|
Name |
Accession |
Description |
Interval |
E-value |
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
10-446 |
0e+00 |
|
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: 594.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 10 LLKNLWSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLEKLDMDFILEQVRLTRHPLVPTIRG 89
Cdd:cd01597 1 LLGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATARTGHPAIPLVKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 90 LEHACPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTA 169
Cdd:cd01597 81 LTAACGDAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 170 IWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLGTPEISWQPARDRFSEYGMLIGLISGTL 249
Cdd:cd01597 161 VWLSELLRHRERLDELRPRVLVVQFGGAAGTLASLGDQGLAVQEALAAELGLGVPAIPWHTARDRIAELASFLALLTGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 250 GKIANEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKVM 329
Cdd:cd01597 241 GKIARDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 330 PEMCLMLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDKAGKQTAHEIVYEASMSGQEEGITFIEAIN 409
Cdd:cd01597 321 PEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLL 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 1236168651 410 RDTRIRDHITQEELDALLDPTTYVGNAPEQVTRVIEQ 446
Cdd:cd01597 401 EDPEVAAYLSDEELDALLDPANYLGSAPALVDRVLAR 437
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
10-443 |
3.96e-179 |
|
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: 507.70 E-value: 3.96e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 10 LLKNLWSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLEKLDMDFILEQVRLTRHPLVPTIRG 89
Cdd:COG0015 1 LISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 90 LEHACPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTA 169
Cdd:COG0015 81 LKEKVGAEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 170 IWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLG-TPEISWQPARDRFSEYGMLIGLISGT 248
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEAWPEVEERVAEKLGLKpNPVTTQIEPRDRHAELFSALALIAGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 249 LGKIANEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKV 328
Cdd:COG0015 241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 329 MPEMCLMLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDK-AGKQTAHEIVYEASMSGQEEGITFIEA 407
Cdd:COG0015 321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRgLGREEAYELVKELARGAWEEGNDLREL 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1236168651 408 INRDTRIRDHITQEELDALLDPTTYVGNAPEQVTRV 443
Cdd:COG0015 401 LAADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
20-398 |
9.82e-155 |
|
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: 443.87 E-value: 9.82e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 20 MRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLEKLDMDFILEQVRLTRHPLVPTIRGLEHACPEHFG 99
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVFEIDAERIAEIEKETGHDVIAFVYALAEKCGEDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 100 EYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARHY 179
Cdd:cd01595 81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 180 QRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLGTPEISWQ-PARDRFSEYGMLIGLISGTLGKIANEILL 258
Cdd:cd01595 161 ERLEEARERVLVGGISGAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQiEPRDRIAELLSALALIAGTLEKIATDIRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 259 LAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKVMPEMCLMLSV 338
Cdd:cd01595 241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236168651 339 IFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDK-AGKQTAHEIVYEASMSGQ 398
Cdd:cd01595 321 ALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKgLGRQEAYELVKEENYLGL 381
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
10-444 |
1.26e-126 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 374.74 E-value: 1.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 10 LLKNLWSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLEKLDMDFILEQVRLTRHPLVPTIRG 89
Cdd:PRK09053 7 LTDLYFGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALAGNLAIPLVKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 90 LEHACPEHFGE---YVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGH 166
Cdd:PRK09053 87 LTAQVAARDAEaarYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 167 KTAIWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLGTPEISWQPARDRFSEYGMLIGLIS 246
Cdd:PRK09053 167 KFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLGEQALPVAQALAAELQLALPALPWHTQRDRIAEFASALGLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 247 GTLGKIANEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPaiVENAACVSNTLKAN--LSVLTDMMKHQHERDGAIWKM 324
Cdd:PRK09053 247 GTLGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNP--VGCAAVLTAATRAPglVATLFAAMPQEHERALGGWHA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 325 EWKVMPEMCLMLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDKAGKQTAHEIVYEASMSGQEEGITF 404
Cdd:PRK09053 325 EWDTLPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADRIGRLDAHHLVEQASKRAVAEGRHL 404
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1236168651 405 IEAINRDTRIRDHITQEELDALLDPTTYVGNAPEQVTRVI 444
Cdd:PRK09053 405 RDVLAEDPQVSAHLSPAALDRLLDPAHYLGQAHAWVDRVL 444
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
15-443 |
2.83e-113 |
|
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: 340.09 E-value: 2.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 15 WSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLEKLDMDFILEQVRLTRHPLVPTIRGLEHAC 94
Cdd:TIGR00928 5 YGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYALKEKC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 95 PEHfGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTE 174
Cdd:TIGR00928 85 GAE-GEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 175 LARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLGTPEISWQ-PARDRFSEYGMLIGLISGTLGKIA 253
Cdd:TIGR00928 164 MLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVEEVEERVTEFLGLKPVPISTQiEPRDRHAELLDALALLATTLEKFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 254 NEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKVMPEMC 333
Cdd:TIGR00928 244 VDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILPDAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 334 LMLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDK-AGKQTAHEIVYEASMSGQE-EGITFIEAINRD 411
Cdd:TIGR00928 324 ILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERgMGREEAYEIVRELAMGAAEvDEPDLLEFLLED 403
|
410 420 430
....*....|....*....|....*....|..
gi 1236168651 412 TRIRDHITQEELDALLDPTTYVGNAPEQVTRV 443
Cdd:TIGR00928 404 ERITKYLKEEELAELLDPETYIGNAGEIVERV 435
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
16-390 |
8.40e-106 |
|
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: 319.11 E-value: 8.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 16 STEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLeklDMDFILEQVRLTRHPLVPTIRGLEHACP 95
Cdd:cd01360 3 GRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKF---DVERVKEIEAETKHDVIAFVTAIAEYCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 96 EHfGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTEL 175
Cdd:cd01360 80 EA-GRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 176 ARHYQRLKEIEPRLFVGSVVGAVGTKASLSdkaDELEVRVLNRLGLGTPEISWQPA-RDRFSEYGMLIGLISGTLGKIAN 254
Cdd:cd01360 159 KRHLERLKEARERILVGKISGAVGTYANLG---PEVEERVAEKLGLKPEPISTQVIqRDRHAEYLSTLALIASTLEKIAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 255 EILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKVMPEMCL 334
Cdd:cd01360 236 EIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATI 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1236168651 335 MLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDK-AGKQTAHEIV 390
Cdd:cd01360 316 LLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKgMSREEAYEIV 372
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
10-350 |
4.58e-94 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
Pssm-ID: 274128 [Multi-domain] Cd Length: 338 Bit Score: 287.41 E-value: 4.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 10 LLKNLWSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIADTAKLEKLDMDFILEQVRLTRHPLVPTIRG 89
Cdd:TIGR02426 1 LLDGLFGDPAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAAAAPDLEALAHAAATAGNPVIPLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 90 LEHACPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTA 169
Cdd:TIGR02426 81 LRKAVAGEAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 170 IWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLGTPEISWQPARDRFSEYGMLIGLISGTL 249
Cdd:TIGR02426 161 GWLAAVLRARDRLAALRTRALPLQFGGAAGTLAALGTRGGAVAAALAARLGLPLPALPWHTQRDRIAEFGSALALVAGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 250 GKIANEILLLAHNEIDELsepFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKVM 329
Cdd:TIGR02426 241 GKIAGDIALLSQTEVGEV---FEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETL 317
|
330 340
....*....|....*....|.
gi 1236168651 330 PEMCLMLSVIFDNMKTVLGGL 350
Cdd:TIGR02426 318 PELVRLTGGALRQAQVLAEGL 338
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
31-353 |
2.76e-92 |
|
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: 282.47 E-value: 2.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 31 QNWLDYEAALAIEQAELGLIPKQAAEVI---ADTAKLEKLDMDFILEQVrlTRHPLVPTIRGLEHACPEHFGEYVHFGPT 107
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAIlaaLDEILEGIAADQVEQEGS--GTHDVMAVEEVLAERAGELNGGYVHTGRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 108 TQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARHYQRLKEIEP 187
Cdd:cd01334 80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 188 RLFVGSVV-GAVGTKASLsdkADELEVRVLNRLGL-GTPEISWQP--ARDRFSEYGMLIGLISGTLGKIANEILLLAHNE 263
Cdd:cd01334 160 RLNVLPLGgGAVGTGANA---PPIDRERVAELLGFfGPAPNSTQAvsDRDFLVELLSALALLAVSLSKIANDLRLLSSGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 264 IDELSEPFSKgQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWKVMPEMCLMLSVIFDNM 343
Cdd:cd01334 237 FGEVELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLL 315
|
330
....*....|
gi 1236168651 344 KTVLGGLNVH 353
Cdd:cd01334 316 TGVLEGLEVN 325
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
240-434 |
1.55e-68 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 217.59 E-value: 1.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 240 MLIGLISGTLGKIANEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDG 319
Cdd:PRK08937 21 IVLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 320 AIWKMEWKVMPEMCLMLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDK-AGKQTAHEIVYEASMSGQ 398
Cdd:PRK08937 101 SHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKgMGREEAHELIREKAMEAW 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1236168651 399 EEGITFIEAINRDTRIRDHITQEELDALLDPTTYVG 434
Cdd:PRK08937 181 KNQKDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
1-333 |
1.65e-63 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 209.14 E-value: 1.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 1 MGTSVFDSVLLKNLWSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLIPKQAAEVIAdtAKLEKLDMDFILEQVRLTR 80
Cdd:PRK05975 1 MSISVFDHPFLSGLFGDDEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIA--AACETFEPDLAALRHATAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 81 HPL-VPT-IRGLEHACPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQ 158
Cdd:PRK05975 79 DGVvVPAlVRQLRAAVGEEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 159 ALPITFGHKTAIWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEVRVLNRLGLgTPEISWQPARDRFSEY 238
Cdd:PRK05975 159 AIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGGAAGTLEKLGGKAAAVRARLAKRLGL-EDAPQWHSQRDFIADF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 239 GMLIGLISGTLGKIANEILLLAHNEiDELSEpfsKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERD 318
Cdd:PRK05975 238 AHLLSLVTGSLGKFGQDIALMAQAG-DEISL---SGGGGSSAMPHKQNPVAAETLVTLARFNATQVSGLHQALVHEQERS 313
|
330
....*....|....*
gi 1236168651 319 GAIWKMEWKVMPEMC 333
Cdd:PRK05975 314 GAAWTLEWMILPQMV 328
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
11-435 |
7.14e-48 |
|
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: 170.19 E-value: 7.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 11 LKNLWSTEEMRAIFSDKVRMQNWLDYEAALAIEQAELGLipKQAAEVIAD-TAKLEKLDMDFILEQVRLTRHPLVPTIRG 89
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGL--DISDEQIEEmKANVENIDFEIAAAEEKKLRHDVMAHVHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 90 LEHACPEHFGeYVHFGPTTQDVMDTGLVLQLKEAHNIFL-RDIKILGRsLLSLSEKHRNTPMPGRTLALQALPITFGHKT 168
Cdd:cd03302 79 FGLLCPAAAG-IIHLGATSCFVTDNTDLIQIRDALDLILpKLAAVIDR-LAEFALEYKDLPTLGFTHYQPAQLTTVGKRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 169 AIWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASL-------SDKADELEVRVLNRLGLGTP-EISWQP-ARDRFSEYG 239
Cdd:cd03302 157 CLWIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFldlfegdHDKVEALDELVTKKAGFKKVyPVTGQTySRKVDIDVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 240 MLIGLISGTLGKIANEILLLAHNEidELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQ-HER- 317
Cdd:cd03302 237 NALSSLGATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQwFERt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 318 --DGAIWKMewkVMPEMCLMLSVIFDNMKTVLGGLNVHTDKMRQNLDILGGFMLAERVMFALSDKAG-KQTAHEIVYEAS 394
Cdd:cd03302 315 ldDSANRRI---AIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGdRQDAHERIRVLS 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1236168651 395 MSG----QEEG-----ITFIEAINRDTRIRDhitqeELDALLDPTTYVGN 435
Cdd:cd03302 392 HQAaavvKQEGgdndlIERIKNDAYFKPIWD-----ELDALLDPKTFIGR 436
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
17-292 |
2.81e-43 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 154.45 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 17 TEEMRAIFSDKVRMQNWLDYE-----AALAIEQAELGLIPKQAAEVIADTaklekldMDFILEQVRLTRH-PLVPTIRGL 90
Cdd:pfam00206 7 ADALMGIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKA-------LDEVAEEGKLDDQfPLKVWQEGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 91 EHA--------------CPEHFGEYVHFGPTTQDVMDTGLVLQLKEA-HNIFLRDIKILGRSLLSLSEKHRNTPMPGRTl 155
Cdd:pfam00206 80 GTAvnmnlnevigellgQLVHPNDHVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRT- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 156 ALQ-ALPITFGHKTAIWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKAdELEVRVLNRLGLGTPEISWQP---- 230
Cdd:pfam00206 159 HLQdATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADP-EFAELVAKELGFFTGLPVKAPnsfe 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1236168651 231 ---ARDRFSEYGMLIGLISGTLGKIANEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVEN 292
Cdd:pfam00206 238 atsDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLEL 302
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
88-343 |
2.17e-40 |
|
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: 144.29 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 88 RGLEHACPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHK 167
Cdd:cd01594 23 RAGELAGGLHGSALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 168 TAIWLTELARHYQRLKEIeprlfvgsvvgavgtkaslsdkadelevrvlnrlglgtpeiswqpardRFSEYGMLIGLISG 247
Cdd:cd01594 103 LRAWAQVLGRDLERLEEA------------------------------------------------AVAEALDALALAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 248 TLGKIANEILLLAHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQHERDGAIWKMEWK 327
Cdd:cd01594 135 HLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSMRE 214
|
250
....*....|....*.
gi 1236168651 328 VMPEMCLMLSVIFDNM 343
Cdd:cd01594 215 ILADSLLLLIDALRLL 230
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
365-444 |
5.73e-26 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 100.60 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 365 GGFMLAERVMFALSDK-AGKQTAHEIVYEASMSGQEEGITFIEAINRDTRIRDHITQEELDALLDPTTYVGNAPEQVTRV 443
Cdd:smart00998 1 GGLIFSERVLLALVEKgLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80
|
.
gi 1236168651 444 I 444
Cdd:smart00998 81 L 81
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
366-443 |
6.64e-24 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 94.79 E-value: 6.64e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1236168651 366 GFMLAERVMFALSDKAGKQTAHEIVYEASM-SGQEEGITFIEAINRDTRIRdHITQEELDALLDPTTYVGNAPEQVTRV 443
Cdd:pfam10397 1 GLIFSERVLLALVKGLGREEAHELVQEAAMkAWEEGKNDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADEIVDRV 78
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
36-449 |
3.56e-21 |
|
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.
Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 95.31 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 36 YEAALAIEQA------ELGLIPKQAAEVIADTakLEKLDMDFILEQVRLTR-----HPLVptIRGLEHACPEHfGEYVHF 104
Cdd:cd01359 9 FEEDIAGSIAhavmlaEQGILTEEEAAKILAG--LAKIRAEIEAGAFELDPedediHMAI--ERRLIERIGDV-GGKLHT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 105 GPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTlALQ-ALPITFGHKTAIWLTELARHYQRLK 183
Cdd:cd01359 84 GRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYT-HLQrAQPITFGHYLLAYAEMLERDLERLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 184 EIEPRLFV---GSVVGAvGTKASLsdkaDELEVRVLnrlgLGTPEISWQP-----ARDRFSEYGMLIGLISGTLGKIANE 255
Cdd:cd01359 163 DAYKRVNVsplGAGALA-GTTFPI----DRERTAEL----LGFDGPTENSldavsDRDFVLEFLSAAALLMVHLSRLAED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 256 ILLLAHNEID--ELSEPFSkgqVGSSTMPHKRNPAIVE-----------NAACVSNTLKAN-LSVLTDMMkhqhERDGAI 321
Cdd:cd01359 234 LILWSTQEFGfvELPDAYS---TGSSIMPQKKNPDVLElirgkagrvigALAGLLTTLKGLpLAYNKDLQ----EDKEPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 322 WKMEWKVMpemcLMLSVifdnMKTVLGGLNVHTDKMRQNLDilGGFMLAERVMFALSDKAGK--QTAHEIVYEASMSGQE 399
Cdd:cd01359 307 FDAVDTLI----ASLRL----LTGVISTLTVNPERMREAAE--AGFSTATDLADYLVREKGVpfREAHHIVGRAVRLAEE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1236168651 400 EGITFIEAINRDTRIRDHITQEELDALLDP-------TTYVGNAPEQVTRVIEQTKA 449
Cdd:cd01359 377 KGKDLSDLTLAELQAISPLFEEDVREALDPensverrTSYGGTAPAEVREQIARARA 433
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
21-293 |
2.82e-20 |
|
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: 92.68 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 21 RAIFSD----KVRMQ---NWLDYEAALAIEQAELGLIPKQAAEV--IADTAKLEKLDMDFILEQVrlTRHplvpTIRGLE 91
Cdd:cd01598 2 RPYFSEyaliKYRVQvevEWLIALSNLEEIPEVPPLTKEELKFLraIIENFSEEDALRIKEIEAT--TNH----DVKAVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 92 -------HACPE--HFGEYVHFGPTTQDVMDTGLVLQLKEA-HNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALP 161
Cdd:cd01598 76 yflkekfETLGLlkKIKEFIHFACTSEDINNLAYALMIKEArNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 162 ITFGHKTAIWLTELARHYQRLKEIEprlFVGSVVGAVGT----KASLSD----KADElevRVLNRLGLgtpeiSWQPA-- 231
Cdd:cd01598 156 TTLGKELAVFVYRLERQYKQLKQIE---ILGKFNGAVGNfnahLVAYPDvdwrKFSE---FFVTSLGL-----TWNPYtt 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236168651 232 ----RDRFSEYGMLIGLISGTLGKIANEILLlaHNEIDELSEPFSKGQVGSSTMPHKRNPAIVENA 293
Cdd:cd01598 225 qiepHDYIAELFDALARINTILIDLCRDIWG--YISLGYFKQKVKKGEVGSSTMPHKVNPIDFENA 288
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
14-449 |
5.39e-20 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 92.03 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 14 LWS------TEEMRAIFSDKVRmqnwLDYEAALA-IEQ--------AELGLIPK-------QAAEVIADTAKLEKLDMDF 71
Cdd:TIGR00838 1 LWGgrftggMDPRVAKFNASLS----FDKELAEYdIEGsiahtkmlKKAGILTEeeaakiiEGLNELKEEGREGPFILDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 72 ILEQVrltrHPLVPtiRGLEHACPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMP 151
Cdd:TIGR00838 77 DDEDI----HMAIE--RELIDRVGEDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 152 GRTLALQALPITFGHKTAIWLTELARHYQRLKEIEPRLFV---GSvvGAVGTKASLSDKadELEVRVLNRLGLGTPEISW 228
Cdd:TIGR00838 151 GYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVsplGS--GALAGTGFPIDR--EYLAELLGFDAVTENSLDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 229 QPARDRFSEYGMLIGLISGTLGKIANEILLLAHNE--IDELSEPFSKgqvGSSTMPHKRNPAIVENAACVSNTLKANLSV 306
Cdd:TIGR00838 227 VSDRDFILELLFVAALIMVHLSRFAEDLILWSTGEfgFVELPDEFSS---GSSIMPQKKNPDVAELIRGKTGRVQGNLTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 307 LTDMMKHQ---HERDgaiwkmewkvMPEMCLMLsviFDNMKTVLGGLNVHT---DKMRQNLDI-----LGGFMLAERVMF 375
Cdd:TIGR00838 304 MLMTLKALplaYNRD----------LQEDKEPL---FDALKTVELSLEMATgmlDTITVNKERmeeaaSAGFSNATELAD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 376 ALSDKAGK-QTAHEIVYEASMSGQEEGITFIEAINRDTRIRDHITQEELDALLDPTTYV-------GNAPEQVTRVIEQT 447
Cdd:TIGR00838 371 YLVRKGVPfREAHHIVGELVATAIERGKGLEELTLEELQKFSPEFDEDVYEALDPESSVekrdakgGTAPEEVLQAIAEA 450
|
..
gi 1236168651 448 KA 449
Cdd:TIGR00838 451 KA 452
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
118-449 |
1.71e-17 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 84.43 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 118 LQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTlALQ-ALPITFGHKTAIWLTELARHYQRLKEIEPRLFV---GS 193
Cdd:PRK00855 121 LYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYT-HLQrAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRsplGS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 194 VVGAvGTKASLsDKAdelevRVLNRLGLGTP---EISWQPARDRFSEYGMLIGLISGTLGKIANEILLLAHNEID--ELS 268
Cdd:PRK00855 200 AALA-GTTFPI-DRE-----RTAELLGFDGVtenSLDAVSDRDFALEFLSAASLLMVHLSRLAEELILWSSQEFGfvELP 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 269 EPFSkgqVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMKHQ---HERDgaiwkmewkvmpeMCLMLSVIFDNMKT 345
Cdd:PRK00855 273 DAFS---TGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLplaYNRD-------------LQEDKEPLFDAVDT 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 346 V----------LGGLNVHTDKMRQNLDIlgGFMLAERVMFALsdkAGKQ----TAHEIVYEASMSGQEEGITFIEAINRD 411
Cdd:PRK00855 337 LklsleamagmLETLTVNKERMREAAGK--GFSTATDLADYL---VRKGvpfrEAHEIVGKAVREAEERGVDLADLSLEE 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1236168651 412 TR-IRDHITQEELDAlLDPTTYV-------GNAPEQVTRVIEQTKA 449
Cdd:PRK00855 412 LQaFSPLITEDVYEV-LTPEGSVaarnsigGTAPEQVREQIARAKA 456
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
118-449 |
5.47e-16 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 79.76 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 118 LQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTlALQ-ALPITFGHKTAIWLTELARHYQRLKEIEPRLFV---GS 193
Cdd:COG0165 120 LYLRDEILELIEALLALQEALLDLAEEHADTIMPGYT-HLQrAQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVsplGA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 194 vvGAV-GTkaSLSdkadelevrvLNR------LGLGTP------EISwqpARDRFSEYGMLIGLISGTLGKIANEILLLA 260
Cdd:COG0165 199 --AALaGT--TFP----------IDRertaelLGFDGPtensldAVS---DRDFALEFLSAASLIMVHLSRLAEELILWS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 261 HNEID--ELSEPFSkgqVGSSTMPHKRNPAIVENAACVSNTLKANL-SVLTdMMKHQ---HERDgaiwkME------WKV 328
Cdd:COG0165 262 SSEFGfvELPDAFS---TGSSIMPQKKNPDVAELIRGKTGRVIGNLtGLLT-TMKGLplaYNKD-----LQedkeplFDA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 329 MPEMCLMLSVifdnMKTVLGGLNVHTDKMRQNLDilGGFMLAervmFALSDK-AGKQ----TAHEIVYEASMSGQEEGIT 403
Cdd:COG0165 333 VDTLKLCLRL----FAGMIATLKVNRERMREAAG--AGFSTA----TDLADYlVRKGvpfrEAHEIVGRLVRYAEEKGKD 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1236168651 404 fIEAINRDT--RIRDHITqEELDALLDP-------TTYVGNAPEQVTRVIEQTKA 449
Cdd:COG0165 403 -LEDLTLEElqAFSPLIE-EDVYEALDPegsvaarDSYGGTAPEAVREQIARARA 455
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
17-313 |
1.55e-13 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 72.09 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 17 TEEMRAIFSD----KVRMQ---NWLdyeAALAiEQAELGLIPKQAAEviaDTAKLEKLDMDFILEQV-------RLTRHP 82
Cdd:PRK09285 20 TAALRPIFSEfgliRYRVQvevEWL---IALA-AHPGIPEVPPFSAE---ANAFLRAIVENFSEEDAarikeieRTTNHD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 83 L----------VPTIRGLEHAcpehfGEYVHFGPTTQDVMDTGLVLQLKEA-HNIFLRDIKILGRSLLSLSEKHRNTPMP 151
Cdd:PRK09285 93 VkaveyflkekLAGLPELEAV-----SEFIHFACTSEDINNLSHALMLKEArEEVLLPALRELIDALKELAHEYADVPML 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 152 GRTLALQALPITFGHKTAIWLTELARHYQRLKEIEprlFVGSVVGAVGT-KASLS--DKADELEV--RVLNRLGLgtpei 226
Cdd:PRK09285 168 SRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVE---ILGKINGAVGNyNAHLAayPEVDWHAFsrEFVESLGL----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 227 SWQP------ARDRFSEygmLIGLISGtlgkiANEILL-----------LAHneideLSEPFSKGQVGSSTMPHKRNPAI 289
Cdd:PRK09285 240 TWNPyttqiePHDYIAE---LFDAVAR-----FNTILIdldrdvwgyisLGY-----FKQKTKAGEIGSSTMPHKVNPID 306
|
330 340
....*....|....*....|....
gi 1236168651 290 VENAacvsntlKANLSVLTDMMKH 313
Cdd:PRK09285 307 FENS-------EGNLGLANALLEH 323
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
100-439 |
2.25e-12 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 68.61 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 100 EYVHFGPTTQDVMDTGLVLQLKEAHN-IFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARH 178
Cdd:PLN02848 118 EFFHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 179 YQRLKEIEprlFVGSVVGAVGT-KASLSdkadelevrvlnrlglGTPEISWQPARDRFSEygmliglisgTLGKIANEIL 257
Cdd:PLN02848 198 RKQLSEVK---IKGKFAGAVGNyNAHMS----------------AYPEVDWPAVAEEFVT----------SLGLTFNPYV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 258 --LLAHNEIDELSEPFSK---------------------------GQVGSSTMPHKRNPAIVENAA---CVSNTLKANLS 305
Cdd:PLN02848 249 tqIEPHDYMAELFNAVSRfnnilidfdrdiwsyislgyfkqitkaGEVGSSTMPHKVNPIDFENSEgnlGLANAELSHLS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 306 vltdmMKHQHERdgaiWKMEwkvmpemcLMLSVIFDNMKTVLG--------------GLNVHTDKMRQNLDIlGGFMLAE 371
Cdd:PLN02848 329 -----MKLPISR----MQRD--------LTDSTVLRNMGVGLGhsllaykstlrgigKLQVNEARLAEDLDQ-TWEVLAE 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1236168651 372 RVMFALS--------DKAGKQTAHEIVYEASMSgqeegiTFIEAINrdtrirdhITQEELDALLD--PTTYVGNAPEQ 439
Cdd:PLN02848 391 PIQTVMRrygvpepyEKLKELTRGRAVTKESMR------EFIEGLE--------LPEEAKDQLLKltPHTYIGAAAAL 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
38-428 |
1.34e-10 |
|
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: 63.21 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 38 AALAieQAELGLIPKQAAEVIADTAK--LE-KLDMDFIL----------------EQV----------RLTRHPLVPtir 88
Cdd:cd01596 51 AALA--NAELGLLDEEKADAIVQACDevIAgKLDDQFPLdvwqtgsgtstnmnvnEVIanralellggKKGKYPVHP--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 89 glehacPEHfgeYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTlALQ-ALPITFGHK 167
Cdd:cd01596 126 ------NDD---VNNSQSSNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRT-HLQdAVPLTLGQE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 168 TAIWLTELARHYQRLKEIEPRLFVGSVVG-AVGTKASLSDKADELEVRVLNRL-GLG--TPE--ISWQPARDRFSEY-GM 240
Cdd:cd01596 196 FSGYAAQLARDIARIEAALERLRELNLGGtAVGTGLNAPPGYAEKVAAELAELtGLPfvTAPnlFEATAAHDALVEVsGA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 241 LIGLiSGTLGKIANEILLLA---HNEIDELSEPfsKGQVGSSTMPHKRNPAIVENAACVSNTLKANlsvltdmmkhqher 317
Cdd:cd01596 276 LKTL-AVSLSKIANDLRLLSsgpRAGLGEINLP--ANQPGSSIMPGKVNPVIPEAVNMVAAQVIGN-------------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 318 DGAIwkmewkVMP------EMCLMLSVIFDNM---KTVLG------------GLNVHTDKMRQNLDilGGFMLAErvmfA 376
Cdd:cd01596 339 DTAI------TMAgsagqlELNVFKPVIAYNLlqsIRLLAnacrsfrdkcveGIEANEERCKEYVE--NSLMLVT----A 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1236168651 377 LSDKAGKQTAHEIVYEAsmsgQEEGITFIEAINRDTrirdHITQEELDALLD 428
Cdd:cd01596 407 LNPHIGYEKAAEIAKEA----LKEGRTLREAALELG----LLTEEELDEILD 450
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
38-429 |
1.97e-09 |
|
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: 59.44 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 38 AALAIEQAELGLIPKQAAEVIADTAKlE----KLDMDF---------------------------ILEQVRLTRHPLVPT 86
Cdd:cd01362 49 KAAAQANAELGLLDEEKADAIVQAAD-EviagKLDDHFplvvwqtgsgtqtnmnvnevianraieLLGGVLGSKKPVHPN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 87 irglehacpEHfgeyVHFGPTTQDVMDTGL----VLQLKEAhniFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPI 162
Cdd:cd01362 128 ---------DH----VNMSQSSNDTFPTAMhiaaALALQER---LLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 163 TFGHKTAIWLTELARHYQRLKEIEPRLFVGSVVG-AVGTKASLSDKADELEVRVLNRLGlGTPeisWQPARDRFSE---- 237
Cdd:cd01362 192 TLGQEFSGYAAQLEHAIARIEAALPRLYELALGGtAVGTGLNAHPGFAEKVAAELAELT-GLP---FVTAPNKFEAlaah 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 238 ------YGMLIGLiSGTLGKIANEILLLA---HNEIDELSEPfsKGQVGSSTMPHKRNPAIVENAACVSNTLKANlsvlt 308
Cdd:cd01362 268 dalveaSGALKTL-AVSLMKIANDIRWLGsgpRCGLGELSLP--ENEPGSSIMPGKVNPTQCEALTMVAAQVMGN----- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 309 dmmkhqherDGAIwkmewkVMP------EMCLMLSVIFDNM---------------KTVLGGLNVHTDKMRQNLDilGGF 367
Cdd:cd01362 340 ---------DAAI------TIAgssgnfELNVFKPVIIYNLlqsirlladacrsfaDKCVAGIEPNRERIAELLE--RSL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236168651 368 MLAErvmfALSDKAGKQTAHEIVYEAsmsgQEEGITFIEAINRDTrirdHITQEELDALLDP 429
Cdd:cd01362 403 MLVT----ALNPHIGYDKAAKIAKKA----HKEGLTLKEAALELG----YLTEEEFDRLVDP 452
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
99-295 |
4.06e-09 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 58.30 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 99 GEYVHFGP--------TTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTlALQ-ALPITFGHKTA 169
Cdd:cd01357 119 GEYQYVHPndhvnmsqSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRT-QLQdAVPMTLGQEFG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 170 IWLTELARHYQRLKEIEPRLFVGSVVG-AVGTKASLSDKADELEVRVLNRL-GLGtpeisWQPARDRF------SEYGML 241
Cdd:cd01357 198 AYATALKRDRARIYKARERLREVNLGGtAIGTGINAPPGYIELVVEKLSEItGLP-----LKRAENLIdatqntDAFVEV 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236168651 242 IGLISGT---LGKIANEILLLAHNE---IDELSEPfsKGQVGSSTMPHKRNPAIVE--NAAC 295
Cdd:cd01357 273 SGALKRLavkLSKIANDLRLLSSGPragLGEINLP--AVQPGSSIMPGKVNPVIPEvvNQVA 332
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
102-299 |
6.26e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 58.07 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 102 VHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARHYQR 181
Cdd:PRK06705 110 MHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLER 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 182 LKEIEpRLFVGSVVGAvgtkASLSDKADELE-VRVLNRLGLGTP-EISWQ--PARDRFSEYGMLIGLISGTLGKIANEIL 257
Cdd:PRK06705 190 MKKTY-KLLNQSPMGA----AALSTTSFPIKrERVADLLGFTNViENSYDavAGADYLLEVSSLLMVMMTNTSRWIHDFL 264
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1236168651 258 LLAHNEIDELSEPFSKGQVgSSTMPHKRNPAIVENAACVSNT 299
Cdd:PRK06705 265 LLATKEYDGITVARPYVQI-SSIMPQKRNPVSIEHARAITSS 305
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
99-448 |
6.99e-09 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 57.87 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 99 GEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARH 178
Cdd:PRK12308 100 GKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 179 YQRLKEIEPRLFV---GSvvGAVGTKASLSDK---ADELEVRVLNRLGLGTpeISwqpARDRFSEYgMLIGLISGT-LGK 251
Cdd:PRK12308 180 YSRLEDALTRLDTcplGS--GALAGTAYPIDRealAHNLGFRRATRNSLDS--VS---DRDHVMEL-MSVASISMLhLSR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 252 IANEILLLAHNEID--ELSEPFSKgqvGSSTMPHKRNPAIVE-----------NAACVSNTLKA-NLSVLTDMmkhQHER 317
Cdd:PRK12308 252 LAEDLIFYNSGESGfiELADTVTS---GSSLMPQKKNPDALElirgktgrvygALAGMMMTVKAlPLAYNKDM---QEDK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 318 DGAIWKME-WKVMPEMCLMlsvifdnmktVLGGLNVHTDKMRQ-------NLDILGGFMLAERVMFalsdkagkQTAHEI 389
Cdd:PRK12308 326 EGLFDALDtWNDCMEMAAL----------CFDGIKVNGERTLEaakqgyaNATELADYLVAKGIPF--------REAHHI 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236168651 390 VYEASMSGQEEGIT-----------FIEAINRDtrIRDHITqeeLDALLDPTTYVGN-APEQVTRVIEQTK 448
Cdd:PRK12308 388 VGVAVVGAIAKGCAleelsleqlkeFSDVIEDD--VYQILT---IESCLEKRCALGGvSPEQVAYAVEQAD 453
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
22-370 |
1.40e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 57.16 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 22 AIFSDKVRMQNWLDYEAALAIEQAELGLI-PKQAAEVIADTAKLEKLDMDFILEQVRltrhplvPtiRGLEHA------- 93
Cdd:PRK02186 430 ASEAPLAELDHLAAIDEAHLVMLGDTGIVaPERARPLLDAHRRLRDAGFAPLLARPA-------P--RGLYMLyeaylie 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 94 -CPEHFGEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWL 172
Cdd:PRK02186 501 rLGEDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVD 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 173 TELARHYQRLKEIEPRLFVgSVVGAvGTKASLSDKADELEVRVLnrLGLGTPEISWQPA---RDRFSEYGMLIGLISGTL 249
Cdd:PRK02186 581 GALARETHALFALFEHIDV-CPLGA-GAGGGTTFPIDPEFVARL--LGFEQPAPNSLDAvasRDGVLHFLSAMAAISTVL 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 250 GKIANEILLLAHNEIDELSEPFS-KGqvGSSTMPHKRNPAIVEN------------AACVSNTLKANLS----VLTDMMK 312
Cdd:PRK02186 657 SRLAQDLQLWTTREFALVSLPDAlTG--GSSMLPQKKNPFLLEFvkgragvvagalASASAALGKTPFSnsfeAGSPMNG 734
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1236168651 313 HQHERDGAIwkmewkvmPEMCLMLSVIFDnmktvlgGLNVHTDKMRQNLDILGGFMLA 370
Cdd:PRK02186 735 PIAQACAAI--------EDAAAVLVLLID-------GLEADQARMRAHLEDGGVSATA 777
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
95-291 |
2.64e-08 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 55.85 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 95 PEHFGEYVHFGPTTQDVMDTGL-VLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLT 173
Cdd:PLN00134 119 PVHPNDHVNRSQSSNDTFPTAMhIAAATEIHSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYAT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 174 ELARHYQRLKEIEPRLFVGSVVG-AVGT----KASLSDKADElEVRVLNRLGLGTPE--ISWQPARDRFSEYGMLIGLIS 246
Cdd:PLN00134 199 QVKYGLNRVQCTLPRLYELAQGGtAVGTglntKKGFDEKIAA-AVAEETGLPFVTAPnkFEALAAHDAFVELSGALNTVA 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1236168651 247 GTLGKIANEILLLAHNE---IDELSEPfsKGQVGSSTMPHKRNPAIVE 291
Cdd:PLN00134 278 VSLMKIANDIRLLGSGPrcgLGELNLP--ENEPGSSIMPGKVNPTQCE 323
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
100-429 |
4.07e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 55.37 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 100 EYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARHY 179
Cdd:PRK13353 133 DHVNMAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 180 QRLKEIEPRLFVGSVVG-AVGTKASLSDKADELEVRVLNRLGlGTPEIswqPARDRF------SEYGMLIGLISGT---L 249
Cdd:PRK13353 213 KRIQQAREHLYEVNLGGtAVGTGLNADPEYIERVVKHLAAIT-GLPLV---GAEDLVdatqntDAFVEVSGALKVCavnL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 250 GKIANEILLLA---HNEIDELSEPfsKGQVGSSTMPHKRNPAIVENAACVSNTLKANlsvltdmmkhqherDGAI-WKME 325
Cdd:PRK13353 289 SKIANDLRLLSsgpRTGLGEINLP--AVQPGSSIMPGKVNPVMPEVVNQIAFQVIGN--------------DVTItLAAE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 326 WKVMpEMCLMLSVIFDNM---------------KTVLGGLNVHTDKMRQnldilggfmLAER---VMFALSDKAGKQTAH 387
Cdd:PRK13353 353 AGQL-ELNVMEPVIAFNLlesisiltnacraftDNCVKGIEANEERCKE---------YVEKsvgIATALNPHIGYEAAA 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1236168651 388 EIVYeasmsgqeegitfiEAINRDTRIRDHI------TQEELDALLDP 429
Cdd:PRK13353 423 RIAK--------------EAIATGRSVRELAlengllSEEELDLILDP 456
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
38-291 |
1.80e-07 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 53.21 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 38 AALAieQAELGLIPKQAAEVIADTAklekldmDFILEQvRLTRHPLVPTI------------------RGLEHACPEHfG 99
Cdd:PRK12273 58 AALA--NKELGLLDEEKADAIVAAC-------DEILAG-KLHDQFVVDVIqggagtstnmnanevianRALELLGHEK-G 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 100 EY--------VHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTlALQ-ALPITFGHKTAI 170
Cdd:PRK12273 127 EYqyvhpndhVNMSQSTNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRT-QLQdAVPMTLGQEFGA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 171 WLTELARHYQRLKEIEPRLfvgSVVG----AVGTKASLSDKADELEVRVLNRL-GLGTpeiswQPARDRF------SEYG 239
Cdd:PRK12273 206 YAVALAEDRKRLYRAAELL---REVNlgatAIGTGLNAPPGYIELVVEKLAEItGLPL-----VPAEDLIeatqdtGAFV 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1236168651 240 MLIGLISGT---LGKIANEILLLAH------NEID--ELsepfskgQVGSSTMPHKRNPAIVE 291
Cdd:PRK12273 278 EVSGALKRLavkLSKICNDLRLLSSgpraglNEINlpAV-------QAGSSIMPGKVNPVIPE 333
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
99-449 |
2.61e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 52.68 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 99 GEYVHFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARH 178
Cdd:PRK04833 100 GKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 179 YQRLKEIEPRLFV-----GSVVG----------------AVGTKASL---SDKADELEvrVLNRLGLGTPEISwqpardR 234
Cdd:PRK04833 180 ESRLQDALKRLDVsplgsGALAGtayeidreqlagwlgfASATRNSLdsvSDRDHVLE--LLSDASISMVHLS------R 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 235 FSEygMLIGLISGTLGKIaneilllahneidELSEPFSKgqvGSSTMPHKRNPAIVE--NAAC---------VSNTLKA- 302
Cdd:PRK04833 252 FAE--DLIFFNSGEAGFV-------------ELSDRVTS---GSSLMPQKKNPDALEliRGKCgrvqgaltgMLMTLKGl 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 303 NLSVLTDMmkhQHERDGAIWKME-WKVmpemCLMLSVIfdnmktVLGGLNVHTDKMRQ-------NLDILGGFMLAERVM 374
Cdd:PRK04833 314 PLAYNKDM---QEDKEGLFDALDtWLD----CLHMAAL------VLDGIQVKRPRCQEaaqqgyaNATELADYLVAKGVP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 375 FalsdkagkQTAHEIVYEASMSGQEEGI-----------TFIEAINRDtrIRDHITqeeLDALLDPTTYVGN-APEQVTR 442
Cdd:PRK04833 381 F--------REAHHIVGEAVVEAIRQGKpledlplaelqKFSSVIGDD--VYPILS---LQSCLDKRAAKGGvSPQQVAQ 447
|
....*..
gi 1236168651 443 VIEQTKA 449
Cdd:PRK04833 448 AIAAAKA 454
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
88-429 |
1.02e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 50.77 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 88 RGLEHACPEHfGEYVHFGP--------TTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQA 159
Cdd:PRK14515 120 RALELLGMEK-GDYHYISPnshvnmaqSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 160 LPITFGHKTAIWLTELARHYQRLKEIEPRLF-VGSVVGAVGTKASLSDKADELEVRVLNRLGlGTPE------ISWQPAR 232
Cdd:PRK14515 199 VPIRLGQEFKAYSRVLERDMKRIQQSRQHLYeVNMGATAVGTGLNADPEYIEAVVKHLAAIS-ELPLvgaedlVDATQNT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 233 DRFSEYGMLIGLISGTLGKIANEILLLAHNEIDELSE-PFSKGQVGSSTMPHKRNPAIVE-------------NAACV-S 297
Cdd:PRK14515 278 DAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEiMLPARQPGSSIMPGKVNPVMPEvinqiafqvigndHTICLaS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 298 NTLKANLSVLTDMMKHQHERDGAIWKMEWKVMPEMCLMlsvifdnmktvlgGLNVHTDKMRQNLDILGGfmlaerVMFAL 377
Cdd:PRK14515 358 EAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLK-------------GIEANEDRLKEYVEKSVG------IITAV 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1236168651 378 SDKAGKQTAHEIVYEASMSGQeegitfieAINRDTRIRDHITQEELDALLDP 429
Cdd:PRK14515 419 NPHIGYEAAARVAKEAIATGQ--------SVRELCVKNGVLSQEDLELILDP 462
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
103-371 |
2.76e-06 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 49.34 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 103 HFGPTTQDVMDTGLVLQLKEAHNIFLRDIKILGRSLLSLSEKHRNTPMPGRTLALQALPITFGHKTAIWLTELARHYQRL 182
Cdd:PLN02646 118 HTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 183 KEIEPRLFV---GSvvGAVGTKASLSDK---ADElevrvlnrLGLGTP---EISWQPARDRFSEYGMLIGLISGTLGKIA 253
Cdd:PLN02646 198 VDCRPRVNFcplGS--CALAGTGLPIDRfmtAKD--------LGFTAPmrnSIDAVSDRDFVLEFLFANSITAIHLSRLG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 254 NEILLLAHNEID--ELSEPFSkgqVGSSTMPHKRNPAIVENAACVSNTLKANLSVLTDMMK---HQHERDgaiWKMEWKV 328
Cdd:PLN02646 268 EEWVLWASEEFGfvTPSDAVS---TGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKglpTAYNRD---LQEDKEP 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1236168651 329 MpemclmlsviFDNMKTVLGGLNVHT----------DKMRQNL--DILGGFMLAE 371
Cdd:PLN02646 342 L----------FDSVDTVSDMLEVATefaqnitfnpERIKKSLpaGMLDATTLAD 386
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
150-291 |
1.40e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 41.03 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236168651 150 MPGRTLALQALPITFGHKTAIWLTELARHYQRLKEIEPRLFVGSVVGAVGTKASLSDKADELEvrvlNRLGLG----TPE 225
Cdd:PRK06389 145 LPGYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMS----ELLGMEknikNPV 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236168651 226 ISWQPARDRFSEYGMLIGLISGTLGKIANEILLLAHNEIDELSEPFSkgqVGSSTMPHKRNPAIVE 291
Cdd:PRK06389 221 YSSSLYIKTIENISYLISSLAVDLSRICQDIIIYYENGIITIPDEFT---TGSSLMPNKRNPDYLE 283
|
|
| |
