|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
17-452 |
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: 881.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLNNIDFQMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 177 QDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLFEGDHQKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKQ 416
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 29788764 417 EGGDNDLIERIRADAYFSPIHSQLEHLLDPSSFTGR 452
Cdd:cd03302 401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
17-460 |
5.56e-163 |
|
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: 468.02 E-value: 5.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLNN--IDFQMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:COG0015 81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 174 LWIQDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLfegdhqkVEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLS 253
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNPVTT-QIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 254 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALtMDPLQTASVQWFERTL 331
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARAL-AAALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 332 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 411
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 29788764 412 AvvkqegGDNDLIERIRADAYFSPIHS--QLEHLLDPSSFTGRAPQQVHRF 460
Cdd:COG0015 392 E------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
17-460 |
2.05e-150 |
|
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: 436.01 E-value: 2.05e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLNNIDFQMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 176 IQDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLFegdhqkvEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 256 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTAsVQWFERTLDD 333
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAV 413
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 29788764 414 vkqegGDNDLIERIRADAYFSPIHSQLE--HLLDPSSFTGRAPQQVHRF 460
Cdd:TIGR00928 392 -----DEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
248-451 |
1.72e-72 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 228.37 E-value: 1.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 248 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTAsVQ 325
Cdd:PRK08937 17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 326 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 405
Cdd:PRK08937 95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29788764 406 LSQQAAAVVkqeggdNDLIERIRADAYFSPIHSQ--LEHLLDPSSFTG 451
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
378-460 |
9.77e-26 |
|
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: 99.80 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 378 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAAAVVKqeggdNDLIERIRADAYFS-PIHSQLEHLLDPSSFTGRAPQQ 456
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 29788764 457 VHRF 460
Cdd:pfam10397 75 VDRV 78
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
377-461 |
5.37e-21 |
|
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: 86.73 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 377 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKqeggdnDLIERIRADAYFSPIHS--QLEHLLDPSSFTGRAP 454
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74
|
....*..
gi 29788764 455 QQVHRFL 461
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 ... |
17-452 |
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: 881.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLNNIDFQMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 177 QDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLFEGDHQKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKQ 416
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 29788764 417 EGGDNDLIERIRADAYFSPIHSQLEHLLDPSSFTGR 452
Cdd:cd03302 401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
26-405 |
1.54e-170 |
|
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: 485.09 E-value: 1.54e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 26 MCFLFSDRYKFQTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLNN--IDFQMAAEEEKRLRHDVMAHVHTFGHCCPK-A 102
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADVfeIDAERIAEIEKETGHDVIAFVYALAEKCGEdA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 103 AGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMD 182
Cdd:cd01595 80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 183 LQNLKRVRDELRFRGVKGTTGTQASFLqlfegdhQKVEQLDKMVTEKAGFKrAFIITGQTYTRKVDIEVLSVLASLGASV 262
Cdd:cd01595 160 LERLEEARERVLVGGISGAVGTHASLG-------PKGPEVEERVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 263 HKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTAsVQWFERTLDDSANRRIC 340
Cdd:cd01595 232 EKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDSSVERNI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29788764 341 LAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 405
Cdd:cd01595 311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
17-460 |
5.56e-163 |
|
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: 468.02 E-value: 5.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLNN--IDFQMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:COG0015 81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 174 LWIQDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLfegdhqkVEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLS 253
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNPVTT-QIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 254 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALtMDPLQTASVQWFERTL 331
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARAL-AAALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 332 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 411
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 29788764 412 AvvkqegGDNDLIERIRADAYFSPIHS--QLEHLLDPSSFTGRAPQQVHRF 460
Cdd:COG0015 392 E------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
17-460 |
2.05e-150 |
|
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: 436.01 E-value: 2.05e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLNNIDFQMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 176 IQDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLFegdhqkvEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 256 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTAsVQWFERTLDD 333
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAV 413
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 29788764 414 vkqegGDNDLIERIRADAYFSPIHSQLE--HLLDPSSFTGRAPQQVHRF 460
Cdd:TIGR00928 392 -----DEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
36-365 |
3.52e-96 |
|
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: 293.25 E-value: 3.52e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 36 FQTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLNNIDFQMAA---EEEKRLRHDVMAHVHTFGHCCPKA-AGIIHLGAT 111
Cdd:cd01334 1 IRADLQVEKAHAKALAELGL-LPKEAAEAILAALDEILEGIAAdqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 112 SCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRD 191
Cdd:cd01334 80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 192 ELRFRGVKGTT-GTQASFlqlfegdhqkVEQLDKMVTEKAGFKRAFIITGQ-TYTRKVDIEVLSVLASLGASVHKICTDI 269
Cdd:cd01334 160 RLNVLPLGGGAvGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 270 RLLAN--LKEMEEPFEKQqIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTASvQWFERTLDDSANRRICLAEAFLT 347
Cdd:cd01334 230 RLLSSgeFGEVELPDAKQ-PGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDL 307
|
330
....*....|....*...
gi 29788764 348 ADTILNTLQNISEGLVVY 365
Cdd:cd01334 308 LDAALRLLTGVLEGLEVN 325
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
20-404 |
6.98e-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: 235.52 E-value: 6.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 20 RYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLNnIDFQMAAEEEKRLRHDVMAHVHTFGHCC 99
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGV-IPAEAAEEIRKKAK-FDVERVKEIEAETKHDVIAFVTAIAEYC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 100 PKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDL 179
Cdd:cd01360 79 GEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 180 CMDLQNLKRVRDELRFRGVKGTTGTQASFlqlfegdHQKVEqldKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVLASLG 259
Cdd:cd01360 159 KRHLERLKEARERILVGKISGAVGTYANL-------GPEVE---ERVAEKLGLKPEPIST-QVIQRDRHAEYLSTLALIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 260 ASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTmDPLQTASVQWFERTLDDSANR 337
Cdd:cd01360 228 STLEKIATEIRHLqrTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNV-IPALENVALWHERDISHSSVE 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29788764 338 RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIR 404
Cdd:cd01360 307 RVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQ 373
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
248-451 |
1.72e-72 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 228.37 E-value: 1.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 248 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTAsVQ 325
Cdd:PRK08937 17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 326 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 405
Cdd:PRK08937 95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29788764 406 LSQQAAAVVkqeggdNDLIERIRADAYFSPIHSQ--LEHLLDPSSFTG 451
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
21-463 |
1.04e-53 |
|
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: 186.30 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 21 YASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGL--PITDEQIQEmKSNLNNIDFQMAAEEEKRLRHDVMAHVHTFGHC 98
Cdd:cd01597 6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVipKEAAAEIAA-AADVERLDLEALAEATARTGHPAIPLVKQLTAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 99 CPKAAG-IIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQ 177
Cdd:cd01597 85 CGDAAGeYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 178 DLCMDLQNLKRVRDELRFRGVKGTTGTQASFlqlfeGDHqkveqldKMVTEKAGFKR----AFIITGQTyTRKVDIEVLS 253
Cdd:cd01597 165 ELLRHRERLDELRPRVLVVQFGGAAGTLASL-----GDQ-------GLAVQEALAAElglgVPAIPWHT-ARDRIAELAS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 254 VLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLAR---HLMALTMDplqtASVQWFE 328
Cdd:cd01597 232 FLALLTGTLGKIARDVYLLmqTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARrvpGLAALLLD----AMVQEHE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 329 RtlDDSANR--RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGsRQDCHEKIRVL 406
Cdd:cd01597 308 R--DAGAWHaeWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLG-RQEAHDLVYEA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29788764 407 SQQAAAvvkqEGGdnDLIERIRAD----AYFSPihSQLEHLLDPSSFTGRAPQQVHRFLEE 463
Cdd:cd01597 385 CMRAVE----EGR--PLREVLLEDpevaAYLSD--EELDALLDPANYLGSAPALVDRVLAR 437
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
106-356 |
1.93e-42 |
|
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: 150.45 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 106 IHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQN 185
Cdd:cd01594 37 VHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVLGRDLER 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 186 LKRVRDelrfrgvkgttgtqasflqlfegdhqkveqldkmvtekagfkrafiitgqtytrkvdIEVLSVLASLGASVHKI 265
Cdd:cd01594 117 LEEAAV---------------------------------------------------------AEALDALALAAAHLSKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 266 CTDIRLLANLKEME--EPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLqTASVQWFERTLDDSANRRICLAE 343
Cdd:cd01594 140 AEDLRLLLSGEFGElgEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVL-TALKGGPERDNEDSPSMREILAD 218
|
250
....*....|...
gi 29788764 344 AFLTADTILNTLQ 356
Cdd:cd01594 219 SLLLLIDALRLLL 231
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
378-460 |
9.77e-26 |
|
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: 99.80 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 378 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAAAVVKqeggdNDLIERIRADAYFS-PIHSQLEHLLDPSSFTGRAPQQ 456
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 29788764 457 VHRF 460
Cdd:pfam10397 75 VDRV 78
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
101-331 |
2.66e-25 |
|
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: 106.37 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 101 KAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLC 180
Cdd:TIGR02426 88 EAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAAVL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 181 MDLQNLKRVRD---ELRFRGVKGT---TGTQASFLQlfegdhQKVEQLDKMVTEKAGF--KRAFIItgqtytrkvdiEVL 252
Cdd:TIGR02426 168 RARDRLAALRTralPLQFGGAAGTlaaLGTRGGAVA------AALAARLGLPLPALPWhtQRDRIA-----------EFG 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29788764 253 SVLASLGASVHKICTDIRLLANLkEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALtMDPLQTASVQWFERTL 331
Cdd:TIGR02426 231 SALALVAGALGKIAGDIALLSQT-EVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGL-AATLHAALPQEHERSL 307
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
106-302 |
4.90e-21 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 93.59 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 106 IHLGATScyvGD--NTDL-IILRNA-FDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCM 181
Cdd:pfam00206 105 VHTGQSS---NDqvPTALrLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 182 DLQNLKRVRDELRFRGVKGTTGTQASFLQLFEGDHQKVEQLDKMvtEKAGFKRAFIITgQTYTRKVDIEVLSVLASLGAS 261
Cdd:pfam00206 182 DRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--TGLPVKAPNSFE-ATSDRDAVVELSGALALLATS 258
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29788764 262 VHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 302
Cdd:pfam00206 259 LSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
377-461 |
5.37e-21 |
|
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: 86.73 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 377 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKqeggdnDLIERIRADAYFSPIHS--QLEHLLDPSSFTGRAP 454
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74
|
....*..
gi 29788764 455 QQVHRFL 461
Cdd:smart00998 75 AIVDRVL 81
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
43-377 |
3.69e-18 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 86.52 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLNNI---DFQMAAEEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:cd01598 21 WLiALSNLEEIPEVPpLTKEELKFLRAIIENFseeDALRIKEIEATTNHDVKAveyflkeKFETLGLL-KKIKEFIHFAC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 111 TScyvGDNTDLII---LRNAF-DLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNL 186
Cdd:cd01598 100 TS---EDINNLAYalmIKEARnEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 187 KRVRDELRFrgvKGTTGTqasflqlFEGDHQKVEQLDKMVTEKAgFKRAFIITGQTYTRKVD-----IEVLSVLASLGAS 261
Cdd:cd01598 177 KQIEILGKF---NGAVGN-------FNAHLVAYPDVDWRKFSEF-FVTSLGLTWNPYTTQIEphdyiAELFDALARINTI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 262 VHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHLMA-LTMDPLQtasvqwfeRTLDD 333
Cdd:cd01598 246 LIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAegnlglsNALLNHLSAkLPISRLQ--------RDLTD 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 29788764 334 SANRR---ICLAEAFLTADTILNTLQNISeglvvypkVIERRIRQEL 377
Cdd:cd01598 318 STVLRnigVAFGHSLIAYKSLLRGLDKLE--------LNEARLLEDL 356
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
17-463 |
3.17e-17 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 83.91 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 17 LAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLNNIDFQMAAEEE-----------KRL 84
Cdd:PRK09053 8 TDLYFGSPAMRAIFSDRATVQRMLDFEAALARAEAACGViPAAAVAPIEAACDAERLDLDALAQAAalagnlaiplvKQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 85 RHDVMAHVhtfghccPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQ 164
Cdd:PRK09053 88 TAQVAARD-------AEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 165 LTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVKGTTGTQASFlqlfeGDHQKVeqldkmVTEKAGFKRAFIITGQTYT 244
Cdd:PRK09053 161 PVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASL-----GEQALP------VAQALAAELQLALPALPWH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 245 RKVD--IEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMrserccSLARHLMALTMDP-- 318
Cdd:PRK09053 230 TQRDriAEFASALGLLAGTLGKIARDVSLLmqTEVGEVFEPAAAGKGGSSTMPHKRNPV------GCAAVLTAATRAPgl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 319 ---LQTASVQWFERTLD------DSANRRICLAEAFLTAdtilntLQNISEGLVVYPKvierRIRQELPfmATENIIMA- 388
Cdd:PRK09053 304 vatLFAAMPQEHERALGgwhaewDTLPELACLAAGALAQ------MAQIVEGLEVDAA----RMRANLD--LTHGLILAe 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 389 --MVKAGGS--RQDCHEKIRVLSQQAAAvvkqEGgdNDLIERIRADAYFSPI--HSQLEHLLDPSSFTGRAPQQVHRFLE 462
Cdd:PRK09053 372 avMLALADRigRLDAHHLVEQASKRAVA----EG--RHLRDVLAEDPQVSAHlsPAALDRLLDPAHYLGQAHAWVDRVLA 445
|
.
gi 29788764 463 E 463
Cdd:PRK09053 446 E 446
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-330 |
2.71e-13 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 70.85 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 100 PKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDL 179
Cdd:PRK05975 96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 180 CMDLQNLKRVRDE---LRFRGVKGTtgtqasfLQLFEGDHQKV-----EQLDKMVTEKAGFKRAFIitgqtytrkVDIEV 251
Cdd:PRK05975 176 LRHRDRLEALRADvfpLQFGGAAGT-------LEKLGGKAAAVrarlaKRLGLEDAPQWHSQRDFI---------ADFAH 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 252 LsvLASLGASVHKICTDIRLLAnlkEMEEpfEKQQIG---SSAMPYKRNPMRSERCCSLARhLMALTMDPLQTASVQWFE 328
Cdd:PRK05975 240 L--LSLVTGSLGKFGQDIALMA---QAGD--EISLSGgggSSAMPHKQNPVAAETLVTLAR-FNATQVSGLHQALVHEQE 311
|
..
gi 29788764 329 RT 330
Cdd:PRK05975 312 RS 313
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
15-311 |
9.83e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 60.54 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 15 SPLAARYAS-----REmcfLFSD----RYKFQ---TWRQlwlWLAEAEQTLGLP-ITDEQIQEMKS---NLNNIDFQMAA 78
Cdd:PRK09285 10 SPLDGRYASktaalRP---IFSEfgliRYRVQvevEWLI---ALAAHPGIPEVPpFSAEANAFLRAiveNFSEEDAARIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 79 EEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGATScyvGDNTDL---IILRNAFD-LLLPKLARVISRLADFAK 147
Cdd:PRK09285 84 EIERTTNHDVKAveyflkeKLAGLPEL-EAVSEFIHFACTS---EDINNLshaLMLKEAREeVLLPALRELIDALKELAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 148 DRADLPTLGFTHFQPAQLTTVGKrcclwiqdlcmDLQN----LKRVRDelRFRGVK------GTTGTQASFLQLF-EGDH 216
Cdd:PRK09285 160 EYADVPMLSRTHGQPATPTTLGK-----------EMANvayrLERQLK--QLEAVEilgkinGAVGNYNAHLAAYpEVDW 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 217 QKveqldkmvtekagFKRAFI----ITGQTYTRKV----DI-EVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQI 287
Cdd:PRK09285 227 HA-------------FSREFVeslgLTWNPYTTQIephdYIaELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEI 293
|
330 340 350
....*....|....*....|....*....|.
gi 29788764 288 GSSAMPYKRNPMRSERC-------CSLARHL 311
Cdd:PRK09285 294 GSSTMPHKVNPIDFENSegnlglaNALLEHL 324
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
15-334 |
1.07e-08 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 57.44 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 15 SPLAARYAS--REMCFLFSD----RYKFQTWRQLWLWLAEAEQTLGLP-ITDEQIQEMKSNLNNIDFQMAAEE---EKRL 84
Cdd:PLN02848 13 SPLDGRYWSkvKDLRPIFSEfgliRYRVLVEVKWLLKLSQIPEVTEVPpFSDEANSFLEGIIAGFSVDDALEVkkiERVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 85 RHDVMAhVHTF--GHCC--PKAAGI---IHLGATSCYVGDNTDLIILRNAFD-LLLPKLARVISRLADFAKDRADLPTLG 156
Cdd:PLN02848 93 NHDVKA-VEYFlkQKCKshPELAKVlefFHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHEFAYVPMLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 157 FTHFQPAQLTTVGKRcclwIQDLCMDLQNLKRVRDELRFRG-VKGTTGT-QASFLQLFEGDHQKVEQldkmvtekaGFKR 234
Cdd:PLN02848 172 RTHGQPASPTTLGKE----MANFAYRLSRQRKQLSEVKIKGkFAGAVGNyNAHMSAYPEVDWPAVAE---------EFVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 235 AFIITGQTYTRKvdIEVLSVLASLGASVHKICT-------DIRLLANLKEMEEPFEKQQIGSSAMPYKRNPM---RSERC 304
Cdd:PLN02848 239 SLGLTFNPYVTQ--IEPHDYMAELFNAVSRFNNilidfdrDIWSYISLGYFKQITKAGEVGSSTMPHKVNPIdfeNSEGN 316
|
330 340 350
....*....|....*....|....*....|
gi 29788764 305 CSLARHLMALTMDPLQTASVQwfeRTLDDS 334
Cdd:PLN02848 317 LGLANAELSHLSMKLPISRMQ---RDLTDS 343
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
124-298 |
2.49e-08 |
|
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: 55.99 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 124 LRNAFDLLLPKLARVISRLAD--FAKDR--ADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVK 199
Cdd:cd01357 144 LRLALILLLRKLLDALAALQEafQAKARefADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 200 GT---TGTQASFlqlfegDHQK--VEQLDKMVteKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLA- 273
Cdd:cd01357 224 GTaigTGINAPP------GYIElvVEKLSEIT--GLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSs 295
|
170 180 190
....*....|....*....|....*....|....
gi 29788764 274 ---------NLKEMeepfekqQIGSSAMPYKRNP 298
Cdd:cd01357 296 gpraglgeiNLPAV-------QPGSSIMPGKVNP 322
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
124-316 |
7.86e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 54.39 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 124 LRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLcmdlqnlkrVRDELRFRGVK---- 199
Cdd:PRK00855 123 LRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEML---------ARDLERLRDARkrvn 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 200 ----------GTTgtqasflqlFEgdhqkveqLD-KMVTEKAGFKRAFI--ITGQTyTRKVDIEVLSVLASLGASVHKIC 266
Cdd:PRK00855 194 rsplgsaalaGTT---------FP--------IDrERTAELLGFDGVTEnsLDAVS-DRDFALEFLSAASLLMVHLSRLA 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29788764 267 TDIRLLANlkemeepfekQQI-----------GSSAMPYKRNP-----MRSeRCCSLARHLMALTM 316
Cdd:PRK00855 256 EELILWSS----------QEFgfvelpdafstGSSIMPQKKNPdvaelIRG-KTGRVYGNLTGLLT 310
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
131-298 |
1.28e-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: 53.97 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 131 LLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVKGT---TG--TQ 205
Cdd:cd01596 155 LLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTavgTGlnAP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 206 ASFLQLFegdhqkVEQLDKmvtekagfkrafiITGQTYTR---KVD--------IEVLSVLASLGASVHKICTDIRLLA- 273
Cdd:cd01596 235 PGYAEKV------AAELAE-------------LTGLPFVTapnLFEataahdalVEVSGALKTLAVSLSKIANDLRLLSs 295
|
170 180 190
....*....|....*....|....*....|....
gi 29788764 274 ---------NLKEMeEPfekqqiGSSAMPYKRNP 298
Cdd:cd01596 296 gpraglgeiNLPAN-QP------GSSIMPGKVNP 322
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
131-302 |
2.31e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 49.98 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 131 LLPKLARVISRLADF----AKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVKGT---TG 203
Cdd:PRK13353 156 LLEGLLAAMGALQDVfeekAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTavgTG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 204 TQAsflqlfegDHQKVEQLDKMVTEKAG--FKRAF-IITGqtyTRKVD--IEVLSVLASLGASVHKICTDIRLLAN---- 274
Cdd:PRK13353 236 LNA--------DPEYIERVVKHLAAITGlpLVGAEdLVDA---TQNTDafVEVSGALKVCAVNLSKIANDLRLLSSgprt 304
|
170 180
....*....|....*....|....*....
gi 29788764 275 -LKEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:PRK13353 305 gLGEINLP--AVQPGSSIMPGKVNPVMPE 331
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
119-298 |
4.03e-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: 49.08 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 119 TDL-IILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFR- 196
Cdd:cd01359 93 TDLrLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVSp 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 197 -GVKGTTGTqaSFLqlfegdhqkveqLD-KMVTEKAGFKRafiITGQTY----TRKVDIEVLSVLASLGASVHKICTDIR 270
Cdd:cd01359 173 lGAGALAGT--TFP------------IDrERTAELLGFDG---PTENSLdavsDRDFVLEFLSAAALLMVHLSRLAEDLI 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 29788764 271 LLANlkemeepFEKQQI--------GSSAMPYKRNP 298
Cdd:cd01359 236 LWST-------QEFGFVelpdaystGSSIMPQKKNP 264
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
124-298 |
5.79e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 48.58 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 124 LRNAFDLLLPKLARVISRLAD-F---AKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVK 199
Cdd:PRK12273 151 IRIALLLSLRKLLDALEQLQEaFeakAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 200 GT---TG--TQASFLQLFegdhqkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 263
Cdd:PRK12273 231 ATaigTGlnAPPGYIELV------VEKLAE-------------ITGLPLVPAEDlieatqdtgafVEVSGALKRLAVKLS 291
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29788764 264 KICTDIRLL-----ANLKEMEEPfeKQQIGSSAMPYKRNP 298
Cdd:PRK12273 292 KICNDLRLLssgprAGLNEINLP--AVQAGSSIMPGKVNP 329
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
124-298 |
7.99e-06 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 48.12 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 124 LRNAFDLLLPKLARVISRLAD-F---AKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVK 199
Cdd:COG1027 146 IRLALLLLLRELLEALERLQEaFaakAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 200 GT---TG--TQASFLQLFegdhqkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 263
Cdd:COG1027 226 GTaigTGlnAPPGYIELV------VEHLAE-------------ITGLPLVRAENlieatqdtdafVEVSGALKRLAVKLS 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29788764 264 KICTDIRLLA----------NLKEMeepfekqQIGSSAMPYKRNP 298
Cdd:COG1027 287 KICNDLRLLSsgpraglgeiNLPAV-------QPGSSIMPGKVNP 324
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
131-316 |
6.23e-05 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 45.47 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 131 LLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVKGT---TGTQAs 207
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTavgTGLNA- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 208 flqlfegdhqkveqldkmvteKAGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 271
Cdd:PRK00485 239 ---------------------HPGFAERVAeelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29788764 272 LAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSErccslarhlmALTM 316
Cdd:PRK00485 298 LASgprcgLGEISLP--ENEPGSSIMPGKVNPTQCE----------ALTM 335
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
131-316 |
8.21e-05 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 44.80 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 131 LLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVKGT---TGTQAs 207
Cdd:cd01362 156 LLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTavgTGLNA- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29788764 208 flqlfegdhqkveqldkmvteKAGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 271
Cdd:cd01362 235 ---------------------HPGFAEKVAaelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29788764 272 LAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSErccslarhlmALTM 316
Cdd:cd01362 294 LGSgprcgLGELSLP--ENEPGSSIMPGKVNPTQCE----------ALTM 331
|
|
| |
