|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
1-456 |
0e+00 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 1021.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 1 MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAA 80
Cdd:PRK09285 1 MELSALTALSPLDGRYASKTAALRPIFSEFGLIRYRVQVEVEWLIALAAHPGIPEVPPFSAEANAFLRAIVENFSEEDAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 81 RIKTIERTTNHDVKAVEYFLKEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQ 160
Cdd:PRK09285 81 RIKEIERTTNHDVKAVEYFLKEKLAGLPELEAVSEFIHFACTSEDINNLSHALMLKEAREEVLLPALRELIDALKELAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 161 YRDIPLLSRTHGQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ 240
Cdd:PRK09285 161 YADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVEILGKINGAVGNYNAHLAAYPEVDWHAFSREFVESLGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 241 WNPYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV 320
Cdd:PRK09285 241 WNPYTTQIEPHDYIAELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGSSTMPHKVNPIDFENSEGNLGLANAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 321 LQHLASKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK 400
Cdd:PRK09285 321 LEHLAAKLPISRWQRDLTDSTVLRNLGVAFGYSLIAYDSLLKGLGKLEVNEARLAEDLDANWEVLAEPIQTVMRRYGIEN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129094 401 PYEKLKELTRGKRVDAEGMKQFIDGLALPEEEKARLKAMTPANYIGRAITMVDELK 456
Cdd:PRK09285 401 PYEKLKELTRGKRITAEALREFIDGLDLPEEAKARLKALTPANYIGLAAELADEIK 456
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
23-446 |
0e+00 |
|
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: 829.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 23 LRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAVEYFLKE 102
Cdd:cd01598 1 LRPYFSEYALIKYRVQVEVEWLIALSNLEEIPEVPPLTKEELKFLRAIIENFSEEDALRIKEIEATTNHDVKAVEYFLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 103 KVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGK 182
Cdd:cd01598 81 KFETLGLLKKIKEFIHFACTSEDINNLAYALMIKEARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 183 EMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCVA 262
Cdd:cd01598 161 ELAVFVYRLERQYKQLKQIEILGKFNGAVGNFNAHLVAYPDVDWRKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 263 RFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKLPVSRWQRDLTDSTV 342
Cdd:cd01598 241 RINTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAEGNLGLSNALLNHLSAKLPISRLQRDLTDSTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 343 LRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMKQF 422
Cdd:cd01598 321 LRNIGVAFGHSLIAYKSLLRGLDKLELNEARLLEDLDANWEVLAEPIQTVMRRYGIPNPYEKLKDLTRGKRIDKETLKEF 400
|
410 420
....*....|....*....|....
gi 16129094 423 IDGLALPEEEKARLKAMTPANYIG 446
Cdd:cd01598 401 IDSLDIPEEAKAELLALTPANYIG 424
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
12-455 |
0e+00 |
|
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: 547.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 12 VDGRYGdkVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevpafAADAIGYLDAIvASFSEEDAARIKTIERTTNH 91
Cdd:TIGR00928 1 LDERYG--SPEMRAIWSEENKFKTWLDVEVAVLRALAELGVI------PAEAVKEIREK-ANFTEVDLERIKEIEAVTRH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 92 DVKAVEYFLKEKVAeipelhAVSEFIHFACTSEDINNLSHALMLKTArDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTH 171
Cdd:TIGR00928 72 DVKAVVYALKEKCG------AEGEFIHFGATSNDIVDTALALLLRDA-LEIILPKLKQLIDRLKELAVEYKDTVMLGRTH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 172 GQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVdwhQFSEEFVTS-LGIQWNPYTTQIEP 250
Cdd:TIGR00928 145 GQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV---EEVEERVTEfLGLKPVPISTQIEP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 251 HDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIA--GEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKL 328
Cdd:TIGR00928 222 RDRHAELLDALALLATTLEKFAVDIRLLQRTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 329 PvSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEP---IQTVMRRYGIEKPYEK 404
Cdd:TIGR00928 302 P-LWHERDLTDSSVERViLPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASErvlIALVERGMGREEAYEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129094 405 LKELTRG-KRVDAEGMKQFIDGLA-LPEEEKARLKA--MTPANYIGRAITMVDEL 455
Cdd:TIGR00928 381 VRELAMGaAEVDEPDLLEFLLEDErITKYLKEEELAelLDPETYIGNAGEIVERV 435
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
12-455 |
0e+00 |
|
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: 536.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 12 VDGRYGDKvsALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevPAFAADAIgylDAIVASFsEEDAARIKTIERTTNH 91
Cdd:COG0015 2 ISPRYASP--EMRAIFSEEAKIRAWLDVEIALAEAQAELGLI---PAEAAAAI---RAAADDF-EIDAERIKEIEKETRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 92 DVKAVEYFLKEKVAEipelhAVSEFIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYRDIPLLSRTH 171
Cdd:COG0015 73 DVKAFVYALKEKVGA-----EAGEYIHFGATSQDINDTALALQLREALE-LLLPDLDALIAALAELAEEHKDTPMLGRTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 172 GQPATPSTIGKEMANVAYRMERQYRQLNQV---EILGKINGAVGNYNAHIAAypevdWHQFSEEFVTSLGIQWNPYTTQI 248
Cdd:COG0015 147 GQHAEPTTFGKKLAVWAAELLRQLERLEEArerVLVGKIGGAVGTYAAHGEA-----WPEVEERVAEKLGLKPNPVTTQI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 249 EPHDYIAELFDCVARFNTILIDFDRDVWGYIA--LNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLAS 326
Cdd:COG0015 222 EPRDRHAELFSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 327 KLpVSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWE-VLAEPIQTVMRRYGI--EKPY 402
Cdd:COG0015 302 AL-ASWHERDLSDSSVERNiLPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGlVLSEAVLMALVRRGLgrEEAY 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129094 403 EKLKELTRGKRVDAEGMKQFIDG-LALPEE-EKARLKAMT-PANYIGRAITMVDEL 455
Cdd:COG0015 381 ELVKELARGAWEEGNDLRELLAAdPEIPAElSKEELEALFdPANYLGAADEIVDRV 436
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
14-320 |
3.83e-108 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 322.40 E-value: 3.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 14 GRYGDKVSALRGIFSEYGLLKFRVQVE-VRWLQKLAAHAAIKEVPA--FAADAIGYLDAIVASFSEEDAARIKTIERTTN 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEdIKGLAALKKAAAKANVILkeEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 91 HDVKA-VEYFLKEKVAEipeLHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSR 169
Cdd:pfam00206 81 TAVNMnLNEVIGELLGQ---LVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKEKAKEFADIVKPGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 170 THGQPATPSTIGKE--MANVAYRMERQ-YRQLNQVEILGKINGAVGNYNAHIAAYP--EVDWHQFSeeFVTSLGiQWNPY 244
Cdd:pfam00206 158 THLQDATPVTLGQElsGYAVALTRDRErLQQLLPRLLVLPLGGGTAVGTGLNADPEfaELVAKELG--FFTGLP-VKAPN 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129094 245 T-TQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIA--LNHFKQKTIAGEIGSSTMPHKVNPIDFENseGNLGLSNAV 320
Cdd:pfam00206 235 SfEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLEL--LTGKAGRVM 311
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
1-456 |
0e+00 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 1021.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 1 MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAA 80
Cdd:PRK09285 1 MELSALTALSPLDGRYASKTAALRPIFSEFGLIRYRVQVEVEWLIALAAHPGIPEVPPFSAEANAFLRAIVENFSEEDAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 81 RIKTIERTTNHDVKAVEYFLKEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQ 160
Cdd:PRK09285 81 RIKEIERTTNHDVKAVEYFLKEKLAGLPELEAVSEFIHFACTSEDINNLSHALMLKEAREEVLLPALRELIDALKELAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 161 YRDIPLLSRTHGQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ 240
Cdd:PRK09285 161 YADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVEILGKINGAVGNYNAHLAAYPEVDWHAFSREFVESLGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 241 WNPYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV 320
Cdd:PRK09285 241 WNPYTTQIEPHDYIAELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGSSTMPHKVNPIDFENSEGNLGLANAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 321 LQHLASKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK 400
Cdd:PRK09285 321 LEHLAAKLPISRWQRDLTDSTVLRNLGVAFGYSLIAYDSLLKGLGKLEVNEARLAEDLDANWEVLAEPIQTVMRRYGIEN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129094 401 PYEKLKELTRGKRVDAEGMKQFIDGLALPEEEKARLKAMTPANYIGRAITMVDELK 456
Cdd:PRK09285 401 PYEKLKELTRGKRITAEALREFIDGLDLPEEAKARLKALTPANYIGLAAELADEIK 456
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
23-446 |
0e+00 |
|
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: 829.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 23 LRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAVEYFLKE 102
Cdd:cd01598 1 LRPYFSEYALIKYRVQVEVEWLIALSNLEEIPEVPPLTKEELKFLRAIIENFSEEDALRIKEIEATTNHDVKAVEYFLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 103 KVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGK 182
Cdd:cd01598 81 KFETLGLLKKIKEFIHFACTSEDINNLAYALMIKEARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 183 EMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCVA 262
Cdd:cd01598 161 ELAVFVYRLERQYKQLKQIEILGKFNGAVGNFNAHLVAYPDVDWRKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 263 RFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKLPVSRWQRDLTDSTV 342
Cdd:cd01598 241 RINTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAEGNLGLSNALLNHLSAKLPISRLQRDLTDSTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 343 LRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMKQF 422
Cdd:cd01598 321 LRNIGVAFGHSLIAYKSLLRGLDKLELNEARLLEDLDANWEVLAEPIQTVMRRYGIPNPYEKLKDLTRGKRIDKETLKEF 400
|
410 420
....*....|....*....|....
gi 16129094 423 IDGLALPEEEKARLKAMTPANYIG 446
Cdd:cd01598 401 IDSLDIPEEAKAELLALTPANYIG 424
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
1-451 |
0e+00 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 812.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 1 MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAA 80
Cdd:PLN02848 4 LELSNLTALSPLDGRYWSKVKDLRPIFSEFGLIRYRVLVEVKWLLKLSQIPEVTEVPPFSDEANSFLEGIIAGFSVDDAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 81 RIKTIERTTNHDVKAVEYFLKEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQ 160
Cdd:PLN02848 84 EVKKIERVTNHDVKAVEYFLKQKCKSHPELAKVLEFFHFACTSEDINNLSHALMLKEGVNSVVLPTMDEIIKAISSLAHE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 161 YRDIPLLSRTHGQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ 240
Cdd:PLN02848 164 FAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVKIKGKFAGAVGNYNAHMSAYPEVDWPAVAEEFVTSLGLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 241 WNPYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV 320
Cdd:PLN02848 244 FNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWSYISLGYFKQITKAGEVGSSTMPHKVNPIDFENSEGNLGLANAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 321 LQHLASKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK 400
Cdd:PLN02848 324 LSHLSMKLPISRMQRDLTDSTVLRNMGVGLGHSLLAYKSTLRGIGKLQVNEARLAEDLDQTWEVLAEPIQTVMRRYGVPE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16129094 401 PYEKLKELTRGKRVDAEGMKQFIDGLALPEEEKARLKAMTPANYIGRAITM 451
Cdd:PLN02848 404 PYEKLKELTRGRAVTKESMREFIEGLELPEEAKDQLLKLTPHTYIGAAAAL 454
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
12-455 |
0e+00 |
|
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: 547.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 12 VDGRYGdkVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevpafAADAIGYLDAIvASFSEEDAARIKTIERTTNH 91
Cdd:TIGR00928 1 LDERYG--SPEMRAIWSEENKFKTWLDVEVAVLRALAELGVI------PAEAVKEIREK-ANFTEVDLERIKEIEAVTRH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 92 DVKAVEYFLKEKVAeipelhAVSEFIHFACTSEDINNLSHALMLKTArDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTH 171
Cdd:TIGR00928 72 DVKAVVYALKEKCG------AEGEFIHFGATSNDIVDTALALLLRDA-LEIILPKLKQLIDRLKELAVEYKDTVMLGRTH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 172 GQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVdwhQFSEEFVTS-LGIQWNPYTTQIEP 250
Cdd:TIGR00928 145 GQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV---EEVEERVTEfLGLKPVPISTQIEP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 251 HDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIA--GEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKL 328
Cdd:TIGR00928 222 RDRHAELLDALALLATTLEKFAVDIRLLQRTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 329 PvSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEP---IQTVMRRYGIEKPYEK 404
Cdd:TIGR00928 302 P-LWHERDLTDSSVERViLPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASErvlIALVERGMGREEAYEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129094 405 LKELTRG-KRVDAEGMKQFIDGLA-LPEEEKARLKA--MTPANYIGRAITMVDEL 455
Cdd:TIGR00928 381 VRELAMGaAEVDEPDLLEFLLEDErITKYLKEEELAelLDPETYIGNAGEIVERV 435
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
12-455 |
0e+00 |
|
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: 536.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 12 VDGRYGDKvsALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevPAFAADAIgylDAIVASFsEEDAARIKTIERTTNH 91
Cdd:COG0015 2 ISPRYASP--EMRAIFSEEAKIRAWLDVEIALAEAQAELGLI---PAEAAAAI---RAAADDF-EIDAERIKEIEKETRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 92 DVKAVEYFLKEKVAEipelhAVSEFIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYRDIPLLSRTH 171
Cdd:COG0015 73 DVKAFVYALKEKVGA-----EAGEYIHFGATSQDINDTALALQLREALE-LLLPDLDALIAALAELAEEHKDTPMLGRTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 172 GQPATPSTIGKEMANVAYRMERQYRQLNQV---EILGKINGAVGNYNAHIAAypevdWHQFSEEFVTSLGIQWNPYTTQI 248
Cdd:COG0015 147 GQHAEPTTFGKKLAVWAAELLRQLERLEEArerVLVGKIGGAVGTYAAHGEA-----WPEVEERVAEKLGLKPNPVTTQI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 249 EPHDYIAELFDCVARFNTILIDFDRDVWGYIA--LNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLAS 326
Cdd:COG0015 222 EPRDRHAELFSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 327 KLpVSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWE-VLAEPIQTVMRRYGI--EKPY 402
Cdd:COG0015 302 AL-ASWHERDLSDSSVERNiLPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGlVLSEAVLMALVRRGLgrEEAY 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129094 403 EKLKELTRGKRVDAEGMKQFIDG-LALPEE-EKARLKAMT-PANYIGRAITMVDEL 455
Cdd:COG0015 381 ELVKELARGAWEEGNDLRELLAAdPEIPAElSKEELEALFdPANYLGAADEIVDRV 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
23-407 |
2.52e-153 |
|
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: 440.02 E-value: 2.52e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 23 LRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKevpafaADAIGYLDAIvASFSEEDAARIKTIERTTNHDVKAVEYFLKE 102
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIP------KEAAEEIRAA-ADVFEIDAERIAEIEKETGHDVIAFVYALAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 103 KVAEipelhAVSEFIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGK 182
Cdd:cd01595 74 KCGE-----DAGEYVHFGATSQDINDTALALQLRDALD-IILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 183 EMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPevDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCVA 262
Cdd:cd01595 148 KFAVWAAELLRHLERLEEARERVLVGGISGAVGTHASLGP--KGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 263 RFNTILIDFDRDVWGYI--ALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKLpVSRWQRDLTDS 340
Cdd:cd01595 226 LIAGTLEKIATDIRLLQrtEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDS 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129094 341 TVLRNLGVGIGYALIAYQSTLKGVSK-LEVNRDHLLDELDHNW-EVLAEPIQTVMRRYGI--EKPYEKLKE 407
Cdd:cd01595 305 SVERNILPDAFLLLDAALSRLQGLLEgLVVNPERMRRNLDLTWgLILSEAVMMALAKKGLgrQEAYELVKE 375
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
14-320 |
3.83e-108 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 322.40 E-value: 3.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 14 GRYGDKVSALRGIFSEYGLLKFRVQVE-VRWLQKLAAHAAIKEVPA--FAADAIGYLDAIVASFSEEDAARIKTIERTTN 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEdIKGLAALKKAAAKANVILkeEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 91 HDVKA-VEYFLKEKVAEipeLHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSR 169
Cdd:pfam00206 81 TAVNMnLNEVIGELLGQ---LVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKEKAKEFADIVKPGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 170 THGQPATPSTIGKE--MANVAYRMERQ-YRQLNQVEILGKINGAVGNYNAHIAAYP--EVDWHQFSeeFVTSLGiQWNPY 244
Cdd:pfam00206 158 THLQDATPVTLGQElsGYAVALTRDRErLQQLLPRLLVLPLGGGTAVGTGLNADPEfaELVAKELG--FFTGLP-VKAPN 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129094 245 T-TQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIA--LNHFKQKTIAGEIGSSTMPHKVNPIDFENseGNLGLSNAV 320
Cdd:pfam00206 235 SfEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLEL--LTGKAGRVM 311
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
33-370 |
3.13e-80 |
|
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: 251.27 E-value: 3.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 33 LKFRVQVEVRWLQklaAHAAIKEVPAFAADAIgylDAIVASFSEEDAARIKTIERTTNHDVKAVEYFLKEKVAEIPelha 112
Cdd:cd01334 1 IRADLQVEKAHAK---ALAELGLLPKEAAEAI---LAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELN---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 113 vSEFIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGKEMANVAYRME 192
Cdd:cd01334 71 -GGYVHTGRSSNDIVDTALRLALRDALD-ILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 193 RQYRQLNQVEILGKINGAV-GNYNAHIAAYPEvdwhqFSEEFVTSLGI-QWNPYTTQ-IEPHDYIAELFDCVARFNTILI 269
Cdd:cd01334 149 RDLERLEEALKRLNVLPLGgGAVGTGANAPPI-----DRERVAELLGFfGPAPNSTQaVSDRDFLVELLSALALLAVSLS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 270 DFDRDVWGYIA--LNHFKQKTiAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKLPVSRWqRDLTDSTVLRNLG 347
Cdd:cd01334 224 KIANDLRLLSSgeFGEVELPD-AKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPL-EDNVDSPVEREAL 301
|
330 340
....*....|....*....|....
gi 16129094 348 VGIGYALIAYQSTLKGV-SKLEVN 370
Cdd:cd01334 302 PDSFDLLDAALRLLTGVlEGLEVN 325
|
|
| ASL_C |
pfam08328 |
Adenylosuccinate lyase C-terminal; This domain is found at the C-terminus of adenylosuccinate ... |
331-445 |
1.40e-79 |
|
Adenylosuccinate lyase C-terminal; This domain is found at the C-terminus of adenylosuccinate lyase(ASL; PurB in E. coli). It has been identified in bacteria, eukaryotes and archaea and is found together with the lyase domain pfam00206. ASL catalyzes the cleavage of succinylaminoimidazole carboxamide ribotide to aminoimidazole carboxamide ribotide and fumarate and the cleavage of adenylosuccinate to adenylate and fumarate.
Pssm-ID: 462430 [Multi-domain] Cd Length: 115 Bit Score: 241.95 E-value: 1.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 331 SRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTR 410
Cdd:pfam08328 1 SRLQRDLTDSTVLRNIGVALGHSLIAYKSLLKGLGKLEVNEAALAADLDNNWEVLAEPIQTVMRRYGIPNPYEKLKELTR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 16129094 411 GKRVDAEGMKQFIDGLALPEEEKARLKAMTPANYI 445
Cdd:pfam08328 81 GKRITKESLREFIDSLDVPEEVKARLLALTPATYT 115
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
15-379 |
8.86e-46 |
|
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: 163.11 E-value: 8.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 15 RYGdkVSALRGIFSEYGLLKFRVQVEvrwLQKLAAHAAIKEVPAFAADAIgyldaivASFSEEDAARIKTIERTTNHDVK 94
Cdd:cd01360 1 RYG--RPEMKKIWSEENKFRKWLEVE---AAVCEAWAKLGVIPAEAAEEI-------RKKAKFDVERVKEIEAETKHDVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 95 AVEYFLKEKVAEipelhaVSEFIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQP 174
Cdd:cd01360 69 AFVTAIAEYCGE------AGRYIHFGLTSSDVVDTALALQLREALD-IILKDLKELLEVLKKKALEHKDTVMVGRTHGIH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 175 ATPSTIGKEMANVAYRMERQYRQLNQVE---ILGKINGAVGNYnAHIAayPEVdwhqfsEEFVT-SLGIQWNPYTTQIEP 250
Cdd:cd01360 142 AEPTTFGLKFALWYAEFKRHLERLKEAReriLVGKISGAVGTY-ANLG--PEV------EERVAeKLGLKPEPISTQVIQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 251 HDYIAELFdcvARFNTILIDFDRdvwgyIALN--HFkQKTIAGEI---------GSSTMPHKVNPIDFEN---------S 310
Cdd:cd01360 213 RDRHAEYL---STLALIASTLEK-----IATEirHL-QRTEVLEVeepfskgqkGSSAMPHKRNPILSENicglarvirS 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129094 311 EGNLGLSNAVLQHlasklpvsrwQRDLTDSTVLRnlgVGIGYALI----AYQSTLKGVSKLEVNRDHLLDELD 379
Cdd:cd01360 284 NVIPALENVALWH----------ERDISHSSVER---VILPDATIlldyILRRMTRVLENLVVYPENMRRNLN 343
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
96-361 |
7.97e-39 |
|
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: 140.05 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 96 VEYFLKEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEvILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPA 175
Cdd:cd01594 16 VEEVLAGRAGELAGGLHGSALVHKGRSSNDIGTTALRLALRDALDD-LLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 176 TPSTIGKEMANVAYRMERQYRQLNQVeilgkingavgnynahiaaypevdwhqfseefvtslgiqwnpyttqiephdYIA 255
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA---------------------------------------------------AVA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 256 ELFDCVARFNTILIDFDRDVWGYIALNHFKQKTI--AGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKLPVSrW 333
Cdd:cd01594 124 EALDALALAAAHLSKIAEDLRLLLSGEFGELGEPflPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGG-P 202
|
250 260
....*....|....*....|....*...
gi 16129094 334 QRDLTDSTVLRNLGVGIGYALIAYQSTL 361
Cdd:cd01594 203 ERDNEDSPSMREILADSLLLLIDALRLL 230
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
22-454 |
1.11e-32 |
|
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: 128.52 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 22 ALRGIFSEYGLLKFRVQVEVrwlqKLA-AHAAIKEVPAFAADAIgyldAIVASFSEEDAARIKTIERTTNHDVKAveyFL 100
Cdd:cd01597 10 AMREIFSDENRVQAMLDVEA----ALArAQAELGVIPKEAAAEI----AAAADVERLDLEALAEATARTGHPAIP---LV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 101 KEKVAEIPELHAvsEFIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTI 180
Cdd:cd01597 79 KQLTAACGDAAG--EYVHWGATTQDIIDTALVLQLRDALD-LLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 181 GKEMANVAYRMERQYRQLNQVE---ILGKINGAVGNYNAHIAAYPEVdwhqfSEEFVTSLGIQ--WNPYTTQiepHDYIA 255
Cdd:cd01597 156 GLKVAVWLSELLRHRERLDELRprvLVVQFGGAAGTLASLGDQGLAV-----QEALAAELGLGvpAIPWHTA---RDRIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 256 ELFDCVARFNTILIDFDRDVwgYI----ALNHFKQKTIAGEIGSSTMPHKVNPIdfeNSEGNLGLSNAVLQHLASKLP-- 329
Cdd:cd01597 228 ELASFLALLTGTLGKIARDV--YLlmqtEIGEVAEPFAKGRGGSSTMPHKRNPV---GCELIVALARRVPGLAALLLDam 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 330 VSRWQRDL----TDSTVLRNLGVGIGYALIAYQSTLKGvskLEVNRDHLLDELDHNWE-VLAEPiqtVMR----RYGIEK 400
Cdd:cd01597 303 VQEHERDAgawhAEWIALPEIFLLASGALEQAEFLLSG---LEVNEDRMRANLDLTGGlILSEA---VMMalapKLGRQE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129094 401 PYEKLKELTRgkRVDAEGmKQFIDGLA--------LPEEEkarLKAMT-PANYIGRAITMVDE 454
Cdd:cd01597 377 AHDLVYEACM--RAVEEG-RPLREVLLedpevaayLSDEE---LDALLdPANYLGSAPALVDR 433
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
86-344 |
6.49e-12 |
|
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: 66.96 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 86 ERTTNHDVKA-VEYF--LKEKVAEIpelhavsefIHFACTSEDINNLSHALMLKTARDeVILPYWRQLIDGIKDLAVQYR 162
Cdd:cd03302 65 EKKLRHDVMAhVHAFglLCPAAAGI---------IHLGATSCFVTDNTDLIQIRDALD-LILPKLAAVIDRLAEFALEYK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 163 DIPLLSRTHGQPATPSTIGKEMANVAYRM----ERQYRQLNQVEILGkINGAVGNYNAHIAAYpEVDWHQFS--EEFVTS 236
Cdd:cd03302 135 DLPTLGFTHYQPAQLTTVGKRACLWIQDLlmdlRNLERLRDDLRFRG-VKGTTGTQASFLDLF-EGDHDKVEalDELVTK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 237 -LGIQWN-PYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWgyiALNHFKQKT---IAGEIGSSTMPHKVNPIdfeNSE 311
Cdd:cd03302 213 kAGFKKVyPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIR---LLANLKEVEepfEKGQIGSSAMPYKRNPM---RSE 286
|
250 260 270
....*....|....*....|....*....|....*..
gi 16129094 312 GNLGLSNaVLQHLAS---KLPVSRW-QRDLTDSTVLR 344
Cdd:cd03302 287 RCCSLAR-HLMNLASnaaQTASTQWfERTLDDSANRR 322
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
281-446 |
7.27e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 58.89 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 281 LNHFKQKTIA-----GEIGSSTMPHKVNPIDFENSEgnlGLSNAVLQHLASKLP-VSRW-QRDLTDSTVLR----NLGVG 349
Cdd:PRK08937 40 LQRSEIREVEepfakGQKGSSAMPHKRNPIGSERIT---GLARVLRSYLVTALEnVPLWhERDLSHSSAERialpDAFLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 350 IGYALIAYQSTLKGvskLEVNRDHLLDELDHNWEVLAepIQTVM-----RRYGIEKPYEKLKELTrgkRVDAEGMKQFID 424
Cdd:PRK08937 117 LDYILNRFVNILEN---LVVFPENIERNLDKTLGFIA--TERVLlelveKGMGREEAHELIREKA---MEAWKNQKDLRE 188
|
170 180
....*....|....*....|....*...
gi 16129094 425 GLALPEEEKARL------KAMTPANYIG 446
Cdd:PRK08937 189 LLEADERFTKQLtkeeldELFDPEAFVG 216
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
47-308 |
1.88e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 58.91 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 47 LAAHAAIKEVPAFAAdAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAveyfLKEKVAE----IPEL-----HAVSE-- 115
Cdd:PRK05975 24 FSAEADIAAMLAFEA-ALAEAEAEHGIIPAEAAERIAAACETFEPDLAA----LRHATARdgvvVPALvrqlrAAVGEea 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 116 --FIHFACTSEDINNLSHALMLKTARdEVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGKEMANVAYRMER 193
Cdd:PRK05975 99 aaHVHFGATSQDVIDTSLMLRLKAAS-EILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 194 QYRQLNQVEILG---KINGAVGNYNAHIAAYPEVdwhqfSEEFVTSLGI----QWNpytTQiepHDYIAELFDCVARFNT 266
Cdd:PRK05975 178 HRDRLEALRADVfplQFGGAAGTLEKLGGKAAAV-----RARLAKRLGLedapQWH---SQ---RDFIADFAHLLSLVTG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16129094 267 ILIDFDRDvwgyIALnhFKQK----TIAGEIGSSTMPHKVNPIDFE 308
Cdd:PRK05975 247 SLGKFGQD----IAL--MAQAgdeiSLSGGGGSSAMPHKQNPVAAE 286
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
141-308 |
6.38e-07 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 51.61 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 141 EVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGKEM----ANVAYRMERQYRQLNQVEILGKINGAVGN-YN 215
Cdd:PLN00134 150 SRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFsgyaTQVKYGLNRVQCTLPRLYELAQGGTAVGTgLN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 216 AHIAaypevdwhqFSEEFVTSLGIQWN-PYTT---QIEP---HDYIAELFDCVARFNTILIDFDRDV----------WGY 278
Cdd:PLN00134 230 TKKG---------FDEKIAAAVAEETGlPFVTapnKFEAlaaHDAFVELSGALNTVAVSLMKIANDIrllgsgprcgLGE 300
|
170 180 190
....*....|....*....|....*....|
gi 16129094 279 IALNhfkqktiAGEIGSSTMPHKVNPIDFE 308
Cdd:PLN00134 301 LNLP-------ENEPGSSIMPGKVNPTQCE 323
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
141-304 |
1.72e-03 |
|
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: 40.56 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 141 EVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGKE----MANVAYRMERQYRQLNQVEILGkING-AVGN-Y 214
Cdd:cd01362 154 ERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEfsgyAAQLEHAIARIEAALPRLYELA-LGGtAVGTgL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129094 215 NAHIaaypevdwhQFSEEFVTSL----GIQW----NPYtTQIEPHDYIAELFdcvARFNTILIDFdrdvwgyialnhFKq 286
Cdd:cd01362 233 NAHP---------GFAEKVAAELaeltGLPFvtapNKF-EALAAHDALVEAS---GALKTLAVSL------------MK- 286
|
170 180 190
....*....|....*....|....*....|....*....
gi 16129094 287 ktIA--------------GEI-------GSSTMPHKVNP 304
Cdd:cd01362 287 --IAndirwlgsgprcglGELslpenepGSSIMPGKVNP 323
|
|
| |
