|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-462 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 965.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 1 MTTHRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 81 LAGKHPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 161 LPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHP 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 241 EYAVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 321 MPGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQ 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556282130 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVGS 462
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGP 462
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-461 |
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: 952.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 1 MTTHRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 81 LAGKHPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 161 LPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHP 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 241 EYAVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 321 MPGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQ 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556282130 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVG 461
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
5-459 |
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: 894.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGK 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 85 HPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKLLPSL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 165 QALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 245 RVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 325 VNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 556282130 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQM 459
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
4-461 |
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: 893.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 4 HRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAG 83
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 84 KHPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKLLPS 163
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 164 LQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYA 243
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 244 VRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPG 323
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 324 KVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLN 403
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 556282130 404 ESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVG 461
Cdd:TIGR00979 401 NSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
5-455 |
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: 820.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGK 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 85 HPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGmARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKLLPSL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 165 QALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 245 RVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 325 VNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 556282130 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVR 455
Cdd:cd01596 400 SLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
11-461 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 724.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 11 MGAIDVPADKLWGAQTQRSLEHFRIS--TEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGKHPQE 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 89 FPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKLLPSLQALR 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 169 ATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAVRVAA 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 249 ELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 329 QCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 556282130 409 VTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVG 461
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTG 453
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
5-462 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 618.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGK 84
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 85 HPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKLLPSL 164
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 165 QALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 245 RVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 325 VNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNE 404
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 556282130 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVGS 462
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
5-461 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 614.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPG--ELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLA 82
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 83 GKHPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREkLLP 162
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 163 SLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEY 242
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 243 AVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMP 322
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 323 GKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLL 402
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 556282130 403 NESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVG 461
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTG 458
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-461 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 595.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 1 MTTHRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKM--PGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAAD 78
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 79 EVLAGKHPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALRe 158
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 159 KLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNT 238
Cdd:PRK12273 161 KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 239 HPEYAVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGS 318
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 319 SIMPGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERI 398
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556282130 399 TQLLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVG 461
Cdd:PRK12273 401 REYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTH 463
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-451 |
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: 583.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGK 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 85 HPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALReKLLPSL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLR-KLLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 165 QALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 245 RVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 325 VNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 556282130 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFD 451
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELD 446
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
5-460 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 548.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGK 84
Cdd:PRK13353 6 RIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILAGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 85 HPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALrEKLLPSL 164
Cdd:PRK13353 86 LHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL-EGLLAAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 165 QALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:PRK13353 165 GALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYIE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 245 RVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:PRK13353 245 RVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPGK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 325 VNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNE 404
Cdd:PRK13353 325 VNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVEK 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 556282130 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMV 460
Cdd:PRK13353 405 SVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-460 |
5.06e-150 |
|
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: 435.41 E-value: 5.06e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPG--ELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVL- 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 82 AGKHPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALrEKLL 161
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSL-IKLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 162 PSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPE 241
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 242 YAVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIM 321
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 322 PGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQL 401
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 556282130 402 LNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMV 460
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLM 458
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
7.62e-142 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 408.68 E-value: 7.62e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 12 GAIDVPADKLWGAQTQRSLEHFRISTEKmpgelIYALALTKRAAAKVNQDlgllTAEKAGAIVAAADEVLA-GKHPQEFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVI----LKEEAAAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 91 LAIWQTGSGTQSNMNMNEVLANRasellggergMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALREKLLPSLQALRAT 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIGEL----------LGQLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 171 LNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHL-EASQPHLAELALGGTAVGTGLNTHPEYAVRVAAE 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLqQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 250 LASLSGQPfVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPrCGIGEIAIPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 556282130 330 CEALTMVCCQVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
5-459 |
1.08e-140 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 412.09 E-value: 1.08e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGK 84
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 85 HPQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALVALrEKLLPSL 164
Cdd:PRK14515 92 WHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNAL-EGLLQTM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 165 QALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:PRK14515 171 GYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 245 RVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:PRK14515 251 AVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 325 VNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERITQLLNE 404
Cdd:PRK14515 331 VNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEK 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 556282130 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQM 459
Cdd:PRK14515 411 SVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEM 465
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-394 |
5.40e-123 |
|
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: 361.05 E-value: 5.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 45 IYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGKHPQEFplaiWQTGSGTQSNMNMNEVLANRASELLGGergm 124
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 125 arKIHpnddvnkSQSSNDVFPTAMHVAALVALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGW 204
Cdd:cd01334 73 --YVH-------TGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 205 VAMLDHSLKHLEASQPHLAELALGGTAVGTGLNTHPEYAVRVAAELASlsgqpFVTAPNKFEALATVDALVHAHGALKGL 284
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 285 AASLMKIANDVRWLASGprcGIGEIAIPEN-EPGSSIMPGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRP 363
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 556282130 364 MVIHNFLQSVRLLADGMASFNEHCAvGIEPN 394
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVLE-GLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
104-384 |
3.05e-58 |
|
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: 191.67 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 104 MNMNEVLANRASELLGGErgmarkiHPNDDVNKSQSSNDVfPTAMHVAALVALREKLLPSLQALRATLNEKAVAFRDIVK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDI-GTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 184 IGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASqphlaelalggtavgtglnthpeyavrvaaelaslsgqpfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 264 kfealatvdALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPeNEPGSSIMPGKVNPTQCEALTMVCCQVMGN 343
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 556282130 344 DVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFN 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
140-465 |
4.67e-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: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 140 SNDVFPTAmHVAALVALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQ 219
Cdd:COG0015 99 SQDINDTA-LALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEAR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 220 PHLAELALGGtAVGTgLNTHPEYAVRVAAELAS---LSGQPFVT--APNKFEAlatvdALVHahgALKGLAASLMKIAND 294
Cdd:COG0015 178 ERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEklgLKPNPVTTqiEPRDRHA-----ELFS---ALALIAGSLEKIARD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 295 VRWLAsgpRCGIGEIA--IPENEPGSSIMPGKVNPTQCEaltmvccqvmgndvavNIGGASGnfelnVYRPMVIH----- 367
Cdd:COG0015 248 IRLLQ---RTEVGEVEepFAKGQVGSSAMPHKRNPIDSE----------------NIEGLAR-----LARALAAAlleal 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 368 ---------------NFLQSVRLLADGM-ASFNEHCAvGIEPNRERITQLLNESLMLV------TALNTH-IG----YDK 420
Cdd:COG0015 304 aswherdlsdssverNILPDAFLLLDGAlERLLKLLE-GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYEL 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 556282130 421 AAEIAKKAHHEGLTLKASALA----LGYLTEAEFDSWVRPEQMVGSLAT 465
Cdd:COG0015 383 VKELARGAWEEGNDLRELLAAdpeiPAELSKEELEALFDPANYLGAADE 431
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
140-433 |
3.40e-25 |
|
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: 106.43 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 140 SNDVFPTAmHVAALVALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQ 219
Cdd:cd01595 89 SQDINDTA-LALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEAR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 220 PHLAELALGGtAVGTGLNTHPEyAVRVAAELASLSGQPFVTAPNKfealaTVDALVHAH--GALKGLAASLMKIANDVRW 297
Cdd:cd01595 168 ERVLVGGISG-AVGTHASLGPK-GPEVEERVAEKLGLKVPPITTQ-----IEPRDRIAEllSALALIAGTLEKIATDIRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 298 LAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMVCCQVMGndvavNIGGASGNFELNVYRPM----VIHNFLQ 371
Cdd:cd01595 241 LQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRA-----LAAPALENLVQWHERDLsdssVERNILP 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556282130 372 SVRLLADGMASFNEHCAVGIEPNRERITQLLNESLMLV------TAL-NTHIGYDKAAEIAKKAHHEGL 433
Cdd:cd01595 313 DAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALaKKGLGRQEAYELVKEENYLGL 381
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
1.17e-24 |
|
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: 95.85 E-value: 1.17e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 556282130 408 LVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
164-462 |
1.49e-22 |
|
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: 99.63 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 164 LQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGGtAVGTglnthpeya 243
Cdd:cd01597 122 LDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT--------- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 244 vrvaaeLASLSGQPFVTAPNKFEAL----------ATVDALVHAHGALKGLAASLMKIANDVRWLAsgpRCGIGEIAIP- 312
Cdd:cd01597 192 ------LASLGDQGLAVQEALAAELglgvpaipwhTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPf 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 313 -ENEPGSSIMPGKVNPTQCEALTmVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGI 391
Cdd:cd01597 263 aKGRGGSSTMPHKRNPVGCELIV-ALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQAEFLLSGL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 392 EPNRERITQLLN--------ESLMLvtALNTHIGYDKA----AEIAKKAHHEGLTLKASALA----LGYLTEAEFDSWVR 455
Cdd:cd01597 342 EVNEDRMRANLDltgglilsEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpevAAYLSDEELDALLD 419
|
....*..
gi 556282130 456 PEQMVGS 462
Cdd:cd01597 420 PANYLGS 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
140-334 |
4.00e-19 |
|
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: 89.33 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 140 SNDVFPTAMHVAALVALrEKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQ 219
Cdd:TIGR00928 97 SNDIVDTALALLLRDAL-EIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 220 phlAELALGGT--AVGTGLNTHPEYAV--RVAAELASLSGQPFVTA--PNKFEAlATVDALVHahgalkgLAASLMKIAN 293
Cdd:TIGR00928 176 ---ERIKVGGIsgAVGTHAAAYPLVEEveERVTEFLGLKPVPISTQiePRDRHA-ELLDALAL-------LATTLEKFAV 244
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556282130 294 DVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALT 334
Cdd:TIGR00928 245 DIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVC 284
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
140-334 |
6.57e-19 |
|
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: 88.38 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 140 SNDVFPTAMhvaALVaLREK---LLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLE 216
Cdd:cd01360 91 SSDVVDTAL---ALQ-LREAldiILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 217 ASQPHLAELALGGtAVGTGLNTHPEYAVRVAAEL----ASLSGQpfVTAPNKFEALATVDALvhahgalkgLAASLMKIA 292
Cdd:cd01360 167 EARERILVGKISG-AVGTYANLGPEVEERVAEKLglkpEPISTQ--VIQRDRHAEYLSTLAL---------IASTLEKIA 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556282130 293 NDVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALT 334
Cdd:cd01360 235 TEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENIC 275
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
53-460 |
7.82e-18 |
|
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: 85.29 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 53 RAAAKVNQDLGLLTAEKAGAIVAAADEVLAGKHPQEFPLaiwqTGSGTQSNMNMNEVLANRASELlggergmARKIHpnd 132
Cdd:cd01359 17 IAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFEL----DPEDEDIHMAIERRLIERIGDV-------GGKLH--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 133 dvnKSQSSNDVFPTAMHVAALVALREkLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSL 212
Cdd:cd01359 83 ---TGRSRNDQVATDLRLYLRDALLE-LLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 213 KHLEASQPHLAELALGGTA-VGTGLNTHPEyavRVAAEL--ASLSgqpfvtaPNKFEALATVDALVHAHGALKGLAASLM 289
Cdd:cd01359 159 ERLADAYKRVNVSPLGAGAlAGTTFPIDRE---RTAELLgfDGPT-------ENSLDAVSDRDFVLEFLSAAALLMVHLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 290 KIANDVRWLASGPRcgiGEIAIPEN-EPGSSIMPGKVNPTQCEALTMVCCQVMGNDVAV-----NIGGASGNFELNVYRP 363
Cdd:cd01359 229 RLAEDLILWSTQEF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLlttlkGLPLAYNKDLQEDKEP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 364 M--VIHNFLQSVRLLAdGMASfnehcavGIEPNRERITQLLNESLMLVTAL------NTHI----GYDKAAEIAKKAHHE 431
Cdd:cd01359 306 LfdAVDTLIASLRLLT-GVIS-------TLTVNPERMREAAEAGFSTATDLadylvrEKGVpfreAHHIVGRAVRLAEEK 377
|
410 420 430
....*....|....*....|....*....|...
gi 556282130 432 GLTLKASALA----LGYLTEAEFDSWVRPEQMV 460
Cdd:cd01359 378 GKDLSDLTLAelqaISPLFEEDVREALDPENSV 410
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
53-343 |
7.28e-16 |
|
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: 79.32 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 53 RAAAKVNQDLGLLTAEKAGAIVAA----ADEVLAGKhpqefplAIWQTgsgTQSNMNMNevLANRASELLGgeRGMARKI 128
Cdd:TIGR00838 36 IAHTKMLKKAGILTEEEAAKIIEGlnelKEEGREGP-------FILDP---DDEDIHMA--IERELIDRVG--EDLGGKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 129 HpnddvnKSQSSNDVFPTAMHVAALVALREkLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAML 208
Cdd:TIGR00838 102 H------TGRSRNDQVATDLRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 209 DHSLKHLEASQPHLAELALGGTAV-GTGLNTHPEYavrvaaeLASLSGQPFVTApNKFEALATVDALVHAHGALKGLAAS 287
Cdd:TIGR00838 175 LRDYERLQDALKRVNVSPLGSGALaGTGFPIDREY-------LAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 556282130 288 LMKIANDVRWLASGPrcgIGEIAIP-ENEPGSSIMPGKVNPTQCEALTMVCCQVMGN 343
Cdd:TIGR00838 247 LSRFAEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
139-333 |
4.01e-15 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 77.36 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 139 SSNDVFPTAMhVAALVALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEAS 218
Cdd:PRK09053 107 TSQDIIDTGL-VLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 219 QPHLAELALGGtAVGTgLNTHPEYAVRVAAELAS-----LSGQPFVTAPnkfealatvDALVHAHGALKGLAASLMKIAN 293
Cdd:PRK09053 186 RPRALVLQFGG-AAGT-LASLGEQALPVAQALAAelqlaLPALPWHTQR---------DRIAEFASALGLLAGTLGKIAR 254
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556282130 294 DVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEAL 333
Cdd:PRK09053 255 DVSLLM---QTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAV 293
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-327 |
3.49e-13 |
|
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: 71.11 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 155 ALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEaSQPHLAelALGGtAVGT 234
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK-QIEILG--KFNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 235 gLNTH---------PEYAVRVAAELAsLSGQPFVTAPNKFEALATV-DALVHAHGALKGLAA------SLMKIANDVRwl 298
Cdd:cd01598 192 -FNAHlvaypdvdwRKFSEFFVTSLG-LTWNPYTTQIEPHDYIAELfDALARINTILIDLCRdiwgyiSLGYFKQKVK-- 267
|
170 180
....*....|....*....|....*....
gi 556282130 299 asgprcgigeiaipENEPGSSIMPGKVNP 327
Cdd:cd01598 268 --------------KGEVGSSTMPHKVNP 282
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
63-327 |
1.09e-10 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 63.25 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 63 GLLTAEKAGAIVAAADEVLAGKHPQEFPLAIwqtgsgtqSNMNMNEVLANRASELLGGErgmARKIHpnddvnKSQSSND 142
Cdd:PRK00855 51 GILSEEEAEKILAGLDEILEEIEAGKFEFSP--------ELEDIHMAIEARLTERIGDV---GGKLH------TGRSRND 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 143 vfptamHVAALV--ALREKLL---PSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEA 217
Cdd:PRK00855 114 ------QVATDLrlYLRDEIDeiaELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 218 SQPHLAELALGGTA-VGTGLNTHPEYavrVAAELAslsgqpfvtapnkFEALA--TVDA------LVHAHGALKGLAASL 288
Cdd:PRK00855 188 ARKRVNRSPLGSAAlAGTTFPIDRER---TAELLG-------------FDGVTenSLDAvsdrdfALEFLSAASLLMVHL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 556282130 289 MKIAND-VRWlaSGPRCGIgeIAIPEN-EPGSSIMPGKVNP 327
Cdd:PRK00855 252 SRLAEElILW--SSQEFGF--VELPDAfSTGSSIMPQKKNP 288
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
151-331 |
1.22e-10 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 63.11 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 151 AALVALREKL---LPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELAL 227
Cdd:cd03302 103 TDLIQIRDALdliLPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 228 GGTaVGTG---LNTHPEYAVRVAA---ELASLSGQPFV------TAPNKfealatVDALVHAhgALKGLAASLMKIANDV 295
Cdd:cd03302 183 KGT-TGTQasfLDLFEGDHDKVEAldeLVTKKAGFKKVypvtgqTYSRK------VDIDVLN--ALSSLGATAHKIATDI 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 556282130 296 RWLAsgprcGIGEIAIP--ENEPGSSIMPGKVNPTQCE 331
Cdd:cd03302 254 RLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSE 286
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
155-327 |
2.63e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 62.08 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 155 ALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEAsQPHLAElaLGGtAVGT 234
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEA-VEILGK--ING-AVGN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 235 gLNTH----PEY---AVrvaaelaslsGQPFVTAPN-KFEALATV----DALVHAHGALKGLAASLMKIANDVrWlasgp 302
Cdd:PRK09285 214 -YNAHlaayPEVdwhAF----------SREFVESLGlTWNPYTTQiephDYIAELFDAVARFNTILIDLDRDV-W----- 276
|
170 180 190
....*....|....*....|....*....|..
gi 556282130 303 rcgiGEIA-------IPENEPGSSIMPGKVNP 327
Cdd:PRK09285 277 ----GYISlgyfkqkTKAGEIGSSTMPHKVNP 304
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
1-347 |
4.89e-10 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 61.28 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 1 MTTHRSEKDSMGAIDVpadKLWGAQTQRS----LEHF--------RISTEKMPGELIYALALTKRaaakvnqdlGLLTAE 68
Cdd:PLN02646 1 ASTSMSASEEEAAKEK---KLWGGRFEEGvtpaVEKFnesisfdkRLYKEDIMGSKAHASMLAKQ---------GIITDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 69 KAGAIVAAADEVLAGKHPQEFplaIWQTGsgtQSNMNMNevLANRASELLGGergMARKIHpnddvnKSQSSNDVFPTAM 148
Cdd:PLN02646 69 DRDSILDGLDEIEKEIEAGKF---EWRPD---REDVHMN--NEARLTELIGE---PAKKLH------TARSRNDQVATDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 149 HVAALVALReKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALG 228
Cdd:PLN02646 132 RLWCRDAID-VIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 229 GTAV-GTGLNTHPEYavrVAAELAslsgqpfVTAP--NKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCG 305
Cdd:PLN02646 211 SCALaGTGLPIDRFM---TAKDLG-------FTAPmrNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGF 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 556282130 306 IgeiaIPEN--EPGSSIMPGKVNPTQCEALTMVCCQVMGNDVAV 347
Cdd:PLN02646 281 V----TPSDavSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTV 320
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
134-333 |
2.53e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 58.53 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 134 VNKSQSSNDVFPTAMhVAALVALREKLLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLK 213
Cdd:PRK05975 102 VHFGATSQDVIDTSL-MLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 214 HLEASQPHLAELALGGtAVGTGLNTHPEyAVRVAAELASLSGqpFVTAPnkfEALATVDALVHAHGALKGLAASLMKIAN 293
Cdd:PRK05975 181 RLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--LEDAP---QWHSQRDFIADFAHLLSLVTGSLGKFGQ 253
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556282130 294 DVRWLASGPrcgiGEIAIPENePGSSIMPGKVNPTQCEAL 333
Cdd:PRK05975 254 DIALMAQAG----DEISLSGG-GGSSAMPHKQNPVAAETL 288
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
134-327 |
1.57e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 50.62 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 134 VNKSQSSNDVFPTAmhvaALVALREKLLPSLQAL---RATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDH 210
Cdd:PRK02186 510 LQTARSRNDINATT----TKLHLREATSRAFDALwrlRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALAR 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 211 SLKHLEASQPHLAELALG-GTAVGTGLNTHPEYAvrvaaelASLSG--QPFvtaPNKFEALATVDALVHAHGALKGLAAS 287
Cdd:PRK02186 586 ETHALFALFEHIDVCPLGaGAGGGTTFPIDPEFV-------ARLLGfeQPA---PNSLDAVASRDGVLHFLSAMAAISTV 655
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556282130 288 LMKIANDVR-WLASgprcGIGEIAIPEN-EPGSSIMPGKVNP 327
Cdd:PRK02186 656 LSRLAQDLQlWTTR----EFALVSLPDAlTGGSSMLPQKKNP 693
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-461 |
1.03e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 46.56 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 280 ALKGLAASLMKIANDVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMVCCQVMGNdVAVNIGGASGNFE 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIGSERITGLARVLRSY-LVTALENVPLWHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 358 LNVY-----RPMVIHNFlqsvrLLADGMASFNEHCAVGIEPNRERITQLLNESL-------MLVTALNTHIG-------- 417
Cdd:PRK08937 98 RDLShssaeRIALPDAF-----LALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaheli 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556282130 418 YDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEQMVG 461
Cdd:PRK08937 173 REKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
160-342 |
2.74e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 43.05 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 160 LLPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAML--DHS-----LKHLEASqPhLAELALGGTAv 232
Cdd:PRK04833 128 LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLarDESrlqdaLKRLDVS-P-LGSGALAGTA- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 233 gtglnthpeYAV-RVAaeLASLSGqpFVTAPNKfeALATVDALVHAHGALKGLAASLM---KIANDVRWLASGpRCGIGE 308
Cdd:PRK04833 205 ---------YEIdREQ--LAGWLG--FASATRN--SLDSVSDRDHVLELLSDASISMVhlsRFAEDLIFFNSG-EAGFVE 268
|
170 180 190
....*....|....*....|....*....|....
gi 556282130 309 IAiPENEPGSSIMPGKVNPTQCEALTMVCCQVMG 342
Cdd:PRK04833 269 LS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQG 301
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
185-333 |
6.26e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 38.72 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556282130 185 GRTHLQDATPLTLGQEISGWVAMLDHSLKHLEASQPHLAELALGgtaVGTGLNTHPEYAVRVAAELASLsgQPFVTAPnK 264
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYG---YGSGYGSPSSVKFNQMSELLGM--EKNIKNP-V 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556282130 265 FEALATVDALVHAHGALKGLAASLMKIANDvrwLASGPRCGIGEIAiPENEPGSSIMPGKVNPTQCEAL 333
Cdd:PRK06389 221 YSSSLYIKTIENISYLISSLAVDLSRICQD---IIIYYENGIITIP-DEFTTGSSLMPNKRNPDYLELF 285
|
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