|
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: 1017.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 1 MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADANGYLDTLVANFNEEDAA 80
Cdd:PRK09285 1 MELSALTALSPLDGRYASKTAALRPIFSEFGLIRYRVQVEVEWLIALAAHPGIPEVPPFSAEANAFLRAIVENFSEEDAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 81 RIKTIERTTNHDVKAVEYFLKEKVADIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQ 160
Cdd:PRK09285 81 RIKEIERTTNHDVKAVEYFLKEKLAGLPELEAVSEFIHFACTSEDINNLSHALMLKEAREEVLLPALRELIDALKELAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 161 YRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ 240
Cdd:PRK09285 161 YADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVEILGKINGAVGNYNAHLAAYPEVDWHAFSREFVESLGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 241 WNPYTTQIEPHDYIAELFDCIARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV 320
Cdd:PRK09285 241 WNPYTTQIEPHDYIAELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGSSTMPHKVNPIDFENSEGNLGLANAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 321 LHHLANKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK 400
Cdd:PRK09285 321 LEHLAAKLPISRWQRDLTDSTVLRNLGVAFGYSLIAYDSLLKGLGKLEVNEARLAEDLDANWEVLAEPIQTVMRRYGIEN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446345911 401 PYEKLKELTRGKRVDAEGMKQFIDSLALPEAEKTRLKAMTPANYIGRAVTLVDELK 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: 819.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 23 LRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADANGYLDTLVANFNEEDAARIKTIERTTNHDVKAVEYFLKE 102
Cdd:cd01598 1 LRPYFSEYALIKYRVQVEVEWLIALSNLEEIPEVPPLTKEELKFLRAIIENFSEEDALRIKEIEATTNHDVKAVEYFLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 103 KVADIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGK 182
Cdd:cd01598 81 KFETLGLLKKIKEFIHFACTSEDINNLAYALMIKEARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 183 EMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCIA 262
Cdd:cd01598 161 ELAVFVYRLERQYKQLKQIEILGKFNGAVGNFNAHLVAYPDVDWRKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 263 RFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKLPVSRWQRDLTDSTV 342
Cdd:cd01598 241 RINTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAEGNLGLSNALLNHLSAKLPISRLQRDLTDSTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 343 LRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMKQF 422
Cdd:cd01598 321 LRNIGVAFGHSLIAYKSLLRGLDKLELNEARLLEDLDANWEVLAEPIQTVMRRYGIPNPYEKLKDLTRGKRIDKETLKEF 400
|
410 420
....*....|....*....|....
gi 446345911 423 IDSLALPEAEKTRLKAMTPANYIG 446
Cdd:cd01598 401 IDSLDIPEEAKAELLALTPANYIG 424
|
|
| 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: 535.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 12 VDGRYGDKvsALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevPAFAADAngyLDTLVANFnEEDAARIKTIERTTNH 91
Cdd:COG0015 2 ISPRYASP--EMRAIFSEEAKIRAWLDVEIALAEAQAELGLI---PAEAAAA---IRAAADDF-EIDAERIKEIEKETRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 92 DVKAVEYFLKEKVADipelhAVSEFIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTH 171
Cdd:COG0015 73 DVKAFVYALKEKVGA-----EAGEYIHFGATSQDINDTALALQLREALE-LLLPDLDALIAALAELAEEHKDTPMLGRTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 172 GQPATPSTLGKEMANVAYRMERQFRQLNQV---EILGKINGAVGNYNAHIAAypevdWHQFSEEFVTSLGIQWNPYTTQI 248
Cdd:COG0015 147 GQHAEPTTFGKKLAVWAAELLRQLERLEEArerVLVGKIGGAVGTYAAHGEA-----WPEVEERVAEKLGLKPNPVTTQI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 249 EPHDYIAELFDCIARFNTILIDFDRDVWGYIA--LNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLAN 326
Cdd:COG0015 222 EPRDRHAELFSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 327 KLpVSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWE-VLAEPIQTVMRRYGI--EKPY 402
Cdd:COG0015 302 AL-ASWHERDLSDSSVERNiLPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGlVLSEAVLMALVRRGLgrEEAY 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446345911 403 EKLKELTRGKRVDAEGMKQFIDS-LALPEA-EKTRLKAMT-PANYIGRAVTLVDEL 455
Cdd:COG0015 381 ELVKELARGAWEEGNDLRELLAAdPEIPAElSKEELEALFdPANYLGAADEIVDRV 436
|
|
| 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: 530.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 12 VDGRYGdkVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevpafAADANGYLDTlVANFNEEDAARIKTIERTTNH 91
Cdd:TIGR00928 1 LDERYG--SPEMRAIWSEENKFKTWLDVEVAVLRALAELGVI------PAEAVKEIRE-KANFTEVDLERIKEIEAVTRH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 92 DVKAVEYFLKEKVAdipelhAVSEFIHFACTSEDINNLSHALMLKTArDEVVLPYWRKLIDAVKDLSVQYRDIPLLSRTH 171
Cdd:TIGR00928 72 DVKAVVYALKEKCG------AEGEFIHFGATSNDIVDTALALLLRDA-LEIILPKLKQLIDRLKELAVEYKDTVMLGRTH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 172 GQPATPSTLGKEMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVdwhQFSEEFVTS-LGIQWNPYTTQIEP 250
Cdd:TIGR00928 145 GQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV---EEVEERVTEfLGLKPVPISTQIEP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 251 HDYIAELFDCIARFNTILIDFDRDVWGYIALNHFKQKTIA--GEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKL 328
Cdd:TIGR00928 222 RDRHAELLDALALLATTLEKFAVDIRLLQRTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 329 PvSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEP---IQTVMRRYGIEKPYEK 404
Cdd:TIGR00928 302 P-LWHERDLTDSSVERViLPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASErvlIALVERGMGREEAYEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446345911 405 LKELTRG-KRVDAEGMKQFIDSLA-LPEAEKTRLKA--MTPANYIGRAVTLVDEL 455
Cdd:TIGR00928 381 VRELAMGaAEVDEPDLLEFLLEDErITKYLKEEELAelLDPETYIGNAGEIVERV 435
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
14-320 |
2.71e-104 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 312.77 E-value: 2.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 14 GRYGDKVSALRGIFSEYGLLKFRVQVE-VRWLQKLAAHAAIKEVPA--FAADANGYLDTLVANFNEEDAARIKTIERTTN 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEdIKGLAALKKAAAKANVILkeEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 91 HDVKA-VEYFLKEKVAdipELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQYRDIPLLSR 169
Cdd:pfam00206 81 TAVNMnLNEVIGELLG---QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKEKAKEFADIVKPGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 170 THGQPATPSTLGKE--MANVAYRMERQ-FRQLNQVEILGKINGAVGNYNAHIAAYP--EVDWHQFSeeFVTSLGiQWNPY 244
Cdd:pfam00206 158 THLQDATPVTLGQElsGYAVALTRDRErLQQLLPRLLVLPLGGGTAVGTGLNADPEfaELVAKELG--FFTGLP-VKAPN 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446345911 245 T-TQIEPHDYIAELFDCIARFNTILIDFDRDVWGYIA--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: 1017.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 1 MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADANGYLDTLVANFNEEDAA 80
Cdd:PRK09285 1 MELSALTALSPLDGRYASKTAALRPIFSEFGLIRYRVQVEVEWLIALAAHPGIPEVPPFSAEANAFLRAIVENFSEEDAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 81 RIKTIERTTNHDVKAVEYFLKEKVADIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQ 160
Cdd:PRK09285 81 RIKEIERTTNHDVKAVEYFLKEKLAGLPELEAVSEFIHFACTSEDINNLSHALMLKEAREEVLLPALRELIDALKELAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 161 YRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ 240
Cdd:PRK09285 161 YADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVEILGKINGAVGNYNAHLAAYPEVDWHAFSREFVESLGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 241 WNPYTTQIEPHDYIAELFDCIARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV 320
Cdd:PRK09285 241 WNPYTTQIEPHDYIAELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGSSTMPHKVNPIDFENSEGNLGLANAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 321 LHHLANKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK 400
Cdd:PRK09285 321 LEHLAAKLPISRWQRDLTDSTVLRNLGVAFGYSLIAYDSLLKGLGKLEVNEARLAEDLDANWEVLAEPIQTVMRRYGIEN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446345911 401 PYEKLKELTRGKRVDAEGMKQFIDSLALPEAEKTRLKAMTPANYIGRAVTLVDELK 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: 819.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 23 LRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADANGYLDTLVANFNEEDAARIKTIERTTNHDVKAVEYFLKE 102
Cdd:cd01598 1 LRPYFSEYALIKYRVQVEVEWLIALSNLEEIPEVPPLTKEELKFLRAIIENFSEEDALRIKEIEATTNHDVKAVEYFLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 103 KVADIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGK 182
Cdd:cd01598 81 KFETLGLLKKIKEFIHFACTSEDINNLAYALMIKEARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 183 EMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCIA 262
Cdd:cd01598 161 ELAVFVYRLERQYKQLKQIEILGKFNGAVGNFNAHLVAYPDVDWRKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 263 RFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKLPVSRWQRDLTDSTV 342
Cdd:cd01598 241 RINTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAEGNLGLSNALLNHLSAKLPISRLQRDLTDSTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 343 LRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMKQF 422
Cdd:cd01598 321 LRNIGVAFGHSLIAYKSLLRGLDKLELNEARLLEDLDANWEVLAEPIQTVMRRYGIPNPYEKLKDLTRGKRIDKETLKEF 400
|
410 420
....*....|....*....|....
gi 446345911 423 IDSLALPEAEKTRLKAMTPANYIG 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 446345911 1 MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADANGYLDTLVANFNEEDAA 80
Cdd:PLN02848 4 LELSNLTALSPLDGRYWSKVKDLRPIFSEFGLIRYRVLVEVKWLLKLSQIPEVTEVPPFSDEANSFLEGIIAGFSVDDAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 81 RIKTIERTTNHDVKAVEYFLKEKVADIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQ 160
Cdd:PLN02848 84 EVKKIERVTNHDVKAVEYFLKQKCKSHPELAKVLEFFHFACTSEDINNLSHALMLKEGVNSVVLPTMDEIIKAISSLAHE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 161 YRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ 240
Cdd:PLN02848 164 FAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVKIKGKFAGAVGNYNAHMSAYPEVDWPAVAEEFVTSLGLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 241 WNPYTTQIEPHDYIAELFDCIARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV 320
Cdd:PLN02848 244 FNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWSYISLGYFKQITKAGEVGSSTMPHKVNPIDFENSEGNLGLANAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 321 LHHLANKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK 400
Cdd:PLN02848 324 LSHLSMKLPISRMQRDLTDSTVLRNMGVGLGHSLLAYKSTLRGIGKLQVNEARLAEDLDQTWEVLAEPIQTVMRRYGVPE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446345911 401 PYEKLKELTRGKRVDAEGMKQFIDSLALPEAEKTRLKAMTPANYIGRAVTL 451
Cdd:PLN02848 404 PYEKLKELTRGRAVTKESMREFIEGLELPEEAKDQLLKLTPHTYIGAAAAL 454
|
|
| 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: 535.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 12 VDGRYGDKvsALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevPAFAADAngyLDTLVANFnEEDAARIKTIERTTNH 91
Cdd:COG0015 2 ISPRYASP--EMRAIFSEEAKIRAWLDVEIALAEAQAELGLI---PAEAAAA---IRAAADDF-EIDAERIKEIEKETRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 92 DVKAVEYFLKEKVADipelhAVSEFIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTH 171
Cdd:COG0015 73 DVKAFVYALKEKVGA-----EAGEYIHFGATSQDINDTALALQLREALE-LLLPDLDALIAALAELAEEHKDTPMLGRTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 172 GQPATPSTLGKEMANVAYRMERQFRQLNQV---EILGKINGAVGNYNAHIAAypevdWHQFSEEFVTSLGIQWNPYTTQI 248
Cdd:COG0015 147 GQHAEPTTFGKKLAVWAAELLRQLERLEEArerVLVGKIGGAVGTYAAHGEA-----WPEVEERVAEKLGLKPNPVTTQI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 249 EPHDYIAELFDCIARFNTILIDFDRDVWGYIA--LNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLAN 326
Cdd:COG0015 222 EPRDRHAELFSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 327 KLpVSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWE-VLAEPIQTVMRRYGI--EKPY 402
Cdd:COG0015 302 AL-ASWHERDLSDSSVERNiLPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGlVLSEAVLMALVRRGLgrEEAY 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446345911 403 EKLKELTRGKRVDAEGMKQFIDS-LALPEA-EKTRLKAMT-PANYIGRAVTLVDEL 455
Cdd:COG0015 381 ELVKELARGAWEEGNDLRELLAAdPEIPAElSKEELEALFdPANYLGAADEIVDRV 436
|
|
| 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: 530.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 12 VDGRYGdkVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIkevpafAADANGYLDTlVANFNEEDAARIKTIERTTNH 91
Cdd:TIGR00928 1 LDERYG--SPEMRAIWSEENKFKTWLDVEVAVLRALAELGVI------PAEAVKEIRE-KANFTEVDLERIKEIEAVTRH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 92 DVKAVEYFLKEKVAdipelhAVSEFIHFACTSEDINNLSHALMLKTArDEVVLPYWRKLIDAVKDLSVQYRDIPLLSRTH 171
Cdd:TIGR00928 72 DVKAVVYALKEKCG------AEGEFIHFGATSNDIVDTALALLLRDA-LEIILPKLKQLIDRLKELAVEYKDTVMLGRTH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 172 GQPATPSTLGKEMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPEVdwhQFSEEFVTS-LGIQWNPYTTQIEP 250
Cdd:TIGR00928 145 GQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV---EEVEERVTEfLGLKPVPISTQIEP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 251 HDYIAELFDCIARFNTILIDFDRDVWGYIALNHFKQKTIA--GEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKL 328
Cdd:TIGR00928 222 RDRHAELLDALALLATTLEKFAVDIRLLQRTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 329 PvSRWQRDLTDSTVLRN-LGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEP---IQTVMRRYGIEKPYEK 404
Cdd:TIGR00928 302 P-LWHERDLTDSSVERViLPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASErvlIALVERGMGREEAYEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446345911 405 LKELTRG-KRVDAEGMKQFIDSLA-LPEAEKTRLKA--MTPANYIGRAVTLVDEL 455
Cdd:TIGR00928 381 VRELAMGaAEVDEPDLLEFLLEDErITKYLKEEELAelLDPETYIGNAGEIVERV 435
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
23-407 |
1.79e-152 |
|
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: 438.09 E-value: 1.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 23 LRGIFSEYGLLKFRVQVEVRWLQklaAHAAIKEVPAFAADAngyLDTlVANFNEEDAARIKTIERTTNHDVKAVEYFLKE 102
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAE---AQAELGLIPKEAAEE---IRA-AADVFEIDAERIAEIEKETGHDVIAFVYALAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 103 KVADipelhAVSEFIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGK 182
Cdd:cd01595 74 KCGE-----DAGEYVHFGATSQDINDTALALQLRDALD-IILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 183 EMANVAYRMERQFRQLNQVEILGKINGAVGNYNAHIAAYPevDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCIA 262
Cdd:cd01595 148 KFAVWAAELLRHLERLEEARERVLVGGISGAVGTHASLGP--KGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 263 RFNTILIDFDRDVWGYI--ALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKLpVSRWQRDLTDS 340
Cdd:cd01595 226 LIAGTLEKIATDIRLLQrtEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDS 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446345911 341 TVLRNLGVGIGYALIAYQSTLKGVSK-LEVNRDHLLDELDHNW-EVLAEPIQTVMRRYGI--EKPYEKLKE 407
Cdd:cd01595 305 SVERNILPDAFLLLDAALSRLQGLLEgLVVNPERMRRNLDLTWgLILSEAVMMALAKKGLgrQEAYELVKE 375
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
14-320 |
2.71e-104 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 312.77 E-value: 2.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 14 GRYGDKVSALRGIFSEYGLLKFRVQVE-VRWLQKLAAHAAIKEVPA--FAADANGYLDTLVANFNEEDAARIKTIERTTN 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEdIKGLAALKKAAAKANVILkeEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 91 HDVKA-VEYFLKEKVAdipELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLSVQYRDIPLLSR 169
Cdd:pfam00206 81 TAVNMnLNEVIGELLG---QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKEKAKEFADIVKPGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 170 THGQPATPSTLGKE--MANVAYRMERQ-FRQLNQVEILGKINGAVGNYNAHIAAYP--EVDWHQFSeeFVTSLGiQWNPY 244
Cdd:pfam00206 158 THLQDATPVTLGQElsGYAVALTRDRErLQQLLPRLLVLPLGGGTAVGTGLNADPEfaELVAKELG--FFTGLP-VKAPN 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446345911 245 T-TQIEPHDYIAELFDCIARFNTILIDFDRDVWGYIA--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 |
2.36e-79 |
|
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: 248.96 E-value: 2.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 33 LKFRVQVEVRWLQklaAHAAIKEVPAFAADAngyLDTLVANFNEEDAARIKTIERTTNHDVKAVEYFLKEKVADIPelha 112
Cdd:cd01334 1 IRADLQVEKAHAK---ALAELGLLPKEAAEA---ILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELN---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 113 vSEFIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMANVAYRME 192
Cdd:cd01334 71 -GGYVHTGRSSNDIVDTALRLALRDALD-ILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 193 RQFRQLNQVEILGKINGAV-GNYNAHIAAYPEvdwhqFSEEFVTSLGI-QWNPYTTQ-IEPHDYIAELFDCIARFNTILI 269
Cdd:cd01334 149 RDLERLEEALKRLNVLPLGgGAVGTGANAPPI-----DRERVAELLGFfGPAPNSTQaVSDRDFLVELLSALALLAVSLS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 270 DFDRDVWGYIA--LNHFKQKTiAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKLPVSRWqRDLTDSTVLRNLG 347
Cdd:cd01334 224 KIANDLRLLSSgeFGEVELPD-AKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPL-EDNVDSPVEREAL 301
|
330 340
....*....|....*....|....
gi 446345911 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 |
7.48e-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: 240.03 E-value: 7.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 331 SRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTR 410
Cdd:pfam08328 1 SRLQRDLTDSTVLRNIGVALGHSLIAYKSLLKGLGKLEVNEAALAADLDNNWEVLAEPIQTVMRRYGIPNPYEKLKELTR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 446345911 411 GKRVDAEGMKQFIDSLALPEAEKTRLKAMTPANYI 445
Cdd:pfam08328 81 GKRITKESLREFIDSLDVPEEVKARLLALTPATYT 115
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
15-379 |
9.67e-45 |
|
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: 160.41 E-value: 9.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 15 RYGdkVSALRGIFSEYGLLKFRVQVEvrwLQKLAAHAAIKEVPAFAADangyldtLVANFNEEDAARIKTIERTTNHDVK 94
Cdd:cd01360 1 RYG--RPEMKKIWSEENKFRKWLEVE---AAVCEAWAKLGVIPAEAAE-------EIRKKAKFDVERVKEIEAETKHDVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 95 AVEYFLKEKVADipelhaVSEFIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQP 174
Cdd:cd01360 69 AFVTAIAEYCGE------AGRYIHFGLTSSDVVDTALALQLREALD-IILKDLKELLEVLKKKALEHKDTVMVGRTHGIH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 175 ATPSTLGKEMANVAYRMERQFRQLNQV--EIL-GKINGAVGNYnAHIAayPEVdwhqfsEEFVT-SLGIQWNPYTTQIEP 250
Cdd:cd01360 142 AEPTTFGLKFALWYAEFKRHLERLKEAreRILvGKISGAVGTY-ANLG--PEV------EERVAeKLGLKPEPISTQVIQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 251 HDYIAELFDCIArfnTILIDFDRdvwgyIALN--HFkQKTIAGEI---------GSSTMPHKVNPIDFEN---------S 310
Cdd:cd01360 213 RDRHAEYLSTLA---LIASTLEK-----IATEirHL-QRTEVLEVeepfskgqkGSSAMPHKRNPILSENicglarvirS 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446345911 311 EGNLGLSNAVLHHlanklpvsrwQRDLTDSTVLRnlgVGIGYALI----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 |
4.74e-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: 140.82 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 96 VEYFLKEKVADIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVvLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPA 175
Cdd:cd01594 16 VEEVLAGRAGELAGGLHGSALVHKGRSSNDIGTTALRLALRDALDDL-LPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 176 TPSTLGKEMANVAYRMERQFRQLNQVeilgkingavgnynahiaaypevdwhqfseefvtslgiqwnpyttqiephdYIA 255
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA---------------------------------------------------AVA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 256 ELFDCIARFNTILIDFDRDVWGYIALNHFKQKTI--AGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLHHLANKLPVSrW 333
Cdd:cd01594 124 EALDALALAAAHLSKIAEDLRLLLSGEFGELGEPflPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGG-P 202
|
250 260
....*....|....*....|....*...
gi 446345911 334 QRDLTDSTVLRNLGVGIGYALIAYQSTL 361
Cdd:cd01594 203 ERDNEDSPSMREILADSLLLLIDALRLL 230
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
22-454 |
7.17e-30 |
|
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: 120.81 E-value: 7.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 22 ALRGIFSEYGLLKFRVQVEVrwlqKLA-AHAAIKEVPAFAADAngylDTLVANFNEEDAARIKTIERTTNHDVKAveyFL 100
Cdd:cd01597 10 AMREIFSDENRVQAMLDVEA----ALArAQAELGVIPKEAAAE----IAAAADVERLDLEALAEATARTGHPAIP---LV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 101 KEKVADIPELHAvsEFIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTL 180
Cdd:cd01597 79 KQLTAACGDAAG--EYVHWGATTQDIIDTALVLQLRDALD-LLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 181 GKEMANVAYRMERQFRQLNQVE---ILGKINGAVGNYNAHIAAYPEVdwhqfSEEFVTSLGIQ--WNPYTTQiepHDYIA 255
Cdd:cd01597 156 GLKVAVWLSELLRHRERLDELRprvLVVQFGGAAGTLASLGDQGLAV-----QEALAAELGLGvpAIPWHTA---RDRIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 256 ELFDCIARFNTILIDFDRDVwgYI----ALNHFKQKTIAGEIGSSTMPHKVNPIdfeNSEGNLGLSNAVLHHLANKLP-- 329
Cdd:cd01597 228 ELASFLALLTGTLGKIARDV--YLlmqtEIGEVAEPFAKGRGGSSTMPHKRNPV---GCELIVALARRVPGLAALLLDam 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 330 VSRWQRDL----TDSTVLRNLGVGIGYALIAYQSTLKGvskLEVNRDHLLDELDHNWE-VLAEPiqtVMR----RYGIEK 400
Cdd:cd01597 303 VQEHERDAgawhAEWIALPEIFLLASGALEQAEFLLSG---LEVNEDRMRANLDLTGGlILSEA---VMMalapKLGRQE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 401 PYEKLKELTRgkRVDAEGmKQFIDSLA-LPEA----EKTRLKAMT-PANYIGRAVTLVDE 454
Cdd:cd01597 377 AHDLVYEACM--RAVEEG-RPLREVLLeDPEVaaylSDEELDALLdPANYLGSAPALVDR 433
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
67-344 |
1.11e-11 |
|
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: 66.57 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 67 LDTLVANFNEEDAARIKTIERTTNHDVKA-VEYFlkekVADIPELHAVsefIHFACTSEDINNLSHALMLKTARDeVVLP 145
Cdd:cd03302 46 IEEMKANVENIDFEIAAAEEKKLRHDVMAhVHAF----GLLCPAAAGI---IHLGATSCFVTDNTDLIQIRDALD-LILP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 146 YWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVE---ILGKINGAVGNYNAHIAAYp 222
Cdd:cd03302 118 KLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRddlRFRGVKGTTGTQASFLDLF- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 223 EVDWHQFS--EEFVTS-LGIQWN-PYTTQIEPHDYIAELFDCIARFNTILIDFDRDVWgyiALNHFKQKT---IAGEIGS 295
Cdd:cd03302 197 EGDHDKVEalDELVTKkAGFKKVyPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIR---LLANLKEVEepfEKGQIGS 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446345911 296 STMPHKVNPIdfeNSEGNLGLSNAVLHHLANKLPVS--RW-QRDLTDSTVLR 344
Cdd:cd03302 274 SAMPYKRNPM---RSERCCSLARHLMNLASNAAQTAstQWfERTLDDSANRR 322
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
281-446 |
3.83e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 59.66 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 281 LNHFKQKTIA-----GEIGSSTMPHKVNPIDFENSEgnlGLSNAVLHHLANKLP-VSRW-QRDLTDSTVLR----NLGVG 349
Cdd:PRK08937 40 LQRSEIREVEepfakGQKGSSAMPHKRNPIGSERIT---GLARVLRSYLVTALEnVPLWhERDLSHSSAERialpDAFLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 350 IGYALIAYQSTLKGvskLEVNRDHLLDELDHNWEVLAepIQTVM-----RRYGIEKPYEKLKELTrgkRVDAEGMKQFID 424
Cdd:PRK08937 117 LDYILNRFVNILEN---LVVFPENIERNLDKTLGFIA--TERVLlelveKGMGREEAHELIREKA---MEAWKNQKDLRE 188
|
170 180
....*....|....*....|....*...
gi 446345911 425 SLALPEAEKTRL------KAMTPANYIG 446
Cdd:PRK08937 189 LLEADERFTKQLtkeeldELFDPEAFVG 216
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
116-305 |
1.06e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 60.41 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 116 FIHFACTSEDINNLSHALMLKTARDeVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQF 195
Cdd:PRK09053 101 YVHWGATSQDIIDTGLVLQLRDALD-LLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 196 RQLN----QVEILgKINGAVGNYNAHIAAYPEVdwhqfSEEFVTSLGIQW--NPYTTQiepHDYIAELFDCIARFNTILI 269
Cdd:PRK09053 180 QRLAalrpRALVL-QFGGAAGTLASLGEQALPV-----AQALAAELQLALpaLPWHTQ---RDRIAEFASALGLLAGTLG 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446345911 270 DFDRDVwgyialnHFKQKTIAGEI---------GSSTMPHKVNPI 305
Cdd:PRK09053 251 KIARDV-------SLLMQTEVGEVfepaaagkgGSSTMPHKRNPV 288
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
141-308 |
1.21e-08 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 57.01 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 141 EVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEM----ANVAYRMERQFRQLNQVEILGKINGAVGN-YN 215
Cdd:PLN00134 150 SRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFsgyaTQVKYGLNRVQCTLPRLYELAQGGTAVGTgLN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 216 AHIAaypevdwhqFSEEFVTSLGIQWN-PYTT---QIEP---HDYIAELFDCIARFNTILIDFDRDV----------WGY 278
Cdd:PLN00134 230 TKKG---------FDEKIAAAVAEETGlPFVTapnKFEAlaaHDAFVELSGALNTVAVSLMKIANDIrllgsgprcgLGE 300
|
170 180 190
....*....|....*....|....*....|
gi 446345911 279 IALNhfkqktiAGEIGSSTMPHKVNPIDFE 308
Cdd:PLN00134 301 LNLP-------ENEPGSSIMPGKVNPTQCE 323
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
76-308 |
2.77e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 52.36 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 76 EEDAARIKTIERTTNHDVKAveyfLKEKVAD----IPEL-----HAVSE----FIHFACTSEDINNLSHALMLKTARdEV 142
Cdd:PRK05975 52 AEAAERIAAACETFEPDLAA----LRHATARdgvvVPALvrqlrAAVGEeaaaHVHFGATSQDVIDTSLMLRLKAAS-EI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 143 VLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVEILG---KINGAVGNYNAHIA 219
Cdd:PRK05975 127 LAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRADVfplQFGGAAGTLEKLGG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 220 AYPEVdwhqfSEEFVTSLGI----QWNpytTQiepHDYIAELFDCIARFNTILIDFDRDvwgyIALnhFKQK----TIAG 291
Cdd:PRK05975 207 KAAAV-----RARLAKRLGLedapQWH---SQ---RDFIADFAHLLSLVTGSLGKFGQD----IAL--MAQAgdeiSLSG 269
|
250
....*....|....*..
gi 446345911 292 EIGSSTMPHKVNPIDFE 308
Cdd:PRK05975 270 GGGSSAMPHKQNPVAAE 286
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
141-304 |
2.35e-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: 43.26 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 141 EVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVEI------LGkinG-AVGN 213
Cdd:cd01362 154 ERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPrlyelaLG---GtAVGT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 214 -YNAHIaaypevdwhQFSEEFVTSL----GIQW----NPYtTQIEPHDYIAELFdciARFNTILIDFdrdvwgyialnhF 284
Cdd:cd01362 231 gLNAHP---------GFAEKVAAELaeltGLPFvtapNKF-EALAAHDALVEAS---GALKTLAVSL------------M 285
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446345911 285 KqktIA--------------GEI-------GSSTMPHKVNP 304
Cdd:cd01362 286 K---IAndirwlgsgprcglGELslpenepGSSIMPGKVNP 323
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
141-304 |
2.05e-03 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 40.46 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 141 EVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMAnvAYRmeRQFRQ-LNQVEILGK------ING-AVG 212
Cdd:PRK00485 158 ERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFS--GYA--AQLEHgIERIEAALPhlyelaLGGtAVG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 213 N-YNAHiaayPEvdwhqFSEEFVtslgiqwnpyttqiephDYIAELFDciarfntilIDFdrdvwgYIALNHFKQ----- 286
Cdd:PRK00485 234 TgLNAH----PG-----FAERVA-----------------EELAELTG---------LPF------VTAPNKFEAlaahd 272
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446345911 287 ---------KTIA---------------------GEI-------GSSTMPHKVNP 304
Cdd:PRK00485 273 alveasgalKTLAvslmkiandirwlasgprcglGEIslpenepGSSIMPGKVNP 327
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
141-304 |
4.95e-03 |
|
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: 39.33 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 141 EVVLPYWRKLIDAVKDLSVQYRDIPLLSRTHGQPATPSTLGKEMANVAYRMERQFRQLNQVEI-LGKIN-G--AVGN-YN 215
Cdd:cd01596 153 ERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALErLRELNlGgtAVGTgLN 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446345911 216 AHiaaypevdwHQFSEEFVTSL----GIQWNPYTTQIEP---HDYIAELFdciARFNTilidfdrdvwgyIALNHFKqkt 288
Cdd:cd01596 233 AP---------PGYAEKVAAELaeltGLPFVTAPNLFEAtaaHDALVEVS---GALKT------------LAVSLSK--- 285
|
170 180 190
....*....|....*....|....*....|....*..
gi 446345911 289 IA--------------GEI-------GSSTMPHKVNP 304
Cdd:cd01596 286 IAndlrllssgpraglGEInlpanqpGSSIMPGKVNP 322
|
|
| |
