|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-461 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 912.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 1 MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQIL 80
Cdd:PRK00485 2 METRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 81 SGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQ-SDESIHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLE 159
Cdd:PRK00485 82 AGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELgSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 160 PALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPE 239
Cdd:PRK00485 162 PALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 240 FGDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIM 319
Cdd:PRK00485 242 FAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 320 PGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNY 399
Cdd:PRK00485 322 PGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKEL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446038383 400 LNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDPH 461
Cdd:PRK00485 402 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-458 |
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: 904.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 1 MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQIL 80
Cdd:COG0114 2 METRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 81 SGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYL-KDHQSDESIHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLE 159
Cdd:COG0114 82 AGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLgGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 160 PALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPE 239
Cdd:COG0114 162 PALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 240 FGDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIM 319
Cdd:COG0114 242 FAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 320 PGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNY 399
Cdd:COG0114 322 PGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEEL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446038383 400 LNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMV 458
Cdd:COG0114 402 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
4-457 |
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: 833.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 4 RIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGE 83
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 84 LDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYL-KDHQSDESIHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPAL 162
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLgGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 163 KLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEFGD 242
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 243 KVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGK 322
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 323 VNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQ 402
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446038383 403 SLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDM 457
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
3-458 |
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: 797.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 3 VRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSG 82
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 83 ELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDES-IHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPA 161
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQpVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 162 LKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEFG 241
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 242 DKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPG 321
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 322 KVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLN 401
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446038383 402 QSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMV 458
Cdd:TIGR00979 401 NSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMV 457
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
4-453 |
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: 787.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 4 RIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGE 83
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 84 LDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDESIHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPALK 163
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 164 LLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEFGDK 243
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 244 VAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGKV 323
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 324 NPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQS 403
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446038383 404 LMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIK 453
Cdd:cd01596 401 LMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
10-460 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 667.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 10 FGEIEVPADKYWGAQTERSKRNFPVG--KERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGELDEH 87
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 88 FPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDES-IHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPALKLLR 166
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSpVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 167 NTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGW----RYMLDRCETMLSeskkHILNLAIGGTAVGTGINAHPEFGD 242
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYatqvKYGLNRVQCTLP----RLYELAQGGTAVGTGLNTKKGFDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 243 KVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGK 322
Cdd:PLN00134 237 KIAAAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 323 VNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQ 402
Cdd:PLN00134 317 VNPTQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446038383 403 SLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDP 460
Cdd:PLN00134 397 SLMLVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
4-461 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 596.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 4 RIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPI--EVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILS 81
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 82 GELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSD-ESIHPNDDVNKSQSSNDTFPTAMHVALYQEVEtKLEP 160
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDyDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLR-ELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 161 ALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEF 240
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 241 GDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMP 320
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 321 GKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYL 400
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446038383 401 NQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDPH 461
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
4-460 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 592.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 4 RIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGE 83
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 84 LDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDES-IHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPAL 162
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSpVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 163 KLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEFGD 242
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 243 KVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGK 322
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 323 VNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQ 402
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446038383 403 SLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDP 460
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-461 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 573.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 1 MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERM---PiEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACD 77
Cdd:PRK12273 3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdyP-ELIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 78 QILSGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLkDHQSDE--SIHPNDDVNKSQSSNDTFPTAMHVALYQEVE 155
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELL-GHEKGEyqYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 156 tKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGIN 235
Cdd:PRK12273 161 -KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 236 AHPEFGDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPG 315
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 316 SSIMPGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEEN 395
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446038383 396 IDNYLNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDPH 461
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
4-449 |
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: 570.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 4 RIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGE 83
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 84 LDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDES-IHPNDDVNKSQSSNDTFPTAMHVALYQEVEtKLEPAL 162
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQyVHPNDHVNMSQSTNDVYPTALRLALILLLR-KLLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 163 KLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEFGD 242
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 243 KVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGK 322
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 323 VNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQ 402
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446038383 403 SLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFE 449
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELD 446
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
1-460 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 538.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 1 MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQIL 80
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 81 SGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDESI-HPNDDVNKSQSSNDTFPTAMHVALYQEVEtKLE 159
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYvSPNDHVNMAQSTNDVFPTAIRIAALNLLE-GLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 160 PALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPE 239
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 240 FGDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIM 319
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 320 PGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNY 399
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446038383 400 LNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDP 460
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHP 462
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
4-460 |
2.39e-153 |
|
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: 443.89 E-value: 2.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 4 RIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPI--EVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQIL- 80
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 81 SGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLkDHQSDE--SIHPNDDVNKSQSSNDTFPTAMHVALYQEVEtKL 158
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELM-GHQKGEyqYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLI-KL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 159 EPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHP 238
Cdd:TIGR00839 159 VDAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 239 EFGDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSI 318
Cdd:TIGR00839 239 EYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 319 MPGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDN 398
Cdd:TIGR00839 319 MPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446038383 399 YLNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDP 460
Cdd:TIGR00839 399 YVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
2-460 |
4.16e-141 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 412.86 E-value: 4.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 2 SVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILS 81
Cdd:PRK14515 10 GVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 82 GELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDES-IHPNDDVNKSQSSNDTFPTAMHVALYQEVEtKLEP 160
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHyISPNSHVNMAQSTNDAFPTAIHIATLNALE-GLLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 161 ALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEF 240
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 241 GDKVAQYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMP 320
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 321 GKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYL 400
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 401 NQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDP 460
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
11-340 |
4.04e-133 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 386.34 E-value: 4.04e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 11 GEIEVPADKYWGAQTERSKRNFPVGKErmpieVVYGFAQLKRAAALANFDLgklsEAKKDAIVYACDQIL-SGELDEHFP 89
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEE-----DIKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 90 LVVWQTGSGTQSNMNVNEVVSYVANMYLkdhqsdesiHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPALKLLRNTL 169
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIGELLGQLV---------HPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 170 KEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSES-KKHILNLAIGGTAVGTGINAHPEFGDKVAQYI 248
Cdd:pfam00206 143 KEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLlPRLLVLPLGGGTAVGTGLNADPEFAELVAKEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 249 SENTGYPfVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPrAGLAEISIPENEPGSSIMPGKVNPTQC 328
Cdd:pfam00206 223 GFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQL 300
|
330
....*....|..
gi 446038383 329 EMLTMVAVQVMG 340
Cdd:pfam00206 301 ELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
47-391 |
2.94e-115 |
|
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: 341.40 E-value: 2.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 47 FAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGELDEHFplvvWQTGSGTQSNMNVNEVVsyvANMYLKDhqsdesi 126
Cdd:cd01334 4 DLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVL---AERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 127 hPNDDVNKSQSSNDTFPTAMHVALYQEVEtKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYML 206
Cdd:cd01334 70 -NGGYVHTGRSSNDIVDTALRLALRDALD-ILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 207 DRCETMLSESKKHILNLAIGGTAVGTGINAHPEFGDKVAQYISEntgypFVSSENKFHALTAHDEVVQLHGTLKALAGDL 286
Cdd:cd01334 148 ERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLAVSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 287 MKIANDVRWLASGpraGLAEISIPEN-EPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMH 365
Cdd:cd01334 223 SKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVERE 299
|
330 340
....*....|....*....|....*.
gi 446038383 366 NTLQSIYLLADGMETFNNNCAvGIEP 391
Cdd:cd01334 300 ALPDSFDLLDAALRLLTGVLE-GLEV 324
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
103-382 |
8.83e-56 |
|
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: 185.12 E-value: 8.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 103 MNVNEVVSYVANMYLKDhqsdesIHPNDDVNKSQSSNDtFPTAMHVALYQEVETKLEPALKLLRNTLKEKEDKFDSIIKI 182
Cdd:cd01594 14 ALVEEVLAGRAGELAGG------LHGSALVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 183 GRTHLQDATPIKLGQEISGWRYMLDRCETMLSEskkhilnlaiggtavgtginahpefgdkvaqyisentgypfvssenk 262
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEE----------------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 263 fhaltAHdeVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPeNEPGSSIMPGKVNPTQCEMLTMVAVQVMGND 342
Cdd:cd01594 120 -----AA--VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446038383 343 TVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFN 382
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
158-455 |
4.52e-28 |
|
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: 115.57 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 158 LEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGtAVGTGiNAH 237
Cdd:COG0015 118 LLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGTY-AAH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 238 PEFGDKVAQYISENTGYpfvssenKFHALT----AHDEVVQLHGTLKALAGDLMKIANDVRWLAsgpRAGLAEIS--IPE 311
Cdd:COG0015 196 GEAWPEVEERVAEKLGL-------KPNPVTtqiePRDRHAELFSALALIAGSLEKIARDIRLLQ---RTEVGEVEepFAK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 312 NEPGSSIMPGKVNPTQCEMLTMVAVQVMGNdtvVGFASSQGNFElnvykpvimH-----------NTLQSIYLLADGM-E 379
Cdd:COG0015 266 GQVGSSAMPHKRNPIDSENIEGLARLARAL---AAALLEALASW---------HerdlsdssverNILPDAFLLLDGAlE 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 380 TFNNNCAvGIEPIEENIDNYLNQSLMLV------TALNPH-IG----YEKAAQIAKKAHKEGLTLKEsAIQ-----TGYV 443
Cdd:COG0015 334 RLLKLLE-GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRE-LLAadpeiPAEL 411
|
330
....*....|..
gi 446038383 444 TEEQFEAWIKPE 455
Cdd:COG0015 412 SKEELEALFDPA 423
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
406-457 |
2.70e-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: 100.47 E-value: 2.70e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446038383 406 LVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDM 457
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
158-427 |
6.23e-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: 102.97 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 158 LEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGtAVGTGINAH 237
Cdd:cd01595 108 ILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHASLG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 238 PEfGDKVAQYISENTGYpfvssenKFHALT----AHDEVVQLHGTLKALAGDLMKIANDVRWLAsgpRAGLAEISIP--E 311
Cdd:cd01595 187 PK-GPEVEERVAEKLGL-------KVPPITtqiePRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 312 NEPGSSIMPGKVNPTQCEMLTMVAVQVMGN-----DTVV------GFASSqgnfelnvykpvIMHNTLQSIYLLADGMET 380
Cdd:cd01595 256 GQVGSSTMPHKRNPIDSENIEGLARLVRALaapalENLVqwherdLSDSS------------VERNILPDAFLLLDAALS 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446038383 381 FNNNCAVGIEPIEENIDNYLNQSLMLV------TALNPH-IGYEKAAQIAKKAH 427
Cdd:cd01595 324 RLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
138-455 |
4.61e-22 |
|
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: 98.19 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 138 SNDTFPTAMHVALYQEVETkLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESK 217
Cdd:TIGR00928 97 SNDIVDTALALLLRDALEI-ILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 218 KHILNLAIGGtAVGTGINAHPEFGDkVAQYISENTGYPFVSSENKFHALTAHDEVVQlhgTLKALAGDLMKIANDVRWLA 297
Cdd:TIGR00928 176 ERIKVGGISG-AVGTHAAAYPLVEE-VEERVTEFLGLKPVPISTQIEPRDRHAELLD---ALALLATTLEKFAVDIRLLQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 298 sgpRAGLAEISIP--ENEPGSSIMPGKVNPTQCEmltmvavQVMGNDTVV-GFASSQGN-----FELNVYKPVIMHNTLQ 369
Cdd:TIGR00928 251 ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFE-------NVCGLARVIrGYASPALEnaplwHERDLTDSSVERVILP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 370 SIYLLADGM-ETFNN---NCAVGIEPIEENIDNYLN----QSLMLVTALNpHIGYEKAAQIAKK-----AHKEGLTLKES 436
Cdd:TIGR00928 321 DAFILADIMlKTTLKvvkKLVVNPENILRNLDLTLGliasERVLIALVER-GMGREEAYEIVRElamgaAEVDEPDLLEF 399
|
330 340
....*....|....*....|...
gi 446038383 437 AIQ----TGYVTEEQFEAWIKPE 455
Cdd:TIGR00928 400 LLEderiTKYLKEEELAELLDPE 422
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
182-459 |
1.33e-21 |
|
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: 96.54 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 182 IGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGtAVGTginaHPEFGDK---VAQYISENTGY--PF 256
Cdd:cd01597 142 VGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT----LASLGDQglaVQEALAAELGLgvPA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 257 VSSenkfHalTAHDEVVQLHGTLKALAGDLMKIANDVRWLAsgpRAGLAEISIP--ENEPGSSIMPGKVNPTQCEMLTMV 334
Cdd:cd01597 217 IPW----H--TARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGGSSTMPHKRNPVGCELIVAL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 335 AVQVMGNDTVVgFASSQGNFELN--------VYKPVIMHNT---LQSIYLLADGMEtfnnncaVGIEPIEENIDnyLNQS 403
Cdd:cd01597 288 ARRVPGLAALL-LDAMVQEHERDagawhaewIALPEIFLLAsgaLEQAEFLLSGLE-------VNEDRMRANLD--LTGG 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446038383 404 LML----VTALNPHIG----YEKAAQIAKKAHKEGLTLKESAIQ----TGYVTEEQFEAWIKPE-------DMVD 459
Cdd:cd01597 358 LILseavMMALAPKLGrqeaHDLVYEACMRAVEEGRPLREVLLEdpevAAYLSDEELDALLDPAnylgsapALVD 432
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
138-335 |
1.16e-15 |
|
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: 78.36 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 138 SNDTFPTAMHVALYQEVETkLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESK 217
Cdd:cd01360 91 SSDVVDTALALQLREALDI-ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEAR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 218 KHILNLAIGGtAVGTGINAHPEFGDKVAQYIsentGYPFVSSENKFHALTAHDEVVQlhgTLKALAGDLMKIANDVRWLA 297
Cdd:cd01360 170 ERILVGKISG-AVGTYANLGPEVEERVAEKL----GLKPEPISTQVIQRDRHAEYLS---TLALIASTLEKIATEIRHLQ 241
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446038383 298 sgpRAGLAEISIP--ENEPGSSIMPGKVNPTQCEMLTMVA 335
Cdd:cd01360 242 ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
137-341 |
3.94e-14 |
|
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: 73.93 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 137 SSNDTFPTAMHVALYQEVETkLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSES 216
Cdd:TIGR00838 106 SRNDQVATDLRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 217 KKHILNLAIGGTAV-GTGINAHPEfgdkvaqYISENTGYPFVSsENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRW 295
Cdd:TIGR00838 185 LKRVNVSPLGSGALaGTGFPIDRE-------YLAELLGFDAVT-ENSLDAVSDRDFILELLFVAALIMVHLSRFAEDLIL 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446038383 296 LASGpRAGLAEISiPENEPGSSIMPGKVNPTQCEMLTMVAVQVMGN 341
Cdd:TIGR00838 257 WSTG-EFGFVELP-DEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
182-340 |
1.15e-13 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 72.74 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 182 IGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGtAVGTgINAHPEFGDKVAQYISENTGYPFvsSEN 261
Cdd:PRK09053 151 VGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGT-LASLGEQALPVAQALAAELQLAL--PAL 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446038383 262 KFHalTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPeNEPGSSIMPGKVNPTQCEMLTMVAVQVMG 340
Cdd:PRK09053 227 PWH--TQRDRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPAAA-GKGGSSTMPHKRNPVGCAAVLTAATRAPG 302
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
167-400 |
1.19e-09 |
|
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: 60.02 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 167 NTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRY--MLDRCEtmLSESKKHILNLAIGGTaVGTGINAHPEFG--- 241
Cdd:cd03302 124 DRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQdlLMDLRN--LERLRDDLRFRGVKGT-TGTQASFLDLFEgdh 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 242 DKVAQ---YISENTGYPfvssenKFHALTA------HDevVQLHGTLKALAGDLMKIANDVRWLasgprAGLAEISIP-- 310
Cdd:cd03302 201 DKVEAldeLVTKKAGFK------KVYPVTGqtysrkVD--IDVLNALSSLGATAHKIATDIRLL-----ANLKEVEEPfe 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 311 ENEPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTVVGF-ASSQGnFELNVYKPVIMHNTLQSIYLLADG-METFNN---NC 385
Cdd:cd03302 268 KGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQtASTQW-FERTLDDSANRRIAIPEAFLAADAiLITLQNiseGL 346
|
250
....*....|....*
gi 446038383 386 AVGIEPIEENIDNYL 400
Cdd:cd03302 347 VVYPKVIERHIRQEL 361
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
150-325 |
2.72e-09 |
|
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: 58.79 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 150 LYQEVETKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKkhILnLAIGGtA 229
Cdd:cd01598 113 IKEARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQIE--IL-GKFNG-A 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 230 VGTgINAHpefgdKVA------QYISENtgypFVSSEN-KFHALTA----HDEVVQLHGTLKALAGDLMKIANDV----- 293
Cdd:cd01598 189 VGN-FNAH-----LVAypdvdwRKFSEF----FVTSLGlTWNPYTTqiepHDYIAELFDALARINTILIDLCRDIwgyis 258
|
170 180 190
....*....|....*....|....*....|...
gi 446038383 294 -RWLASGPRAGlaeisipenEPGSSIMPGKVNP 325
Cdd:cd01598 259 lGYFKQKVKKG---------EVGSSTMPHKVNP 282
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
183-340 |
2.01e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 55.83 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 183 GRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGtAVGTGINAHPEfGDKVAQYISENTGYPFVSsenk 262
Cdd:PRK05975 152 GHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLGLEDAP---- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 263 fHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLAsgpRAGlAEISIPENEpGSSIMPGKVNPTQCEMLTMV----AVQV 338
Cdd:PRK05975 226 -QWHSQRDFIADFAHLLSLVTGSLGKFGQDIALMA---QAG-DEISLSGGG-GSSAMPHKQNPVAAETLVTLarfnATQV 299
|
..
gi 446038383 339 MG 340
Cdd:PRK05975 300 SG 301
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
278-455 |
1.78e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 51.57 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 278 TLKALAGDLMKIANDVRWLAsGPRAGLAEISIPENEPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQ---GNF 354
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLwheRDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 355 ELNVYKPVImhntLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQSL-------MLVTALNPHIG----YEKAAQIA 423
Cdd:PRK08937 101 SHSSAERIA----LPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaHELIREKA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 446038383 424 KKAHKEGLTLKESAIQ----TGYVTEEQFEAWIKPE 455
Cdd:PRK08937 177 MEAWKNQKDLRELLEAderfTKQLTKEELDELFDPE 212
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
117-459 |
2.90e-07 |
|
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: 52.55 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 117 LKDHQSDESIHPN----------DDVNKSQ---SSNDTFPTAMHVALYQEVETKLEpALKLLRNTLKEKEDKFDSIIKIG 183
Cdd:cd01359 53 FELDPEDEDIHMAierrlierigDVGGKLHtgrSRNDQVATDLRLYLRDALLELLE-LLLDLQRALLDRAEEHADTIMPG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 184 RTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTA-VGTGINAHPEFgdkVAQY-----ISENTGYpfV 257
Cdd:cd01359 132 YTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVSPLGAGAlAGTTFPIDRER---TAELlgfdgPTENSLD--A 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 258 SSENKFHA-LTAHDEVVQLHgtLKALAGDLMkiandvrwLASGPRAGLAEISipenEP---GSSIMPGKVNPTQCEMLTM 333
Cdd:cd01359 207 VSDRDFVLeFLSAAALLMVH--LSRLAEDLI--------LWSTQEFGFVELP----DAystGSSIMPQKKNPDVLELIRG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 334 VAVQVMGNdtVVGFassqgnfeLNVYK--PVIMHNTLQSIY-LLADGMETFNNNCAV------GIEPIEENIDNYLNQSL 404
Cdd:cd01359 273 KAGRVIGA--LAGL--------LTTLKglPLAYNKDLQEDKePLFDAVDTLIASLRLltgvisTLTVNPERMREAAEAGF 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446038383 405 MLVTALN---------P-HIGYEKAAQIAKKAHKEGLTLKE---SAIQTG-YVTEEQFEAWIKPEDMVD 459
Cdd:cd01359 343 STATDLAdylvrekgvPfREAHHIVGRAVRLAEEKGKDLSDltlAELQAIsPLFEEDVREALDPENSVE 411
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
154-325 |
7.27e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 45.13 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 154 VETKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLseskKHILNLA-IGGtAVGT 232
Cdd:PRK09285 139 REEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQL----EAVEILGkING-AVGN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 233 gINAH----PEFgDKVAqyISENtgypFVSS-ENKFHALTA----HDEVVQLHGTLKALAGDLMKIANDVrW-------L 296
Cdd:PRK09285 214 -YNAHlaayPEV-DWHA--FSRE----FVESlGLTWNPYTTqiepHDYIAELFDAVARFNTILIDLDRDV-WgyislgyF 284
|
170 180
....*....|....*....|....*....
gi 446038383 297 ASGPRAGlaEIsipenepGSSIMPGKVNP 325
Cdd:PRK09285 285 KQKTKAG--EI-------GSSTMPHKVNP 304
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
136-331 |
8.75e-05 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 44.77 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 136 QSSNDTFPTAMHVALYQEVEtKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSE 215
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQGQ-QLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLED 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 216 SKKHILNLAIG-GTAVGTginAHPEFGDKVAQyiseNTGYPfVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVR 294
Cdd:PRK12308 186 ALTRLDTCPLGsGALAGT---AYPIDREALAH----NLGFR-RATRNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLI 257
|
170 180 190
....*....|....*....|....*....|....*..
gi 446038383 295 WLASGpRAGLAEISiPENEPGSSIMPGKVNPTQCEML 331
Cdd:PRK12308 258 FYNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELI 292
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
149-329 |
1.13e-04 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 44.34 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 149 ALYQEVETKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKkhILNLAIGgt 228
Cdd:PLN02848 137 MLKEGVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVK--IKGKFAG-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 229 AVGTgINAH----PEFG-DKVAQYISENTGY---PFVSSenkfhaLTAHDEVVQLHGTLKALAGDLMKIANDVRWLASgp 300
Cdd:PLN02848 213 AVGN-YNAHmsayPEVDwPAVAEEFVTSLGLtfnPYVTQ------IEPHDYMAELFNAVSRFNNILIDFDRDIWSYIS-- 283
|
170 180
....*....|....*....|....*....
gi 446038383 301 RAGLAEISIPeNEPGSSIMPGKVNPTQCE 329
Cdd:PLN02848 284 LGYFKQITKA-GEVGSSTMPHKVNPIDFE 311
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
52-345 |
5.03e-04 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 42.40 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 52 RAAALANFDLGKLSEAKKDAIVYACDQILSGELDEHFplvVWQTGsgtqsnmnvnevvsyvanmylkdhqsDESIHPNDD 131
Cdd:PLN02646 53 KAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKF---EWRPD--------------------------REDVHMNNE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 132 -------------VNKSQSSNDTFPTAMHVALYQEVEtKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQE 198
Cdd:PLN02646 104 arlteligepakkLHTARSRNDQVATDTRLWCRDAID-VIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHW 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 199 ISGWRYMLDRCETMLSESKKHILNLAIGGTAV-GTGinahpeFG-DKvaQYISENTGYPFVSSeNKFHALTAHDEVVQLH 276
Cdd:PLN02646 183 LLSHVEQLERDAGRLVDCRPRVNFCPLGSCALaGTG------LPiDR--FMTAKDLGFTAPMR-NSIDAVSDRDFVLEFL 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446038383 277 GTLKALAGDLMKIANDVRWLASGPRAGLaeisIPEN--EPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTVV 345
Cdd:PLN02646 254 FANSITAIHLSRLGEEWVLWASEEFGFV----TPSDavSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTV 320
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
137-331 |
7.55e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 41.90 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 137 SSNDTFPTAMHVALYQEVeTKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSES 216
Cdd:PRK04833 108 SRNDQVATDLKLWCKDQV-AELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038383 217 KKHiLN---LAIGGTAvGTginAHPEFGDKVAQYISentgypFVS-SENKFHALTAHDEVVQLHGTLKALAGDLMKIAND 292
Cdd:PRK04833 187 LKR-LDvspLGSGALA-GT---AYEIDREQLAGWLG------FASaTRNSLDSVSDRDHVLELLSDASISMVHLSRFAED 255
|
170 180 190
....*....|....*....|....*....|....*....
gi 446038383 293 VRWLASGpRAGLAEISiPENEPGSSIMPGKVNPTQCEML 331
Cdd:PRK04833 256 LIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELI 292
|
|
| |
