|
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: 888.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 177 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQ 416
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 4557269 417 EGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 452
Cdd:cd03302 401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
17-460 |
1.97e-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: 469.18 E-value: 1.97e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:COG0015 81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 174 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDKMVTEKAGFKRAFiITGQTYTRKVDIEVLS 253
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNP-VTTQIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 254 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 331
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 332 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 411
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 4557269 412 SvvkqegGDNDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRASQQVQRF 460
Cdd:COG0015 392 E------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
17-460 |
3.47e-151 |
|
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: 437.93 E-value: 3.47e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 176 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFegddhkvEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 256 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDD 333
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAsv 413
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAA-- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4557269 414 vkqEGGDNDLIERIQVDAYFSPIHSQLD--HLLDPSSFTGRASQQVQRF 460
Cdd:TIGR00928 390 ---EVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
248-451 |
4.90e-73 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 229.92 E-value: 4.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 248 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 325
Cdd:PRK08937 17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 326 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 405
Cdd:PRK08937 95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 4557269 406 LSQQAASVVkqeggdNDLIERIQVDAYFSPIHSQ--LDHLLDPSSFTG 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 |
5.01e-24 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 95.17 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 378 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAASVVKqeggdNDLIERIQVDAYFS-PIHSQLDHLLDPSSFTGRASQQ 456
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 4557269 457 VQRF 460
Cdd:pfam10397 75 VDRV 78
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
377-461 |
1.61e-19 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 82.88 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 377 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKqeggdnDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRAS 454
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74
|
....*..
gi 4557269 455 QQVQRFL 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: 888.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 97 HCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 176
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 177 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 256
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 257 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 336
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 337 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQ 416
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 4557269 417 EGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 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 |
1.35e-172 |
|
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: 490.09 E-value: 1.35e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 26 MCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHTFGHCCPK-A 102
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADVfeIDAERIAEIEKETGHDVIAFVYALAEKCGEdA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 103 AGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMD 182
Cdd:cd01595 80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 183 LQNLKRVRDDLRFRGVKGTTGTQASFLQlfegddhKVEQLDKMVTEKAGFKrAFIITGQTYTRKVDIEVLSVLASLGASV 262
Cdd:cd01595 160 LERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEERVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 263 HKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDDSANRRIC 340
Cdd:cd01595 232 EKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDSSVERNI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557269 341 LAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 405
Cdd:cd01595 311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
17-460 |
1.97e-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: 469.18 E-value: 1.97e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:COG0015 81 LKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 174 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDKMVTEKAGFKRAFiITGQTYTRKVDIEVLS 253
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNP-VTTQIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 254 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 331
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 332 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 411
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 4557269 412 SvvkqegGDNDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRASQQVQRF 460
Cdd:COG0015 392 E------EGNDLRELLAADPEIPAELSkeELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
17-460 |
3.47e-151 |
|
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: 437.93 E-value: 3.47e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 176 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFegddhkvEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 256 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDD 333
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAsv 413
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAA-- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4557269 414 vkqEGGDNDLIERIQVDAYFSPIHSQLD--HLLDPSSFTGRASQQVQRF 460
Cdd:TIGR00928 390 ---EVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
36-365 |
2.08e-98 |
|
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: 299.03 E-value: 2.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 36 FRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLENIDFKMAA---EEEKRLRHDVMAHVHTFGHCCPKA-AGIIHLGAT 111
Cdd:cd01334 1 IRADLQVEKAHAKALAELGL-LPKEAAEAILAALDEILEGIAAdqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 112 SCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRD 191
Cdd:cd01334 80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 192 DLRFRGVKGTT-GTQASFlqlfegddhkVEQLDKMVTEKAGFKRAFIITGQ-TYTRKVDIEVLSVLASLGASVHKICTDI 269
Cdd:cd01334 160 RLNVLPLGGGAvGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 270 RLLAN--LKEMEEPFEKQqIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASvQWFERTLDDSANRRICLAEAFLT 347
Cdd:cd01334 230 RLLSSgeFGEVELPDAKQ-PGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDL 307
|
330
....*....|....*...
gi 4557269 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 |
9.76e-76 |
|
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: 242.84 E-value: 9.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 20 RYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQE----MKSNLENIDfkmaaEEEKRLRHDVMAHVHTF 95
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGV-IPAEAAEEirkkAKFDVERVK-----EIEAETKHDVIAFVTAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 96 GHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 175
Cdd:cd01360 75 AEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 176 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfegdDHKVEqldKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 255
Cdd:cd01360 155 YAEFKRHLERLKEARERILVGKISGAVGTYANL-------GPEVE---ERVAEKLGLKPEPIST-QVIQRDRHAEYLSTL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 256 ASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERTLDD 333
Cdd:cd01360 224 ALIASTLEKIATEIRHLqrTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNV-IPALENVALWHERDISH 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557269 334 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIR 404
Cdd:cd01360 303 SSVERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQ 373
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
248-451 |
4.90e-73 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 229.92 E-value: 4.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 248 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 325
Cdd:PRK08937 17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 326 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 405
Cdd:PRK08937 95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 4557269 406 LSQQAASVVkqeggdNDLIERIQVDAYFSPIHSQ--LDHLLDPSSFTG 451
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
17-463 |
3.67e-54 |
|
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: 187.84 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL--PITDEQIQEmKSNLENIDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:cd01597 2 LGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVipKEAAAEIAA-AADVERLDLEALAEATARTGHPAIPLVKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 95 FGHCCPKAAG-IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 173
Cdd:cd01597 81 LTAACGDAAGeYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 174 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfeGDDhkveqldKMVTEKAGFKR----AFIITGQTyTRKVDI 249
Cdd:cd01597 161 VWLSELLRHRERLDELRPRVLVVQFGGAAGTLASL-----GDQ-------GLAVQEALAAElglgVPAIPWHT-ARDRIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 250 EVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLAR---HLMTLVMDplqtASV 324
Cdd:cd01597 228 ELASFLALLTGTLGKIARDVYLLmqTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARrvpGLAALLLD----AMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 325 QWFERtlDDSANR--RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGsRQDCHEK 402
Cdd:cd01597 304 QEHER--DAGAWHaeWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLG-RQEAHDL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557269 403 IRVLSQQAAsvvkQEGGdnDLIERI----QVDAYFSPihSQLDHLLDPSSFTGRASQQVQRFLEE 463
Cdd:cd01597 381 VYEACMRAV----EEGR--PLREVLledpEVAAYLSD--EELDALLDPANYLGSAPALVDRVLAR 437
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
96-356 |
1.30e-43 |
|
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: 153.53 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 96 GHCCPKAAGII-----HLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGK 170
Cdd:cd01594 22 GRAGELAGGLHgsalvHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 171 RCCLWIQDLCMDLQNLKRVRDdlrfrgvkgttgtqasflqlfegddhkveqldkmvtekagfkrafiitgqtytrkvdIE 250
Cdd:cd01594 102 ELRAWAQVLGRDLERLEEAAV---------------------------------------------------------AE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 251 VLSVLASLGASVHKICTDIRLLANLKEME--EPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLqTASVQWFE 328
Cdd:cd01594 125 ALDALALAAAHLSKIAEDLRLLLSGEFGElgEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVL-TALKGGPE 203
|
250 260
....*....|....*....|....*...
gi 4557269 329 RTLDDSANRRICLAEAFLTADTILNTLQ 356
Cdd:cd01594 204 RDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
17-331 |
6.30e-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: 110.99 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 17 LASRYAS-PEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLENIDFKMAAEEE-------------K 82
Cdd:TIGR02426 1 LLDGLFGdPAALELFSDRAFLRAMLDFEAALARAQADAGL-IPAEAAAAIEAACAAAAPDLEALAHaaatagnpviplvK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 83 RLRHDVMAhvhtfghccpKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQP 162
Cdd:TIGR02426 80 ALRKAVAG----------EAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 163 AQLTTVGKRCCLWIQDLCMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDkMVTEKAGF--KR 234
Cdd:TIGR02426 150 AVPTTFGLKAAGWLAAVLRARDRLAALRTRalpLQFGGAAGTlaaLGTRGGAVA-----AALAARLG-LPLPALPWhtQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 235 AFIItgqtytrkvdiEVLSVLASLGASVHKICTDIRLLANLkEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTL 314
Cdd:TIGR02426 224 DRIA-----------EFGSALALVAGALGKIAGDIALLSQT-EVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGL 291
|
330
....*....|....*..
gi 4557269 315 VMdPLQTASVQWFERTL 331
Cdd:TIGR02426 292 AA-TLHAALPQEHERSL 307
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
378-460 |
5.01e-24 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 95.17 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 378 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAASVVKqeggdNDLIERIQVDAYFS-PIHSQLDHLLDPSSFTGRASQQ 456
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 4557269 457 VQRF 460
Cdd:pfam10397 75 VDRV 78
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
22-302 |
1.64e-22 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 97.82 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 22 ASPEMCFVFSDR--YKFRTWRQLWLW---LAEAEQTLGLPIT----------DEQIQEMKSNLENI----------DFKM 76
Cdd:pfam00206 6 PADALMGIFTDRsrFNFRLGEEDIKGlaaLKKAAAKANVILKeeaaaiikalDEVAEEGKLDDQFPlkvwqegsgtAVNM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 77 AAEEekRLRHDVMAHVHTFGHccpkaagiIHLGATScyvGD--NTDL-IILRNAL-DLLLPKLARVISRLADFAKERASL 152
Cdd:pfam00206 86 NLNE--VIGELLGQLVHPNDH--------VHTGQSS---NDqvPTALrLALKDALsEVLLPALRQLIDALKEKAKEFADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 153 PTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMvtEKAGF 232
Cdd:pfam00206 153 VKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--TGLPV 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557269 233 KRAFIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 302
Cdd:pfam00206 231 KAPNSFE-ATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
15-463 |
1.89e-20 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 93.54 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 15 SPLASRY-ASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEE----------- 81
Cdd:PRK09053 5 ARLTDLYfGSPAMRAIFSDRATVQRMLDFEAALARAEAACGViPAAAVAPIEAACDAERLDLDALAQAAalagnlaiplv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 82 KRLRHDVMAHVhtfghccPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQ 161
Cdd:PRK09053 85 KQLTAQVAARD-------AEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 162 PAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASF----------------LQLFEGDDHKveQLDKM 225
Cdd:PRK09053 158 QALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqalpvaqalaaelqLALPALPWHT--QRDRI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 226 VtekagfkrafiitgqtytrkvdiEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSER 303
Cdd:PRK09053 236 A-----------------------EFASALGLLAGTLGKIARDVSLLmqTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 304 CCSLARHLMTLVMDpLQTASVQWFERTLD------DSANRRICLAEAFLTAdtilntLQNISEGLVVYPKvierRIRQEL 377
Cdd:PRK09053 293 VLTAATRAPGLVAT-LFAAMPQEHERALGgwhaewDTLPELACLAAGALAQ------MAQIVEGLEVDAA----RMRANL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 378 PfmATENIIMA---MVKAGGS--RQDCHEKIRVLSQQAasVVKQEGGDNDLIERIQVDAYFSPihSQLDHLLDPSSFTGR 452
Cdd:PRK09053 362 D--LTHGLILAeavMLALADRigRLDAHHLVEQASKRA--VAEGRHLRDVLAEDPQVSAHLSP--AALDRLLDPAHYLGQ 435
|
490
....*....|.
gi 4557269 453 ASQQVQRFLEE 463
Cdd:PRK09053 436 AHAWVDRVLAE 446
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
377-461 |
1.61e-19 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 82.88 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 377 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKqeggdnDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRAS 454
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74
|
....*..
gi 4557269 455 QQVQRFL 461
Cdd:smart00998 75 AIVDRVL 81
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
43-377 |
5.52e-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: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMA---AEEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:cd01598 21 WLiALSNLEEIPEVPpLTKEELKFLRAIIENFSEEDAlriKEIEATTNHDVKAveyflkeKFETLGLL-KKIKEFIHFAC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 111 TScyvGDNTDLII---LRNAL-DLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNL 186
Cdd:cd01598 100 TS---EDINNLAYalmIKEARnEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 187 KRVRDDLRFrgvKGTTGTQASflqlfegddHKVE--QLDKMVTEKAgFKRAFIITGQTYTRKVD-----IEVLSVLASLG 259
Cdd:cd01598 177 KQIEILGKF---NGAVGNFNA---------HLVAypDVDWRKFSEF-FVTSLGLTWNPYTTQIEphdyiAELFDALARIN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 260 ASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHL-MTLVMDPLQtasvqwfeRTL 331
Cdd:cd01598 244 TILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAegnlglsNALLNHLsAKLPISRLQ--------RDL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 4557269 332 DDSANRR---ICLAEAFLTADTILNTLQNISeglvvypkVIERRIRQEL 377
Cdd:cd01598 316 TDSTVLRnigVAFGHSLIAYKSLLRGLDKLE--------LNEARLLEDL 356
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-330 |
1.62e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 74.71 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 100 PKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDL 179
Cdd:PRK05975 96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 180 CMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDKMVTEKAGFKRAFIitgqtytrkVDIEVLs 253
Cdd:PRK05975 176 LRHRDRLEALRADvfpLQFGGAAGTlekLGGKAAAVR-----ARLAKRLGLEDAPQWHSQRDFI---------ADFAHL- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 254 vLASLGASVHKICTDIRLLAnlkEMEEpfEKQQIG---SSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERT 330
Cdd:PRK05975 241 -LSLVTGSLGKFGQDIALMA---QAGD--EISLSGgggSSAMPHKQNPVAAETLVTLARFNATQV-SGLHQALVHEQERS 313
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
43-311 |
2.18e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 62.46 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMAA---EEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:PRK09285 43 WLiALAAHPGIPEVPpFSAEANAFLRAIVENFSEEDAArikEIERTTNHDVKAveyflkeKLAGLPEL-EAVSEFIHFAC 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 111 TScyvGDNTDL---IILRNALD-LLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKrcclwiqdlcmDLQN- 185
Cdd:PRK09285 122 TS---EDINNLshaLMLKEAREeVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGK-----------EMANv 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 186 ---LKRVRDdlRFRGVK------GTTGTQASFLQLF-EGDDHKveqldkmvtekagFKRAFI----ITGQTYTRKV---- 247
Cdd:PRK09285 188 ayrLERQLK--QLEAVEilgkinGAVGNYNAHLAAYpEVDWHA-------------FSREFVeslgLTWNPYTTQIephd 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557269 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 |
2.30e-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: 59.46 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 124 LRNALDLLLPKLARVISRLAD--FAKER--ASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:cd01357 144 LRLALILLLRKLLDALAALQEafQAKARefADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 200 GT---TGTQASFlqlfEGDDHKVEQLDKMVteKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLA--- 273
Cdd:cd01357 224 GTaigTGINAPP----GYIELVVEKLSEIT--GLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSsgp 297
|
170 180 190
....*....|....*....|....*....|..
gi 4557269 274 -------NLKEMeepfekqQIGSSAMPYKRNP 298
Cdd:cd01357 298 raglgeiNLPAV-------QPGSSIMPGKVNP 322
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
15-170 |
6.02e-08 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 54.74 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 15 SPLASRYAS--PEMCFVFSD----RYKFRTWRQLWLWLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMAAEE---EKRL 84
Cdd:PLN02848 13 SPLDGRYWSkvKDLRPIFSEfgliRYRVLVEVKWLLKLSQIPEVTEVPpFSDEANSFLEGIIAGFSVDDALEVkkiERVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 85 RHDVMAhVHTF--GHCC--PKAAGI---IHLGATSCYVGDNTDLIILRNALD-LLLPKLARVISRLADFAKERASLPTLG 156
Cdd:PLN02848 93 NHDVKA-VEYFlkQKCKshPELAKVlefFHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHEFAYVPMLS 171
|
170
....*....|....
gi 4557269 157 FTHFQPAQLTTVGK 170
Cdd:PLN02848 172 RTHGQPASPTTLGK 185
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
124-314 |
7.73e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 54.39 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 124 LRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQnlkRVRDDLRfRgVK---- 199
Cdd:PRK00855 123 LRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLE---RLRDARK-R-VNrspl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 200 ------GTTgtqasflqlFEgddhkveqLD-KMVTEKAGFKRAFI--ITGQTyTRKVDIEVLSVLASLGASVHKICTDIR 270
Cdd:PRK00855 198 gsaalaGTT---------FP--------IDrERTAELLGFDGVTEnsLDAVS-DRDFALEFLSAASLLMVHLSRLAEELI 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 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 |
9.87e-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: 54.35 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 128 LDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG- 203
Cdd:cd01596 152 LERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTavgTGl 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 204 -TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTR---KVD--------IEVLSVLASLGASVHKICTDIRL 271
Cdd:cd01596 232 nAPPGYAEKV------AAELAE-------------LTGLPFVTapnLFEataahdalVEVSGALKTLAVSLSKIANDLRL 292
|
170 180 190
....*....|....*....|....*....|....*..
gi 4557269 272 LA----------NLKEMeEPfekqqiGSSAMPYKRNP 298
Cdd:cd01596 293 LSsgpraglgeiNLPAN-QP------GSSIMPGKVNP 322
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
124-298 |
1.15e-07 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 53.98 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 124 LRNALDLLLPKLARVISRLAD-F---AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:PRK12273 151 IRIALLLSLRKLLDALEQLQEaFeakAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 200 GT---TG--TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 263
Cdd:PRK12273 231 ATaigTGlnAPPGYIELV------VEKLAE-------------ITGLPLVPAEDlieatqdtgafVEVSGALKRLAVKLS 291
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4557269 264 KICTDIRLL-----ANLKEMEEPfeKQQIGSSAMPYKRNP 298
Cdd:PRK12273 292 KICNDLRLLssgprAGLNEINLP--AVQAGSSIMPGKVNP 329
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
124-298 |
2.86e-07 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 52.75 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 124 LRNALDLLLPKLARVISRLAD-F---AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:COG1027 146 IRLALLLLLRELLEALERLQEaFaakAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 200 GT---TG--TQASFLQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVH 263
Cdd:COG1027 226 GTaigTGlnAPPGYIELV------VEHLAE-------------ITGLPLVRAENlieatqdtdafVEVSGALKRLAVKLS 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4557269 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 |
2.11e-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: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 119 TDL-IILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFR- 196
Cdd:cd01359 93 TDLrLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVSp 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 197 -GVKGTTGTqaSFLqlfegddhkveqLD-KMVTEKAGFKRafiITGQTY----TRKVDIEVLSVLASLGASVHKICTDIR 270
Cdd:cd01359 173 lGAGALAGT--TFP------------IDrERTAELLGFDG---PTENSLdavsDRDFVLEFLSAAALLMVHLSRLAEDLI 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 4557269 271 LLANlkemeepFEKQQI--------GSSAMPYKRNP 298
Cdd:cd01359 236 LWST-------QEFGFVelpdaystGSSIMPQKKNP 264
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
124-302 |
7.84e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 48.06 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 124 LRNALDLLLPKLARVISRLADF----AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVK 199
Cdd:PRK13353 149 IRIAALNLLEGLLAAMGALQDVfeekAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 200 GT---TGTQASflqlfegddhkVEQLDKMVTEKAGfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHKI 265
Cdd:PRK13353 229 GTavgTGLNAD-----------PEYIERVVKHLAA------ITGLPLVGAEDlvdatqntdafVEVSGALKVCAVNLSKI 291
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4557269 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 |
1.37e-04 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 44.41 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 131 LLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG--TQ 205
Cdd:cd01362 156 LLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTavgTGlnAH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 206 ASFLQL------------FEGDDHKVEQL---DKMVtekagfkrafiitgqtytrkvdiEVLSVLASLGASVHKICTDIR 270
Cdd:cd01362 236 PGFAEKvaaelaeltglpFVTAPNKFEALaahDALV-----------------------EASGALKTLAVSLMKIANDIR 292
|
170 180 190
....*....|....*....|....*....|....*..
gi 4557269 271 LLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:cd01362 293 WLGSgprcgLGELSLP--ENEPGSSIMPGKVNPTQCE 327
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
131-302 |
2.17e-04 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 43.54 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 131 LLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TGTQAs 207
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTavgTGLNA- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 208 flqlfegddHKveqldkmvtekaGFKRAFI-----ITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRL 271
Cdd:PRK00485 239 ---------HP------------GFAERVAeelaeLTGLPFVTAPNkfealaahdalVEASGALKTLAVSLMKIANDIRW 297
|
170 180 190
....*....|....*....|....*....|....*.
gi 4557269 272 LAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:PRK00485 298 LASgprcgLGEISLP--ENEPGSSIMPGKVNPTQCE 331
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
126-302 |
1.76e-03 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 40.75 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 126 NALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---T 202
Cdd:PRK14515 161 NALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATavgT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557269 203 GTQAsflqlfegDDHKVEQLDKMVTEKAGF--KRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN-----L 275
Cdd:PRK14515 241 GLNA--------DPEYIEAVVKHLAAISELplVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASgprvgL 312
|
170 180
....*....|....*....|....*..
gi 4557269 276 KEMEEPfeKQQIGSSAMPYKRNPMRSE 302
Cdd:PRK14515 313 AEIMLP--ARQPGSSIMPGKVNPVMPE 337
|
|
| |
