENIDFKMAAEEE-------------K 82
Cdd:TIGR02426   1 LLDGLFGdPAALELFSDRAFLRAMLDFEAALARAQADAGL-IPAEAAAAIEAACAAAAPDLEALAHaaatagnpviplvK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   83 RLRHDVMAhvhtfghccpKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQP 162
Cdd:TIGR02426  80 ALRKAVAG----------EAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  163 AQLTTVGKRCCLWIQDLCMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDkMVTEKAGF--KR 234
Cdd:TIGR02426 150 AVPTTFGLKAAGWLAAVLRARDRLAALRTRalpLQFGGAAGTlaaLGTRGGAVA-----AALAARLG-LPLPALPWhtQR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  235 AFIItgqtytrkvdiEVLSVLASLGASVHKICTDIRLLANLkEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTL 314
Cdd:TIGR02426 224 DRIA-----------EFGSALALVAGALGKIAGDIALLSQT-EVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGL 291

                         330
                  ....*....|....*..
gi 183227688  315 VMdPLQTASVQWFERTL 331
Cdd:TIGR02426 292 AA-TLHAALPQEHERSL 307
Lyase_1 pfam00206
Lyase;
22-302 9.97e-23

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 97.82  E-value: 9.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   22 ASPEMCFVFSDR--YKFRTWRQLWLW---LAEAEQTLGLPIT----------DEQIQEMKSNLENI----------DFKM 76
Cdd:pfam00206   6 PADALMGIFTDRsrFNFRLGEEDIKGlaaLKKAAAKANVILKeeaaaiikalDEVAEEGKLDDQFPlkvwqegsgtAVNM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688   77 AAEEekRLRHDVMAHVHTFGHccpkaagiIHLGATScyvGD--NTDL-IILRNAL-DLLLPKLARVISRLADFAKERASL 152
Cdd:pfam00206  86 NLNE--VIGELLGQLVHPNDH--------VHTGQSS---NDqvPTALrLALKDALsEVLLPALRQLIDALKEKAKEFADI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  153 PTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMvtEKAGF 232
Cdd:pfam00206 153 VKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--TGLPV 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183227688  233 KRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 302
Cdd:pfam00206 231 KAPNSFE-ATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 43-377 4.00e-19

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: 88.83  E-value: 4.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMA---AEEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:cd01598   21 WLiALSNLEEIPEVPpLTKEELKFLRAIIENFSEEDAlriKEIEATTNHDVKAveyflkeKFETLGLL-KKIKEFIHFAC 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 111 TScyvGDNTDLII---LRNAL-DLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNL 186
Cdd:cd01598  100 TS---EDINNLAYalmIKEARnEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 187 KRVRDDLRFrgvKGTTGTQASflqlfegddHKVE--QLDKMVTEKAgFKRAFIITGQTYTRKVD-----IEVLSVLASLG 259
Cdd:cd01598  177 KQIEILGKF---NGAVGNFNA---------HLVAypDVDWRKFSEF-FVTSLGLTWNPYTTQIEphdyiAELFDALARIN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 260 ASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHL-MTLVMDPLQtasvqwfeRTL 331
Cdd:cd01598  244 TILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAegnlglsNALLNHLsAKLPISRLQ--------RDL 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 183227688 332 DDSANRR---ICLAEAFLTADTILNTLQNISeglvvypkVIERRIRQEL 377
Cdd:cd01598  316 TDSTVLRnigVAFGHSLIAYKSLLRGLDKLE--------LNEARLLEDL 356
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 15-298 3.09e-15

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


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 77.36  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  15 SPLASRY-ASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEE----------- 81
Cdd:PRK09053   5 ARLTDLYfGSPAMRAIFSDRATVQRMLDFEAALARAEAACGViPAAAVAPIEAACDAERLDLDALAQAAalagnlaiplv 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  82 KRLRHDVMAHVhtfghccPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQ 161
Cdd:PRK09053  85 KQLTAQVAARD-------AEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 162 PAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASF----------------LQLFEGDDHKveQLDKM 225
Cdd:PRK09053 158 QALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqalpvaqalaaelqLALPALPWHT--QRDRI 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183227688 226 VtekagfkrafiitgqtytrkvdiEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNP 298
Cdd:PRK09053 236 A-----------------------EFASALGLLAGTLGKIARDVSLLmqTEVGEVFEPAAAGKGGSSTMPHKRNP 287
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 100-330 1.20e-14

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 74.71  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 100 PKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDL 179
Cdd:PRK05975  96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 180 CMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDKMVTEKAGFKRAFIitgqtytrkVDIEVLs 253
Cdd:PRK05975 176 LRHRDRLEALRADvfpLQFGGAAGTlekLGGKAAAVR-----ARLAKRLGLEDAPQWHSQRDFI---------ADFAHL- 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 254 vLASLGASVHKICTDIRLLAnlkEMEEpfEKQQIG---SSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERT 330
Cdd:PRK05975 241 -LSLVTGSLGKFGQDIALMA---QAGD--EISLSGgggSSAMPHKQNPVAAETLVTLARFNATQV-SGLHQALVHEQERS 313
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 43-311 1.91e-10

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 62.46  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMAA---EEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:PRK09285  43 WLiALAAHPGIPEVPpFSAEANAFLRAIVENFSEEDAArikEIERTTNHDVKAveyflkeKLAGLPEL-EAVSEFIHFAC 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 111 TScyvGDNTDL---IILRNALD-LLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKrcclwiqdlcmDLQN- 185
Cdd:PRK09285 122 TS---EDINNLshaLMLKEAREeVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGK-----------EMANv 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 186 ---LKRVRDdlRFRGVK------GTTGTQASFLQLF-EGDDHKveqldkmvtekagFKRAFI----ITGQTYTRKV---- 247
Cdd:PRK09285 188 ayrLERQLK--QLEAVEilgkinGAVGNYNAHLAAYpEVDWHA-------------FSREFVeslgLTWNPYTTQIephd 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183227688 248 DI-EVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHL 311
Cdd:PRK09285 253 YIaELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGSSTMPHKVNPIDFENSegnlglaNALLEHL 324
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 124-298 2.03e-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: 59.07  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 124 LRNALDLLLPKLARVISRLAD--FAKER--ASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:cd01357  144 LRLALILLLRKLLDALAALQEafQAKARefADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLG 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 200 GT---TGTQASFlqlfEGDDHKVEQLDKMVteKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLA--- 273
Cdd:cd01357  224 GTaigTGINAPP----GYIELVVEKLSEIT--GLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSsgp 297

                        170       180       190
                 ....*....|....*....|....*....|..
gi 183227688 274 -------NLKEMeepfekqQIGSSAMPYKRNP 298
Cdd:cd01357  298 raglgeiNLPAV-------QPGSSIMPGKVNP 322
PLN02848 PLN02848
adenylosuccinate lyase
 15-170 4.84e-08

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 54.74  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  15 SPLASRYAS--PEMCFVFSD----RYKFRTWRQLWLWLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMAAEE---EKRL 84
Cdd:PLN02848  13 SPLDGRYWSkvKDLRPIFSEfgliRYRVLVEVKWLLKLSQIPEVTEVPpFSDEANSFLEGIIAGFSVDDALEVkkiERVT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688  85 RHDVMAhVHTF--GHCC--PKAAGI---IHLGATSCYVGDNTDLIILRNALD-LLLPKLARVISRLADFAKERASLPTLG 156
Cdd:PLN02848  93 NHDVKA-VEYFlkQKCKshPELAKVlefFHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHEFAYVPMLS 171

                        170
                 ....*....|....
gi 183227688 157 FTHFQPAQLTTVGK 170
Cdd:PLN02848 172 RTHGQPASPTTLGK 185
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 124-314 6.90e-08

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 54.39  E-value: 6.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 124 LRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQnlkRVRDDLRfRgVK---- 199
Cdd:PRK00855 123 LRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLE---RLRDARK-R-VNrspl 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 200 ------GTTgtqasflqlFEgddhkveqLD-KMVTEKAGFKRAFI--ITGQTyTRKVDIEVLSVLASLGASVHKICTDIR 270
Cdd:PRK00855 198 gsaalaGTT---------FP--------IDrERTAELLGFDGVTEnsLDAVS-DRDFALEFLSAASLLMVHLSRLAEELI 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 271 LLANlkemeepfekQQI-----------GSSAMPYKRNP-----MRSeRCCSLARHLMTL 314
Cdd:PRK00855 260 LWSS----------QEFgfvelpdafstGSSIMPQKKNPdvaelIRG-KTGRVYGNLTGL 308
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 128-298 8.09e-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: 53.97  E-value: 8.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 128 LDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG- 203
Cdd:cd01596  152 LERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTavgTGl 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 204 -TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTR---KVD--------IEVLSVLASLGASVHKICTDIRL 271
Cdd:cd01596  232 nAPPGYAEKV------AAELAE-------------LTGLPFVTapnLFEataahdalVEVSGALKTLAVSLSKIANDLRL 292

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 183227688 272 LA----------NLKEMeEPfekqqiGSSAMPYKRNP 298
Cdd:cd01596  293 LSsgpraglgeiNLPAN-QP------GSSIMPGKVNP 322
aspA PRK12273
aspartate ammonia-lyase; Provisional
 124-298 1.14e-07

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 53.59  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 124 LRNALDLLLPKLARVISRLAD-F---AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:PRK12273 151 IRIALLLSLRKLLDALEQLQEaFeakAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLG 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 200 GT---TG--TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 263
Cdd:PRK12273 231 ATaigTGlnAPPGYIELV------VEKLAE-------------ITGLPLVPAEDlieatqdtgafVEVSGALKRLAVKLS 291

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 183227688 264 KICTDIRLL-----ANLKEMEEPfeKQQIGSSAMPYKRNP 298
Cdd:PRK12273 292 KICNDLRLLssgprAGLNEINLP--AVQAGSSIMPGKVNP 329
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
124-298 2.70e-07

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


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 52.36  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 124 LRNALDLLLPKLARVISRLAD-F---AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:COG1027  146 IRLALLLLLRELLEALERLQEaFaakAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLG 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 200 GT---TG--TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 263
Cdd:COG1027  226 GTaigTGlnAPPGYIELV------VEHLAE-------------ITGLPLVRAENlieatqdtdafVEVSGALKRLAVKLS 286

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 183227688 264 KICTDIRLLA----------NLKEMeepfekqQIGSSAMPYKRNP 298
Cdd:COG1027  287 KICNDLRLLSsgpraglgeiNLPAV-------QPGSSIMPGKVNP 324
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 119-298 1.97e-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: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 119 TDL-IILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFR- 196
Cdd:cd01359   93 TDLrLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVSp 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 197 -GVKGTTGTqaSFLqlfegddhkveqLD-KMVTEKAGFKRafiITGQTY----TRKVDIEVLSVLASLGASVHKICTDIR 270
Cdd:cd01359  173 lGAGALAGT--TFP------------IDrERTAELLGFDG---PTENSLdavsDRDFVLEFLSAAALLMVHLSRLAEDLI 235

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 183227688 271 LLANlkemeepFEKQQI--------GSSAMPYKRNP 298
Cdd:cd01359  236 LWST-------QEFGFVelpdaystGSSIMPQKKNP 264
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 124-302 7.09e-06

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 48.06  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 124 LRNALDLLLPKLARVISRLADF----AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:PRK13353 149 IRIAALNLLEGLLAAMGALQDVfeekAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 200 GT---TGTQASflqlfegddhkVEQLDKMVTEKAGfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHKI 265
Cdd:PRK13353 229 GTavgTGLNAD-----------PEYIERVVKHLAA------ITGLPLVGAEDlvdatqntdafVEVSGALKVCAVNLSKI 291

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 183227688 266 CTDIRLLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:PRK13353 292 ANDLRLLSSgprtgLGEINLP--AVQPGSSIMPGKVNPVMPE 331
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 131-302 1.07e-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: 44.41  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 131 LLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG--TQ 205
Cdd:cd01362  156 LLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTavgTGlnAH 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 206 ASFLQL------------FEGDDHKVEQL---DKMVtekagfkrafiitgqtytrkvdiEVLSVLASLGASVHKICTDIR 270
Cdd:cd01362  236 PGFAEKvaaelaeltglpFVTAPNKFEALaahDALV-----------------------EASGALKTLAVSLMKIANDIR 292

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 183227688 271 LLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:cd01362  293 WLGSgprcgLGELSLP--ENEPGSSIMPGKVNPTQCE 327
fumC PRK00485
fumarate hydratase; Reviewed
 131-302 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 183227688 131 LLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TGTQAs 207
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTavgTGLNA- 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 208 flqlfegddHKveqldkmvtekaGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 271
Cdd:PRK00485 239 ---------HP------------GFAERVAeelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 297

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 183227688 272 LAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:PRK00485 298 LASgprcgLGEISLP--ENEPGSSIMPGKVNPTQCE 331
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 126-302 1.45e-03

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 40.75  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 126 NALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---T 202
Cdd:PRK14515 161 NALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATavgT 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183227688 203 GTQAsflqlfegDDHKVEQLDKMVTEKAGF--KRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN-----L 275
Cdd:PRK14515 241 GLNA--------DPEYIEAVVKHLAAISELplVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASgprvgL 312

                        170       180
                 ....*....|....*....|....*..
gi 183227688 276 KEMEEPfeKQQIGSSAMPYKRNPMRSE 302
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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