|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-454 |
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: 761.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 1 MSNTRIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGL 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 81 LEGDYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGEV------VNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQT 154
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGElgskkpVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 155 LPALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHP 234
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 235 EFAARFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSI 314
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 315 MPGKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQ 394
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 395 ALSRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLT 454
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-458 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 750.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 1 MSNTRIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGL 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 81 LEGDYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGEV------VNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQT 154
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGElgskkpVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 155 LPALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHP 234
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 235 EFAARFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSI 314
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 315 MPGKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQ 394
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051752624 395 ALSRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLTAGGV 458
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
5-453 |
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: 705.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 5 RIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLEGD 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 85 YMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGEV------VNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQTLPAL 158
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVlgskkpVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 159 LHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEFAA 238
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 239 RFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMPGK 318
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 319 VNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQALSR 398
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1051752624 399 NPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKL 453
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
5-449 |
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: 672.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 5 RIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLEGD 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 85 YMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGEV-----VNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQTLPALL 159
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKkgkypVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 160 HLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEFAAR 239
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 240 FSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMPGKV 319
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 320 NPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQALSRN 399
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1051752624 400 PILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLD 449
Cdd:cd01596 401 LMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
5-457 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 556.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 5 RIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAP--FVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLE 82
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHpeLIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 83 GDYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLG------EVVNPNDHVNCGQSSNDIIPTTIHVsAALVLHEQTLP 156
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGgkkgdyDYVHPNDHVNMSQSTNDVYPTAIRL-ALLLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 157 ALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEF 236
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 237 AARFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMP 316
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 317 GKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQAL 396
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051752624 397 SRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLTAGG 457
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-454 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 543.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 1 MSNTRIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRM-PAP-FVRALILAKAAAARANVDLKQISEGQGKAIVDAAQ 78
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsDYPeLIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 79 GLLEGDYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLG------EVVNPNDHVNCGQSSNDIIPTTIHVsAALVLHE 152
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGhekgeyQYVHPNDHVNMSQSTNDAYPTAIRI-ALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 153 QTLPALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINA 232
Cdd:PRK12273 161 KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 233 HPEFAARFSGHLSHLTKVKFTPGKNLFAliGSQDTA--VAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQP 310
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIE--ATQDTGafVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 311 GSSIMPGKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEA 390
Cdd:PRK12273 319 GSSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051752624 391 KLKQALSRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLT 454
Cdd:PRK12273 399 RCREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMT 462
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-449 |
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: 528.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 5 RIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLEGD 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 85 YMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLG------EVVNPNDHVNCGQSSNDIIPTTIHVsAALVLHEQTLPAL 158
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGhekgeyQYVHPNDHVNMSQSTNDVYPTALRL-ALILLLRKLLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 159 LHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEFAA 238
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 239 RFSGHLSHLTKVKFTPGKNLFAliGSQDTA--VAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMP 316
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLID--ATQNTDafVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 317 GKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQAL 396
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1051752624 397 SRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLD 449
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
3-458 |
1.33e-174 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 497.97 E-value: 1.33e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 3 NTRIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLE 82
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 83 GDYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLG------EVVNPNDHVNCGQSSNDIIPTTIHVsAALVLHEQTLP 156
Cdd:PRK13353 84 GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGgekgdyHYVSPNDHVNMAQSTNDVFPTAIRI-AALNLLEGLLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 157 ALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEF 236
Cdd:PRK13353 163 AMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 237 AARFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMP 316
Cdd:PRK13353 243 IERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 317 GKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQAL 396
Cdd:PRK13353 323 GKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051752624 397 SRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLTAGGV 458
Cdd:PRK13353 403 EKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGI 464
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
5-453 |
3.97e-174 |
|
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: 496.18 E-value: 3.97e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 5 RIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLEGD 84
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 85 YMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGEV------VNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQTLPAL 158
Cdd:TIGR00979 82 LDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKlgskqpVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 159 LHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEFAA 238
Cdd:TIGR00979 162 ENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 239 RFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMPGK 318
Cdd:TIGR00979 242 KVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 319 VNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQALSR 398
Cdd:TIGR00979 322 VNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1051752624 399 NPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKL 453
Cdd:TIGR00979 402 SLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQM 456
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
11-455 |
1.75e-168 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 481.88 E-value: 1.75e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 11 MGELQVPAEALYGAQTQRAVNNFPIS--HQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLEGDYMQH 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 89 FPVDIFQTGSGTSSNMNANEVIATLASRLLGE------VVNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQTLPALLHLV 162
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGpvgeksPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 163 QVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEFAARFSG 242
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 243 HLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMPGKVNPV 322
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 323 IPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQALSRNPIL 402
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1051752624 403 VTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLTA 455
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTG 453
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
4-457 |
1.57e-131 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 387.74 E-value: 1.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 4 TRIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLEG 83
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 84 DYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGE------VVNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQTLPA 157
Cdd:PRK12425 82 QHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNgrggksPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 158 LLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEFA 237
Cdd:PRK12425 162 IAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 238 ARFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMPG 317
Cdd:PRK12425 242 EAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 318 KVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQALS 397
Cdd:PRK12425 322 KVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 398 RNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLTAGG 457
Cdd:PRK12425 402 RGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAG 461
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-458 |
1.54e-128 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 380.88 E-value: 1.54e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 3 NTRIERDSMGELQVPAEALYGAQTQRAVNNFPISHQRMPAPFVRALILAKAAAARANVDLKQISEGQGKAIVDAAQGLLE 82
Cdd:PRK14515 10 GVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 83 GDYMQHFPVDIFQTGSGTSSNMNANEVIATLASRLLGE------VVNPNDHVNCGQSSNDIIPTTIHVsAALVLHEQTLP 156
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMekgdyhYISPNSHVNMAQSTNDAFPTAIHI-ATLNALEGLLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 157 ALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAVGTGINAHPEF 236
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 237 AARFSGHLSHLTKVKFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGLQPGSSIMP 316
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 317 GKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQAL 396
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051752624 397 SRNPILVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKLTAGGV 458
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHPGI 470
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
59-388 |
2.02e-96 |
|
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: 292.87 E-value: 2.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 59 NVDLKQISEGQGKAIVDAAQGLLEGDYMQHFpvdiFQTGSGTSSNMNANEVIATLASRLlgevvnPNDHVNCGQSSNDIi 138
Cdd:cd01334 15 LAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------NGGYVHTGRSSNDI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 139 PTTIHVSAALVLHEQTLPALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQA 218
Cdd:cd01334 84 VDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLNV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 219 LAQGGTAVGTGINAHPEFAARFSGHLSHltkvkFTPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGpla 298
Cdd:cd01334 164 LPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSG--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 299 GLGEIEL-EGLQPGSSIMPGKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLSSLELLANASRLL 377
Cdd:cd01334 236 EFGEVELpDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLL 315
|
330
....*....|.
gi 1051752624 378 ADKaIASFKVN 388
Cdd:cd01334 316 TGV-LEGLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-336 |
1.72e-94 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 287.73 E-value: 1.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 12 GELQVPAEALYGAQTQRAVNNFPISHQRMPApfvraLILAKAAAARANVDLKQISegqgKAIVDAAQGLLE-GDYMQHFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKG-----LAALKKAAAKANVILKEEA----AAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 91 VDIFQTGSGTSSNMNANEVIATLasrlLGEVVNPNDHVNCGQSSNDIIPTTIHVSAALVLHEQTLPALLHLVQVIEQKAE 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIGEL----LGQLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKEKAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 171 AVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPA-LQALAQGGTAVGTGINAHPEFAARFSGHLSHLTK 249
Cdd:pfam00206 148 EFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAKELGFFTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 250 VKFTPGkNLFALIGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPlAGLGEIELEGLQPGSSIMPGKVNPVIPEATAM 329
Cdd:pfam00206 228 LPVKAP-NSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQLELLTG 305
|
....*..
gi 1051752624 330 VAAQVIG 336
Cdd:pfam00206 306 KAGRVMG 312
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
104-378 |
8.71e-47 |
|
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: 161.24 E-value: 8.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 104 MNANEVIATLASRLLGEVVNPNdHVNCGQSSNDIiPTTIHVSAALVLHEQTLPALLHLVQVIEQKAEAVHPFIKTGRTHL 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-LVHKGRSSNDI-GTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 184 MDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALqalaqggtavgtginahpefaarfsghlshltkvkftpgknlfalig 263
Cdd:cd01594 92 QDAQPVTLGYELRAWAQVLGRDLERLEEAAVAE----------------------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 264 sqdtavaVSGQLKATAVSLMKIANDLRWMNSGPLAGLGEIELEGlQPGSSIMPGKVNPVIPEATAMVAAQVIGNDTVITV 343
Cdd:cd01594 125 -------ALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPG-QPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLT 196
|
250 260 270
....*....|....*....|....*....|....*
gi 1051752624 344 AGQSGNFELNVMLPIIAQNLLSSLELLANASRLLA 378
Cdd:cd01594 197 ALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
402-453 |
3.43e-20 |
|
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: 83.52 E-value: 3.43e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1051752624 402 LVTALNPIIGYQKAAEIAKQAYQQGRPVIDVALEHTDLPRSQLEVLLDPEKL 453
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
134-454 |
2.03e-17 |
|
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: 83.98 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 134 SNDIIPTTIhvsaALVL---HEQTLPALLHLVQVIEQKAEAvH---PFIktGRTHLMDAMPVRMSQVLNGWAQQLKANIG 207
Cdd:COG0015 99 SQDINDTAL----ALQLreaLELLLPDLDALIAALAELAEE-HkdtPML--GRTHGQHAEPTTFGKKLAVWAAELLRQLE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 208 HLQDLLPALQALAQGGtAVGTGiNAH----PEFAARFSGHLShLTKVKFTPGknlfalIGSQDTAVAVSGQLKATAVSLM 283
Cdd:COG0015 172 RLEEARERVLVGKIGG-AVGTY-AAHgeawPEVEERVAEKLG-LKPNPVTTQ------IEPRDRHAELFSALALIAGSLE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 284 KIANDLRWMNSgplAGLGEIElEGLQP---GSSIMPGKVNPVIPEatamvaaQVIGNdtvitvAGQsgnfeLNVMLPIIA 360
Cdd:COG0015 243 KIARDIRLLQR---TEVGEVE-EPFAKgqvGSSAMPHKRNPIDSE-------NIEGL------ARL-----ARALAAALL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 361 QNLLSSLE-----------LLANASRLL------ADKAIASFKVNEAKLKQALSRNPILV------TALNPI-IGYQKA- 415
Cdd:COG0015 301 EALASWHErdlsdssvernILPDAFLLLdgalerLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAy 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1051752624 416 ---AEIAKQAYQQGRPVIDVALEHTDLP----RSQLEVLLDPEKLT 454
Cdd:COG0015 381 elvKELARGAWEEGNDLRELLAADPEIPaelsKEELEALFDPANYL 426
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
131-451 |
6.24e-14 |
|
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: 73.43 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 131 GQSSNDIIPTtihvsaALVLheQTLPALLHLVQVIEQKAEAVHPFIKT-------GRTHLMDAMPVRMSQVLNGWAQQLK 203
Cdd:cd01597 96 GATTQDIIDT------ALVL--QLRDALDLLERDLDALLDALARLAAThrdtpmvGRTHLQHALPITFGLKVAVWLSELL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 204 ANIGHLQDLLPALQALAQGGtAVGT-------GINAHPEFAARF-------SGHLSHLTKVKFTpgkNLFALIgsqdtav 269
Cdd:cd01597 168 RHRERLDELRPRVLVVQFGG-AAGTlaslgdqGLAVQEALAAELglgvpaiPWHTARDRIAELA---SFLALL------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 270 avsgqlkatAVSLMKIANDLRWMNSgplAGLGEIElEGLQPG---SSIMPGKVNPVIPEATAMVAAQVIGNDTVITVAGQ 346
Cdd:cd01597 237 ---------TGTLGKIARDVYLLMQ---TEIGEVA-EPFAKGrggSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 347 ------SGNFELNVMLpiIAQNLLSSLELLANASRLLADkaiasFKVNEAKLKQALSRNPILVTA------LNPIIGYQK 414
Cdd:cd01597 304 qeherdAGAWHAEWIA--LPEIFLLASGALEQAEFLLSG-----LEVNEDRMRANLDLTGGLILSeavmmaLAPKLGRQE 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1051752624 415 A----AEIAKQAYQQGRPVIDVALEHTD----LPRSQLEVLLDPE 451
Cdd:cd01597 377 AhdlvYEACMRAVEEGRPLREVLLEDPEvaayLSDEELDALLDPA 421
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
107-427 |
1.71e-12 |
|
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: 68.69 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 107 NEVIATLasRLLGEVVNPND--HVNCGQSSNDIIPTTIhvsaALVL---HEQTLPALLHLVQVIEQKAEAvH---PFIkt 178
Cdd:cd01595 62 HDVIAFV--YALAEKCGEDAgeYVHFGATSQDINDTAL----ALQLrdaLDIILPDLDALIDALAKLALE-HkdtPML-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 179 GRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGtAVGTGINAH---PEFAARFsghlshLTKVKFTPg 255
Cdd:cd01595 133 GRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHASLGpkgPEVEERV------AEKLGLKV- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 256 knlfALIGSQ----DTAVAVSGQLKATAVSLMKIANDLRWMNSgplAGLGEIElEGL---QPGSSIMPGKVNPVIPEATA 328
Cdd:cd01595 205 ----PPITTQieprDRIAELLSALALIAGTLEKIATDIRLLQR---TEIGEVE-EPFekgQVGSSTMPHKRNPIDSENIE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 329 MVAAQVIGNdtvITVAGQSGNFEL-------NVMLPIIAQNLLSSLELLANASRLLADkaiasFKVNEAKLKQALSRNPI 401
Cdd:cd01595 277 GLARLVRAL---AAPALENLVQWHerdlsdsSVERNILPDAFLLLDAALSRLQGLLEG-----LVVNPERMRRNLDLTWG 348
|
330 340 350
....*....|....*....|....*....|...
gi 1051752624 402 LV------TALNP-IIGYQKAAEIAKQAYQQGR 427
Cdd:cd01595 349 LIlseavmMALAKkGLGRQEAYELVKEENYLGL 381
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
131-455 |
3.14e-12 |
|
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: 68.15 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 131 GQSSNDIIPTTIHvsaaLVLHEQTL---PALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIG 207
Cdd:TIGR00838 104 GRSRNDQVATDLR----LYLRDHVLelaEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 208 HLQDLLPALQALAQGGTAV-GTGINAHPEFAARFSGhLSHLTKvkftpgkNLFALIGSQDTAVAVSGQLKATAVSLMKIA 286
Cdd:TIGR00838 180 RLQDALKRVNVSPLGSGALaGTGFPIDREYLAELLG-FDAVTE-------NSLDAVSDRDFILELLFVAALIMVHLSRFA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 287 NDLRWMNSGPLaglGEIEL-EGLQPGSSIMPGKVNPVIPEATAMVAAQVIGNDTVITVAGQSGNFELNVMLPIIAQNLLS 365
Cdd:TIGR00838 252 EDLILWSTGEF---GFVELpDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQEDKEPLFD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 366 SLELLANASRLLAdKAIASFKVNEAKLKQALSRNPILVTALNPII---------GYQKAAEIAKQAYQQGRPVIDVALEH 436
Cdd:TIGR00838 329 ALKTVELSLEMAT-GMLDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHHIVGELVATAIERGKGLEELTLEE 407
|
330
....*....|....*....
gi 1051752624 437 TdlprSQLEVLLDPEKLTA 455
Cdd:TIGR00838 408 L----QKFSPEFDEDVYEA 422
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
131-451 |
4.46e-12 |
|
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: 67.57 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 131 GQSSNDIIPTTIHV---SAALVLHEQTLPALLHLVQVIEQKAEAVHPfiktGRTHLMDAMPVRMSQVLNGWAQQLKANIG 207
Cdd:cd01359 84 GRSRNDQVATDLRLylrDALLELLELLLDLQRALLDRAEEHADTIMP----GYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 208 HLQDLLPALQALAQGGTA-VGTGINAHPEFAAR---FSGhlshltkvkftPGKNLFALIGSQDTAVAVSGQLKATAVSLM 283
Cdd:cd01359 160 RLADAYKRVNVSPLGAGAlAGTTFPIDRERTAEllgFDG-----------PTENSLDAVSDRDFVLEFLSAAALLMVHLS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 284 KIANDLRWMNSGPLaglGEIEL-EGLQPGSSIMPGKVNPVIPEATAMVAAQVIGN-DTVITVA-------------GQSG 348
Cdd:cd01359 229 RLAEDLILWSTQEF---GFVELpDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGAlAGLLTTLkglplaynkdlqeDKEP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 349 NFELnvmlpiiAQNLLSSLELLANasrlladkAIASFKVNEAKLKQALSRNPILVTALNPII----------GYQKAAEI 418
Cdd:cd01359 306 LFDA-------VDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDLADYLvrekgvpfreAHHIVGRA 370
|
330 340 350
....*....|....*....|....*....|....*..
gi 1051752624 419 AKQAYQQGRPVIDVALE--HTDLPRSQLEVL--LDPE 451
Cdd:cd01359 371 VRLAEEKGKDLSDLTLAelQAISPLFEEDVReaLDPE 407
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
127-451 |
5.75e-11 |
|
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: 64.29 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 127 HVNCGQSSNDIIPTtihvSAALVL---HEQTLPALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLK 203
Cdd:TIGR00928 90 FIHFGATSNDIVDT----ALALLLrdaLEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 204 AnigHLQDLLPALQALAQGGT--AVGTGINAHP------EFAARFSGhlshLTKVKFTpgknlfALIGSQDTAVAVSGQL 275
Cdd:TIGR00928 166 R---QLERLLQAKERIKVGGIsgAVGTHAAAYPlveeveERVTEFLG----LKPVPIS------TQIEPRDRHAELLDAL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 276 KATAVSLMKIANDLRWMNSGPLAGLGEIELEGlQPGSSIMPGKVNPVIPEatamvaaQVIGNDTVI----TVAGQSGN-- 349
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTEHFEVEEPFGKG-QVGSSAMPHKRNPIDFE-------NVCGLARVIrgyaSPALENAPlw 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 350 FELNVMLPIIAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQALSRNPILVTALNPII-------GYQKAAEIAKQ- 421
Cdd:TIGR00928 305 HERDLTDSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVREl 384
|
330 340 350
....*....|....*....|....*....|....*...
gi 1051752624 422 ----AYQQGRPVIDVALEHTDLPR----SQLEVLLDPE 451
Cdd:TIGR00928 385 amgaAEVDEPDLLEFLLEDERITKylkeEELAELLDPE 422
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
108-343 |
8.02e-10 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 60.89 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 108 EVIATLASRLLGEVVN-PNDHVNCGQSSNDIIPTTIH---VSAALVLheqtLPALLHLVQVIEQKAEAVHPFIKTGRTHL 183
Cdd:PLN02646 96 EDVHMNNEARLTELIGePAKKLHTARSRNDQVATDTRlwcRDAIDVI----RKRIKTLQVALVELAEKNVDLVVPGYTHL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 184 MDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTAV-GTGINAHPEFAARFSGhlshltkvkFT-PGKNLFAL 261
Cdd:PLN02646 172 QRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALaGTGLPIDRFMTAKDLG---------FTaPMRNSIDA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 262 IGSQDTAVAVSGQLKATAVSLMKIANDLRWMNSGPLAGLgeIELEGLQPGSSIMPGKVNPVIPEATAMVAAQVIGNDTVI 341
Cdd:PLN02646 243 VSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFV--TPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTV 320
|
..
gi 1051752624 342 TV 343
Cdd:PLN02646 321 LA 322
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
157-435 |
2.02e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 49.76 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 157 ALLHLVQVIEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTA-VGTGINAHPE 235
Cdd:PRK00855 133 LLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIDRE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 236 FAAR---FSGhlshltkvkftPGKNLFALIGSQDTAVAVSGQLKATAVSLMKIANDL-RWMNsgplAGLGEIELeglqP- 310
Cdd:PRK00855 213 RTAEllgFDG-----------VTENSLDAVSDRDFALEFLSAASLLMVHLSRLAEELiLWSS----QEFGFVEL----Pd 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 311 ----GSSIMPGKVNPVIPEATAMVAAQVIGNDTVItvagqsgnfeLNVM--LPI---------------IAQNLLSSLEL 369
Cdd:PRK00855 274 afstGSSIMPQKKNPDVAELIRGKTGRVYGNLTGL----------LTVMkgLPLaynrdlqedkeplfdAVDTLKLSLEA 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051752624 370 LAnasrlladKAIASFKVNEAKLKQALSRNPILVTALNPII---------GYQKAAEIAKQAYQQGRPVIDVALE 435
Cdd:PRK00855 344 MA--------GMLETLTVNKERMREAAGKGFSTATDLADYLvrkgvpfreAHEIVGKAVREAEERGVDLADLSLE 410
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
108-325 |
8.15e-06 |
|
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: 47.93 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 108 EVIATLasRLLGEVVNPN-DHVNCGQSSNDIIPTtihvSAALVLHEQT---LPALLHLVQVIEQKAEAVHPFIKTGRTHL 183
Cdd:cd01360 66 DVIAFV--TAIAEYCGEAgRYIHFGLTSSDVVDT----ALALQLREALdiiLKDLKELLEVLKKKALEHKDTVMVGRTHG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 184 MDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGtAVGTGINAHPE---FAARFSGhLSHltkvkftpgknlfA 260
Cdd:cd01360 140 IHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKISG-AVGTYANLGPEveeRVAEKLG-LKP-------------E 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051752624 261 LIGSQ----DT-AVAVSgQLKATAVSLMKIANDLRwmnsgplaGL-----GEIElEGL---QPGSSIMPGKVNPVIPE 325
Cdd:cd01360 205 PISTQviqrDRhAEYLS-TLALIASTLEKIATEIR--------HLqrtevLEVE-EPFskgQKGSSAMPHKRNPILSE 272
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
279-452 |
1.08e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 46.17 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 279 AVSLMKIANDLRWMNsGPLAGLGEIELEGLQPGSSIMPGKVNPVIPEATAMVAAQVIGNdtVITVAG-QSGNFELNVMLP 357
Cdd:PRK08937 27 ATSLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY--LVTALEnVPLWHERDLSHS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 358 -----IIAQNLLSSLELLANASRLLADkaiasFKVNEAKLKQALSRN-------PILVTALNPIIGYQKAAEIAKQAY-- 423
Cdd:PRK08937 104 saeriALPDAFLALDYILNRFVNILEN-----LVVFPENIERNLDKTlgfiateRVLLELVEKGMGREEAHELIREKAme 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1051752624 424 --QQGRPVIDVALEHTD----LPRSQLEVLLDPEK 452
Cdd:PRK08937 179 awKNQKDLRELLEADERftkqLTKEELDELFDPEA 213
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
160-346 |
3.78e-05 |
|
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: 45.77 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 160 HLVQVIEQKAE--AVHPFIKT-GRTHLMDAMPVRMSQVLNGWAQQLKANIGHLQDLLPALQALAQGGTaVGTGinahPEF 236
Cdd:cd03302 118 KLAAVIDRLAEfaLEYKDLPTlGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQ----ASF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 237 AARFSGHLShltKVKftpgkNLFALIGSQ---DTAVAVSGQ-------------LKATAVSLMKIANDLRWMnsgplAGL 300
Cdd:cd03302 193 LDLFEGDHD---KVE-----ALDELVTKKagfKKVYPVTGQtysrkvdidvlnaLSSLGATAHKIATDIRLL-----ANL 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1051752624 301 GEIE--LEGLQPGSSIMPGKVNPVIPEATAMVAAQVIG--NDTVITVAGQ 346
Cdd:cd03302 260 KEVEepFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNlaSNAAQTASTQ 309
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
128-450 |
8.24e-05 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 45.01 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 128 VNCGQSSNDIIPT--TIHVSAALVLHEQTLPALLHLVQVIEQkAEAVHPFIktGRTHLMDAMPVRMSQVLNGWAQQLKAN 205
Cdd:PRK09053 102 VHWGATSQDIIDTglVLQLRDALDLLEPDLDRLCDALATLAA-RHRATPMV--GRTWLQQALPVTLGLKFAGWLDALLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 206 IGHLQDLLPALQALaQGGTAVGT----GINAhPEFAARFSGHLshltkvkftpGKNLFALI--GSQDTAVAVSGQLKATA 279
Cdd:PRK09053 179 RQRLAALRPRALVL-QFGGAAGTlaslGEQA-LPVAQALAAEL----------QLALPALPwhTQRDRIAEFASALGLLA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 280 VSLMKIANDLRWMNSGPLAGLGEIELEGlQPGSSIMPGKVNPVipEATAMVAAQVIGNDTVITV-AGQSGNFELNVMLPI 358
Cdd:PRK09053 247 GTLGKIARDVSLLMQTEVGEVFEPAAAG-KGGSSTMPHKRNPV--GCAAVLTAATRAPGLVATLfAAMPQEHERALGGWH 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 359 IAQNLLSSLELLANASRLLADKAIASFKVNEAKLKQAL--SRNPIL----VTALNPIIGYQKAAEI----AKQAYQQGRP 428
Cdd:PRK09053 324 AEWDTLPELACLAAGALAQMAQIVEGLEVDAARMRANLdlTHGLILaeavMLALADRIGRLDAHHLveqaSKRAVAEGRH 403
|
330 340
....*....|....*....|....*.
gi 1051752624 429 VIDVALEHTD----LPRSQLEVLLDP 450
Cdd:PRK09053 404 LRDVLAEDPQvsahLSPAALDRLLDP 429
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
128-336 |
5.06e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 39.45 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 128 VNCGQSSNDIIPTTihvsAALVLHEQTLPALLHLVQV---IEQKAEAVHPFIKTGRTHLMDAMPVRMSQVLNGWAQQLKA 204
Cdd:PRK02186 510 LQTARSRNDINATT----TKLHLREATSRAFDALWRLrraLVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALAR 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051752624 205 NIGHLQDLLPALQALAQG-GTAVGTGINAHPEFAARFSGhlshltkvkF-TPGKNLFALIGSQDTAVAVSGQLKATAVSL 282
Cdd:PRK02186 586 ETHALFALFEHIDVCPLGaGAGGGTTFPIDPEFVARLLG---------FeQPAPNSLDAVASRDGVLHFLSAMAAISTVL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1051752624 283 MKIANDLRwmnsgpLAGLGEIEL----EGLQPGSSIMPGKVNPVIPEATAMVAAQVIG 336
Cdd:PRK02186 657 SRLAQDLQ------LWTTREFALvslpDALTGGSSMLPQKKNPFLLEFVKGRAGVVAG 708
|
|
| |
