|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
26-486 |
0e+00 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 922.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 26 SSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGarERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADE 105
Cdd:COG0114 2 METRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 106 VASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIQNE 184
Cdd:COG0114 80 VIAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKpVHPNDHVNMSQSSNDTFPTAMHIAAALALEER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 185 LIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTK 264
Cdd:COG0114 160 LLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 265 PGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSS 344
Cdd:COG0114 240 PGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 345 IMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIH 424
Cdd:COG0114 320 IMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324993 425 ELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLG 486
Cdd:COG0114 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
26-488 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 917.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 26 SSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGarERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADE 105
Cdd:PRK00485 2 METRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 106 VASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIQNE 184
Cdd:PRK00485 80 VIAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKpVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 185 LIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTK 264
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 265 PGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSS 344
Cdd:PRK00485 240 PGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 345 IMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIH 424
Cdd:PRK00485 320 IMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIK 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324993 425 ELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGPK 488
Cdd:PRK00485 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
28-486 |
0e+00 |
|
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]
Pssm-ID: 130052 [Multi-domain] Cd Length: 458 Bit Score: 911.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 28 FRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGgaRERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVA 107
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 108 SGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELI 186
Cdd:TIGR00979 79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQpVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 187 PELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPG 266
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 267 FDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIM 346
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 347 PGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHEL 426
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 427 LTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLG 486
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
29-484 |
0e+00 |
|
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: 899.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 29 RTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGarERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVAS 108
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 109 GKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIP 187
Cdd:cd01362 79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKpVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 188 ELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGF 267
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 268 DVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMP 347
Cdd:cd01362 239 AEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 348 GKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELL 427
Cdd:cd01362 319 GKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324993 428 TKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHM 484
Cdd:cd01362 399 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
29-480 |
0e+00 |
|
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: 834.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 29 RTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGarERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVAS 108
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 109 GKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQVHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIPE 188
Cdd:cd01596 79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 189 LTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGFD 268
Cdd:cd01596 159 LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 269 VKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMPG 348
Cdd:cd01596 239 EKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 349 KVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELLT 428
Cdd:cd01596 319 KVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6324993 429 KSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVV 480
Cdd:cd01596 399 NSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
35-487 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 829.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 35 FGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVASGKLDDH 114
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 115 FPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIPELTNLK 193
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSpVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 194 NALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGFDVKIAE 273
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 274 QISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMPGKVNPT 353
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 354 QNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELLTKSLML 433
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 6324993 434 VTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGP 487
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
29-488 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 619.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 29 RTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVAS 108
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 109 GKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGS-KQVHPNNHCNQSQSSNDTFPTVMHIAASLQIQnELIP 187
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDyDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLR-ELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 188 ELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGF 267
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 268 DVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMP 347
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 348 GKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELL 427
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324993 428 TKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGPK 488
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
29-487 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 599.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 29 RTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGarERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVAS 108
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 109 GKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIP 187
Cdd:PRK12425 81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSpVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 188 ELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGF 267
Cdd:PRK12425 161 AIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 268 DVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMP 347
Cdd:PRK12425 241 AEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 348 GKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELL 427
Cdd:PRK12425 321 GKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 428 TKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGP 487
Cdd:PRK12425 401 ERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
24-488 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 589.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 24 MNSSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAA 103
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 104 DEVASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGS-KQVHPNNHCNQSQSSNDTFPTVMHIAASLQIq 182
Cdd:PRK12273 81 DEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEyQYVHPNDHVNMSQSTNDAYPTAIRIALLLSL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 183 NELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLN 262
Cdd:PRK12273 160 RKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 263 TKPGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPG 342
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 343 SSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPR 422
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324993 423 IHELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGPK 488
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
29-477 |
0e+00 |
|
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: 571.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 29 RTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGarERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVAS 108
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 109 GKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAASLQIqNELIP 187
Cdd:cd01357 79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQyVHPNDHVNMSQSTNDVYPTALRLALILLL-RKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 188 ELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGF 267
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 268 DVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMP 347
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 348 GKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELL 427
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 6324993 428 TKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDE 477
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
24-488 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 548.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 24 MNSSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARerMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAA 103
Cdd:PRK13353 1 TNKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYK--IHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQAC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 104 DEVASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQ-VHPNNHCNQSQSSNDTFPTVMHIAAsLQIQ 182
Cdd:PRK13353 79 DEILAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHyVSPNDHVNMAQSTNDVFPTAIRIAA-LNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 183 NELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLN 262
Cdd:PRK13353 158 EGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 263 TKPGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPG 342
Cdd:PRK13353 238 ADPEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 343 SSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPR 422
Cdd:PRK13353 318 SSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEER 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324993 423 IHELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGPK 488
Cdd:PRK13353 398 CKEYVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
36-367 |
1.02e-148 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 427.17 E-value: 1.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 36 GEIHVPADKYWGAQTQRSFQNFKIGGARERmplplvhAFGVLKKSAAIVNESLggldPKISKAIQQAADEVAS-GKLDDH 114
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIK-------GLAALKKAAAKANVIL----KEEAAAIIKALDEVAEeGKLDDQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 115 FPLVVFQTGSGTQSNMNANEVISnraiEILGGKigskqVHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIPELTNLKN 194
Cdd:pfam00206 70 FPLKVWQEGSGTAVNMNLNEVIG----ELLGQL-----VHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLID 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 195 ALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSL-KTLSFLAQGGTAVGTGLNTKPGFDVKIAE 273
Cdd:pfam00206 141 ALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLpRLLVLPLGGGTAVGTGLNADPEFAELVAK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 274 QISKETGLKfQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPrCGYHELMLPENEPGSSIMPGKVNPT 353
Cdd:pfam00206 221 ELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPD 298
|
330
....*....|....
gi 6324993 354 QNEALTQVCVQVMG 367
Cdd:pfam00206 299 QLELLTGKAGRVMG 312
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
29-487 |
2.31e-148 |
|
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]
Pssm-ID: 213564 [Multi-domain] Cd Length: 468 Bit Score: 432.33 E-value: 2.31e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 29 RTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEV-A 107
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEIlN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 108 SGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQV-HPNNHCNQSQSSNDTFPTVMHIAASLQIQNeLI 186
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYlNPNDHVNKSQSTNDAYPTGFRIAVYSSLIK-LV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 187 PELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPG 266
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 267 FDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIM 346
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 347 PGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHEL 426
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324993 427 LTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGP 487
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
20-487 |
1.56e-144 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 422.87 E-value: 1.56e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 20 NIRRMNSSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARerMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAI 99
Cdd:PRK14515 3 TLTEVKNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYK--IHEGLIKAFAIVKKAAALANTDVGRLELNKGGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 100 QQAADEVASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGS-KQVHPNNHCNQSQSSNDTFPTVMHIAaS 178
Cdd:PRK14515 81 AEAAQEILDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDyHYISPNSHVNMAQSTNDAFPTAIHIA-T 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 179 LQIQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVG 258
Cdd:PRK14515 160 LNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 259 TGLNTKPGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPE 338
Cdd:PRK14515 240 TGLNADPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 339 NEPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKA 418
Cdd:PRK14515 320 RQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324993 419 NEPRIHELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGP 487
Cdd:PRK14515 400 NEDRLKEYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
71-419 |
6.35e-120 |
|
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: 354.12 E-value: 6.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 71 VHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVASGKLDDHFplvvFQTGSGTQSNMNANEVISNRAIEILGGKIgs 150
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGGYV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 151 kqvhpnnhcnQSQSSNDTFPTVMHIAASLQIQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYV 230
Cdd:cd01334 75 ----------HTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 231 QQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGFDVKIAEQISKetglkFQTAPNKFEALAAHDAIVECSGALNTLA 310
Cdd:cd01334 145 AELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 311 CSLFKIAQDIRYLGSGprcGYHELMLPEN-EPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPV 389
Cdd:cd01334 220 VSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPV 296
|
330 340 350
....*....|....*....|....*....|
gi 6324993 390 MIANLLNSIRLITDAAYSFRVHCvEGIKAN 419
Cdd:cd01334 297 EREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
130-409 |
6.43e-61 |
|
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: 198.99 E-value: 6.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 130 MNANEVISNRAIEILGGKIGSKQVHpnnhcnqSQSSNDTFPTVMHIAASLQIQNELIPELTNLKNALEAKSKEFDHIVKI 209
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSALVH-------KGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 210 GRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSlktlsflaqggtavgtglntkpgfdvkiaeqisketglkfqtapnk 289
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA---------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 290 fealaahdAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPeNEPGSSIMPGKVNPTQNEALTQVCVQVMGNN 369
Cdd:cd01594 121 --------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6324993 370 AAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFR 409
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
433-484 |
9.63e-26 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 99.32 E-value: 9.63e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6324993 433 LVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHM 484
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
162-352 |
4.41e-24 |
|
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: 103.74 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 162 SQSSNDTfptvmhiAASLQIQ---NELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQ 238
Cdd:cd01595 89 SQDINDT-------ALALQLRdalDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 239 RVAHSLKTLSFLAQGGtAVGTGLNTKPGfDVKIAEQISKETGLKFQTAPNKFEalaAHDAIVECSGALNTLACSLFKIAQ 318
Cdd:cd01595 162 RLEEARERVLVGGISG-AVGTHASLGPK-GPEVEERVAEKLGLKVPPITTQIE---PRDRIAELLSALALIAGTLEKIAT 236
|
170 180 190
....*....|....*....|....*....|....*.
gi 6324993 319 DIRYLGsgpRCGYHELMLP--ENEPGSSIMPGKVNP 352
Cdd:cd01595 237 DIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNP 269
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
166-486 |
1.75e-23 |
|
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: 102.47 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 166 NDTfptvmhiAASLQIQ---NELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAH 242
Cdd:COG0015 103 NDT-------ALALQLRealELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 243 SLKTLSFLAQGGtAVGTgLNTKPGFDVKIAEQISKETGLKF-----QTAPnkfealaaHDAIVECSGALNTLACSLFKIA 317
Cdd:COG0015 176 ARERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEKLGLKPnpvttQIEP--------RDRHAELFSALALIAGSLEKIA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 318 QDIRYLGSgPRCGYHELMLPENEPGSSIMPGKVNP--TQN-EALTQV---CVQVMGNNAAITF--AGSQGQFELNVFkPV 389
Cdd:COG0015 246 RDIRLLQR-TEVGEVEEPFAKGQVGSSAMPHKRNPidSENiEGLARLaraLAAALLEALASWHerDLSDSSVERNIL-PD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 390 MIanllnsirLITDAAY-SFRvHCVEGIKANEPRIHELLTKSLMLV------TALNPK-IGYDAA-SKVAKNAHKK---G 457
Cdd:COG0015 324 AF--------LLLDGALeRLL-KLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAyELVKELARGAweeG 394
|
330 340 350
....*....|....*....|....*....|...
gi 6324993 458 ITLKESALE----LGVLTEKEFDEWVVPEHMLG 486
Cdd:COG0015 395 NDLRELLAAdpeiPAELSKEELEALFDPANYLG 427
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
172-486 |
2.05e-19 |
|
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: 90.38 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 172 VMHIAASLQIQN---ELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLS 248
Cdd:cd01597 102 IIDTALVLQLRDaldLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 249 FLAQGGtAVGT--GLNTKpGFDVkiAEQISKETGLKFQTAPnkfeALAAHDAIVECSGALNTLACSLFKIAQDIRYLGsg 326
Cdd:cd01597 182 VVQFGG-AAGTlaSLGDQ-GLAV--QEALAAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM-- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 327 pRCGYHELMLP--ENEPGSSIMPGKVNPTQNEALtQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDA 404
Cdd:cd01597 252 -QTEIGEVAEPfaKGRGGSSTMPHKRNPVGCELI-VALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 405 AYSFRVHCVEGIKANEPRIHELL--TKSLML----VTALNPKIG----YDAASKVAKNAHKKGITLKESALE----LGVL 470
Cdd:cd01597 330 ALEQAEFLLSGLEVNEDRMRANLdlTGGLILseavMMALAPKLGrqeaHDLVYEACMRAVEEGRPLREVLLEdpevAAYL 409
|
330
....*....|....*.
gi 6324993 471 TEKEFDEWVVPEHMLG 486
Cdd:cd01597 410 SDEELDALLDPANYLG 425
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
165-368 |
1.56e-17 |
|
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: 84.71 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 165 SNDTFPTV--MHIAASLQIqneLIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAH 242
Cdd:TIGR00928 97 SNDIVDTAlaLLLRDALEI---ILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 243 SLKTLSFLAQGGtAVGTGLNTKPGFDvKIAEQISKETGLKFQTAPNKFEAlaaHDAIVECSGALNTLACSLFKIAQDIRY 322
Cdd:TIGR00928 174 AKERIKVGGISG-AVGTHAAAYPLVE-EVEERVTEFLGLKPVPISTQIEP---RDRHAELLDALALLATTLEKFAVDIRL 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6324993 323 LgsgPRCGYHELMLP--ENEPGSSIMPGKVNPTQNEALTQVCVQVMGN 368
Cdd:TIGR00928 249 L---QRTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLARVIRGY 293
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
94-479 |
3.08e-17 |
|
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: 83.94 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 94 KISKAIQQAADEVASGKLDDHFPLvvfqtgsgtqsnMNANEVISNRAIEILGGKIGSKqVHpnnhcnQSQSSNDTFPTVM 173
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGK-LH------TGRSRNDQVATDL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 174 HIAASLQIqNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQG 253
Cdd:TIGR00838 116 RLYLRDHV-LELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 254 GTAV-GTGLNTKPGFdvkIAEqisketGLKFQTA-PNKFEALAAHDAIVECSGALNTLACSLFKIAQDIrYLGSGPRCGY 331
Cdd:TIGR00838 195 SGALaGTGFPIDREY---LAE------LLGFDAVtENSLDAVSDRDFILELLFVAALIMVHLSRFAEDL-ILWSTGEFGF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 332 HELMlPENEPGSSIMPGKVNPTQNEALTQVCVQVMGNNA-------AITFAGSQGQFELN--VFKPVmiANLLNSIRLIT 402
Cdd:TIGR00838 265 VELP-DEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTgmlmtlkALPLAYNRDLQEDKepLFDAL--KTVELSLEMAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 403 DAaysfrvhcVEGIKANEPRIHELLTKSLMLVTALN--------P-KIGYDAASKVAKNAHKKGITLKESALELGVLTEK 473
Cdd:TIGR00838 342 GM--------LDTITVNKERMEEAASAGFSNATELAdylvrkgvPfREAHHIVGELVATAIERGKGLEELTLEELQKFSP 413
|
....*.
gi 6324993 474 EFDEWV 479
Cdd:TIGR00838 414 EFDEDV 419
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
165-359 |
4.96e-17 |
|
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: 82.60 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 165 SNDtfptVMHIAASLQIQ--NELI-PELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVA 241
Cdd:cd01360 91 SSD----VVDTALALQLReaLDIIlKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 242 HSLKTLSFLAQGGtAVGTGLNTKPgfdvKIAEQISKETGLKFQTAPNKfeaLAAHDAIVECSGALNTLACSLFKIAQDIR 321
Cdd:cd01360 167 EARERILVGKISG-AVGTYANLGP----EVEERVAEKLGLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIR 238
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6324993 322 YLgsgPRCGYHELMLP--ENEPGSSIMPGKVNPTQNEALT 359
Cdd:cd01360 239 HL---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENIC 275
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
185-352 |
3.35e-14 |
|
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: 74.19 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 185 LIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENgiQRvaHSLKTLSFLAQGGTAVGTgLNTK 264
Cdd:cd01598 121 ILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLER--QY--KQLKQIEILGKFNGAVGN-FNAH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 265 ----PGFD-VKIAEQISKETGLKFQTAPNKFEalaAHDAIVECSGALNTLACSLFKIAQDI-RYLGSgprcGYHELMLPE 338
Cdd:cd01598 196 lvayPDVDwRKFSEFFVTSLGLTWNPYTTQIE---PHDYIAELFDALARINTILIDLCRDIwGYISL----GYFKQKVKK 268
|
170
....*....|....
gi 6324993 339 NEPGSSIMPGKVNP 352
Cdd:cd01598 269 GEVGSSTMPHKVNP 282
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
172-486 |
4.21e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 68.12 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 172 VMHIAASLQIQ---NELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHsLKTLS 248
Cdd:PRK09053 111 IIDTGLVLQLRdalDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAA-LRPRA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 249 FLAQGGTAVGT--GLNTKpGFDVkiAEQISKETGLKFQTAPNKfealAAHDAIVECSGALNTLACSLFKIAQDIRYlgsg 326
Cdd:PRK09053 190 LVLQFGGAAGTlaSLGEQ-ALPV--AQALAAELQLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDVSL---- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 327 prcgyheLMLPE----NEP------GSSIMPGKVNPTQNEALTQVCVQVMGnNAAITFAGS-----------QGQFElnv 385
Cdd:PRK09053 259 -------LMQTEvgevFEPaaagkgGSSTMPHKRNPVGCAAVLTAATRAPG-LVATLFAAMpqeheralggwHAEWD--- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 386 fkpvmianLLNSIRLITDAAYSFRVHCVEGIKANEPRI--HELLTKSLML----VTALNPKIGYDAASKVAKNAHKKGI- 458
Cdd:PRK09053 328 --------TLPELACLAAGALAQMAQIVEGLEVDAARMraNLDLTHGLILaeavMLALADRIGRLDAHHLVEQASKRAVa 399
|
330 340 350
....*....|....*....|....*....|....*
gi 6324993 459 -------TLKESALELGVLTEKEFDEWVVPEHMLG 486
Cdd:PRK09053 400 egrhlrdVLAEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
70-485 |
5.60e-11 |
|
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: 64.49 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 70 LVHAfGVLKKSAA--IvnesLGGLDpKISKAIQQAADEVASGKLDDHFplvvfqtgsgtqsnmnANEvisNRAIEILGgK 147
Cdd:cd01359 23 LAEQ-GILTEEEAakI----LAGLA-KIRAEIEAGAFELDPEDEDIHM----------------AIE---RRLIERIG-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 148 IGSKqVHpnnhcnQSQSSNDTFPTVMHIAASLQIqNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFS 227
Cdd:cd01359 77 VGGK-LH------TGRSRNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 228 GYVQQVENGIQRVAHSLKTLSFLAQGGTA-VGTGLNTKPgfdvkiaEQISKETGlkFQT-APNKFEALAAHDAIVECSGA 305
Cdd:cd01359 149 AYAEMLERDLERLADAYKRVNVSPLGAGAlAGTTFPIDR-------ERTAELLG--FDGpTENSLDAVSDRDFVLEFLSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 306 LNTLACSLFKIAQDIrYLGSGPRCGYHELmlpeneP-----GSSIMPGKVNPTQNEALTQVCVQVMGNNAAItFAGSQGQ 380
Cdd:cd01359 220 AALLMVHLSRLAEDL-ILWSTQEFGFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGL-LTTLKGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 381 FE-----LNVFKPVM---IANLLNSIRLITDaaysfrvhCVEGIKANEPRIHELLTKSLMLVTAL------NPKI----G 442
Cdd:cd01359 292 PLaynkdLQEDKEPLfdaVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDLadylvrEKGVpfreA 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 6324993 443 YDAASKVAKNAHKKGITLKESALELGV----LTEKEFDEWVVPEHML 485
Cdd:cd01359 364 HHIVGRAVRLAEEKGKDLSDLTLAELQaispLFEEDVREALDPENSV 410
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
185-375 |
6.72e-10 |
|
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: 61.18 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 185 LIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTaVGTG---L 261
Cdd:cd03302 115 ILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQasfL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 262 NTKPGFDVKIA---EQISKETGLKF------QTAPNKfealaaHDAIVECsgALNTLACSLFKIAQDIRYLGsgprcGYH 332
Cdd:cd03302 194 DLFEGDHDKVEaldELVTKKAGFKKvypvtgQTYSRK------VDIDVLN--ALSSLGATAHKIATDIRLLA-----NLK 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324993 333 ELMLP--ENEPGSSIMPGKVNPTQNEALTQVCVQVMG--NNAAITFA 375
Cdd:cd03302 261 EVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMNlaSNAAQTAS 307
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
181-352 |
6.83e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 60.92 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 181 IQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHslktLSFLAQGGTAVGT- 259
Cdd:PRK09285 139 REEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEA----VEILGKINGAVGNy 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 260 --GLNTKPGFD-VKIAEQISKETGLKF-----QTAPnkfealaaHDAIVECSGAL---NTLacsLFKIAQDI------RY 322
Cdd:PRK09285 215 naHLAAYPEVDwHAFSREFVESLGLTWnpyttQIEP--------HDYIAELFDAVarfNTI---LIDLDRDVwgyislGY 283
|
170 180 190
....*....|....*....|....*....|
gi 6324993 323 LGSGPRCGyhelmlpenEPGSSIMPGKVNP 352
Cdd:PRK09285 284 FKQKTKAG---------EIGSSTMPHKVNP 304
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
181-352 |
2.56e-09 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 59.37 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 181 IQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVEngiqRVAHSLKTLSFLAQGGTAVG-- 258
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLS----RQRKQLSEVKIKGKFAGAVGny 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 259 -TGLNTKPGFD-VKIAEQISKETGLKFQTAPNKFEalaAHDAIVECSGALNTLACSLFKIAQDI-RYLGsgprCGYHELM 335
Cdd:PLN02848 218 nAHMSAYPEVDwPAVAEEFVTSLGLTFNPYVTQIE---PHDYMAELFNAVSRFNNILIDFDRDIwSYIS----LGYFKQI 290
|
170
....*....|....*..
gi 6324993 336 LPENEPGSSIMPGKVNP 352
Cdd:PLN02848 291 TKAGEVGSSTMPHKVNP 307
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
164-352 |
5.66e-09 |
|
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: 58.19 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 164 SSNDTFPTVMHIAASLQIqNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHS 243
Cdd:COG0165 109 SRNDQVATDFRLYLRDEI-LELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 244 LKTLSFLAQGGTAV-GTGLNTKP-------GFDvkiaeqisketglkfQTAPNKFEALAAHDAIVECSGALNTLACSLFK 315
Cdd:COG0165 188 YKRLNVSPLGAAALaGTTFPIDRertaellGFD---------------GPTENSLDAVSDRDFALEFLSAASLIMVHLSR 252
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324993 316 IAQDIrYLGSGPRCGYHELmlpeneP-----GSSIMPGKVNP 352
Cdd:COG0165 253 LAEEL-ILWSSSEFGFVEL------PdafstGSSIMPQKKNP 287
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
94-352 |
1.56e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 56.70 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 94 KISKAIQQAADEVASGKL-------DDHfplvvfqtgsgtqsnmnanEVISNRAIEILG---GKIGSkqvhpnnhcnqSQ 163
Cdd:PRK00855 60 KILAGLDEILEEIEAGKFefspeleDIH-------------------MAIEARLTERIGdvgGKLHT-----------GR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 164 SSNDTFPTVMHIAASLQIQnELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHS 243
Cdd:PRK00855 110 SRNDQVATDLRLYLRDEID-EIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 244 LKTLSFLAQGGTA-VGTGLNTKP-------GFDvKIAEqisketglkfqtapNKFEALAAHDAIVECSGALNTLACSLFK 315
Cdd:PRK00855 189 RKRVNRSPLGSAAlAGTTFPIDRertaellGFD-GVTE--------------NSLDAVSDRDFALEFLSAASLLMVHLSR 253
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6324993 316 IAQDIrYLGSGPRCGYHELmlpeneP-----GSSIMPGKVNP 352
Cdd:PRK00855 254 LAEEL-ILWSSQEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
305-486 |
4.33e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 53.49 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 305 ALNTLACSLFKIAQDIRYLgSGPRCGYHELMLPENEPGSSIMPGKVNPTQNEALTQVCVQVMGnNAAITFAGSQGQFELN 384
Cdd:PRK08937 22 VLALIATSLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRS-YLVTALENVPLWHERD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 385 VF-KPVMIANLLNSIrLITDAAYSFRVHCVEGIKANEPRIHE--------LLTKSLMLvTALNPKIG----YDAASKVAK 451
Cdd:PRK08937 100 LShSSAERIALPDAF-LALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHELIREKAM 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 6324993 452 NAHKKGITLKESALE----LGVLTEKEFDEWVVPEHMLG 486
Cdd:PRK08937 178 EAWKNQKDLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
144-372 |
7.03e-08 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 54.79 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 144 LGGKIG--SKQVHpnnhcnQSQSSNDTFPTVMHIAASLQIQnELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLT 221
Cdd:PRK12308 92 LIGKVGdlGKKLH------TGRSRNDQVATDLKLWCRQQGQ-QLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 222 LGQEFSGYVQQVENGIQRVAHSLKTLSFLAQG-GTAVGTglntkpgfdvkiAEQISKET---GLKFQTAP-NKFEALAAH 296
Cdd:PRK12308 165 FAHWCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGT------------AYPIDREAlahNLGFRRATrNSLDSVSDR 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324993 297 DAIVECSGALNTLACSLFKIAQDIRYLGSGpRCGYHElmLPEN-EPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAI 372
Cdd:PRK12308 233 DHVMELMSVASISMLHLSRLAEDLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALELIRGKTGRVYGALAGM 306
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
88-352 |
7.35e-08 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 54.73 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 88 LGGLDpKISKAIQQAADEVASGKLDDHfplvvfqtgsgtqsnMNanevISNRAIEILGGKigSKQVHpnnhcnQSQSSND 167
Cdd:PLN02646 74 LDGLD-EIEKEIEAGKFEWRPDREDVH---------------MN----NEARLTELIGEP--AKKLH------TARSRND 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 168 TFPTVMHIAASLQIqNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTL 247
Cdd:PLN02646 126 QVATDTRLWCRDAI-DVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 248 SFLAQGGTAV-GTGLntkpGFDvkiAEQISKETGLKfQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSG 326
Cdd:PLN02646 205 NFCPLGSCALaGTGL----PID---RFMTAKDLGFT-APMRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASE 276
|
250 260
....*....|....*....|....*...
gi 6324993 327 PrCGYhelMLPEN--EPGSSIMPGKVNP 352
Cdd:PLN02646 277 E-FGF---VTPSDavSTGSSIMPQKKNP 300
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
164-372 |
3.53e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 49.21 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 164 SSNDTFPTVMHIAASLQIQnELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHS 243
Cdd:PRK04833 108 SRNDQVATDLKLWCKDQVA-ELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 244 LKTL--SFLAQGGTAvGTGLNTKpgfdvkiAEQISKETGLKFQTApNKFEALAAHDAIVE-CSGALNTLAcSLFKIAQDI 320
Cdd:PRK04833 187 LKRLdvSPLGSGALA-GTAYEID-------REQLAGWLGFASATR-NSLDSVSDRDHVLElLSDASISMV-HLSRFAEDL 256
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324993 321 RYLGSGpRCGYHELMlPENEPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAI 372
Cdd:PRK04833 257 IFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGM 306
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
185-358 |
4.58e-06 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 48.51 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 185 LIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVqqveNGIQRVAHSLKTLS---FLAQGGTAVGTGL 261
Cdd:PRK05975 127 LAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWR----APLLRHRDRLEALRadvFPLQFGGAAGTLE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 262 NTKPGFDvKIAEQISKETGLkfqtaPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRcgyhELMLPENEp 341
Cdd:PRK05975 203 KLGGKAA-AVRARLAKRLGL-----EDAPQWHSQRDFIADFAHLLSLVTGSLGKFGQDIALMAQAGD----EISLSGGG- 271
|
170
....*....|....*..
gi 6324993 342 GSSIMPGKVNPTQNEAL 358
Cdd:PRK05975 272 GSSAMPHKQNPVAAETL 288
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
172-437 |
5.67e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.08 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 172 VMHIAASLQIQNELIPELTnlknALEAKSKEFDHIVKIGRTHL-----------------QDATPLTLGQEFSGYVQQVE 234
Cdd:PRK02186 509 VLQTARSRNDINATTTKLH----LREATSRAFDALWRLRRALVfkasanvdcalpiysqyQPALPGSLGHYLLAVDGALA 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 235 NGIQRVAHSLKTLSFLAQG-GTAVGTGLNTKPGFDVKIaeqisketgLKF-QTAPNKFEALAAHDAIVECSGALNTLACS 312
Cdd:PRK02186 585 RETHALFALFEHIDVCPLGaGAGGGTTFPIDPEFVARL---------LGFeQPAPNSLDAVASRDGVLHFLSAMAAISTV 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 313 LFKIAQDIRYLGSGPrcgYHELMLPEN-EPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFElNVFK--PV 389
Cdd:PRK02186 656 LSRLAQDLQLWTTRE---FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFS-NSFEagSP 731
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6324993 390 MIANLLNSIRLITDAAySFRVHCVEGIKANEPRIHELLTKSLMLVTAL 437
Cdd:PRK02186 732 MNGPIAQACAAIEDAA-AVLVLLIDGLEADQARMRAHLEDGGVSATAV 778
|
|
| PBPb |
smart00062 |
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ... |
257-308 |
1.34e-04 |
|
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe
Pssm-ID: 214497 [Multi-domain] Cd Length: 219 Bit Score: 43.09 E-value: 1.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324993 257 VGTGLNTKP-----------GFDVKIAEQISKETGLKFQ----TAPNKFEALAAHDAIVECSGALNT 308
Cdd:smart00062 4 VGTNGDYPPfsfadedgeltGFDVDLAKAIAKELGLKVEfvevSFDSLLTALKSGKIDVVAAGMTIT 70
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
210-352 |
3.55e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 42.96 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324993 210 GRTHLQDATPLTLgQEFSGYVQQV-ENGIQRVAHSLKTLSFLAQG-GTAVGTGLNTKpgFDvkiaeQISKETGLKFQTAP 287
Cdd:PRK06389 147 GYTHFRQAMPMTV-NTYINYIKSIlYHHINNLDSFLMDLREMPYGyGSGYGSPSSVK--FN-----QMSELLGMEKNIKN 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324993 288 NKFEALAAHDAIVECSGALNTLACSLFKIAQD-IRYLgsgpRCGYHELMlPENEPGSSIMPGKVNP 352
Cdd:PRK06389 219 PVYSSSLYIKTIENISYLISSLAVDLSRICQDiIIYY----ENGIITIP-DEFTTGSSLMPNKRNP 279
|
|
| |
