|
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: 917.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 1 MTAMRVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 81 IDGFRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 161 LPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHP 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 241 EYAVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 321 MPGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQ 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553831256 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVGS 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: 912.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 1 MTAMRVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 81 IDGFRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 161 LPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHP 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 241 EYAVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 321 MPGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQ 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553831256 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVG 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: 857.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 5 RVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVIDGF 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 85 RYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQLLPQM 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 165 DVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 245 RVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 325 VNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLLNE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2553831256 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDM 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: 844.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 4 MRVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVIDG 83
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 84 FRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQLLPQ 163
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 164 MDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEYA 243
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 244 VRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG 323
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 324 KVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLLN 403
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553831256 404 ESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVG 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: 784.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 5 RVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVIDGF 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 85 RYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGnERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQLLPQM 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 165 DVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 245 RVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 325 VNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLLNE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2553831256 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVR 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: 698.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 11 MGDIDVPQARLWGAQTQRSLEHFRISV--EKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVIDGFRYQE 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGerERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 89 FPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQLLPQMDVLI 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 169 QTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEYAVRVAK 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 249 AIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 329 QCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLLNESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2553831256 409 VTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVG 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: 588.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 5 RVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVIDGF 84
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 85 RYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQLLPQM 164
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 165 DVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEYAV 244
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 245 RVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 325 VNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLLNE 404
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553831256 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVGS 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: 575.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 5 RVERDSMGDIDVPQARLWGAQTQRSLEHFRIS---VEKMPQaLIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVI 81
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISgrpISDHPE-LIRALAMVKKAAALANRELGLLDKEKADAIVAACDEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 82 DGFRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQqLL 161
Cdd:COG1027 80 AGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 162 PQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPE 241
Cdd:COG1027 159 EALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 242 YAVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:COG1027 239 YIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 322 PGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQL 401
Cdd:COG1027 319 PGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREY 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 402 LNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVG 461
Cdd:COG1027 399 VENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTG 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: 567.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 1 MTAMRVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQ--ALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQ 78
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDypELIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 79 EVIDGFRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQ 158
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 159 qLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNT 238
Cdd:PRK12273 162 -LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 239 HPEYAVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGS 318
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 319 SIMPGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRI 398
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553831256 399 NQLLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVG 461
Cdd:PRK12273 401 REYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTH 463
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-452 |
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: 557.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 5 RVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVIDGF 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 85 RYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQqLLPQM 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 165 DVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 245 RVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 325 VNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLLNE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2553831256 405 SLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDE 452
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
2-460 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 525.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 2 TAMRVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVI 81
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 82 DGFRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQqLL 161
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG-LL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 162 PQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPE 241
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 242 YAVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 322 PGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQL 401
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553831256 402 LNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMV 460
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-465 |
1.18e-139 |
|
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: 409.22 E-value: 1.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 5 RVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKM--PQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVID 82
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKIsdIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 83 GFRYQ-EFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIrQQLL 161
Cdd:TIGR00839 81 NGKCHdQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSL-IKLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 162 PQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPE 241
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 242 YAVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 322 PGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQL 401
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553831256 402 LNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVGSTIR 465
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYK 463
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-459 |
3.31e-135 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 398.22 E-value: 3.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 3 AMRVERDSMGDIDVPQARLWGAQTQRSLEHFRISVEKMPQALIDALAVVKKAAAQVNLDLGLLSEEKAEAIMQAAQEVID 82
Cdd:PRK14515 10 GVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 83 GFRYQEFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGNERKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIrQQLLP 162
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNAL-EGLLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 163 QMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTAVGTGLNTHPEY 242
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 243 AVRVAKAIAQLSGCDFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPENEPGSSIMP 322
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 323 GKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFNEHCARGIEPNRPRINQLL 402
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553831256 403 NESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDM 459
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEM 465
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
3.13e-128 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 374.01 E-value: 3.13e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 12 GDIDVPQARLWGAQTQRSLEHFRISVEKmpqalIDALAVVKKAAAQVNLDLgllsEEKAEAIMQAAQEVIDGFRY-QEFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAEEGKLdDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 91 LAVWQTGSGTQSNMNMNEVLAnrasELLGgergneRKVHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQQLLPQMDVLIQT 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 171 LQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGL-EHLYELALGGTAVGTGLNTHPEYAVRVAKA 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLpRLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 250 IAQLSGCDfVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASGPrCGIGEISIPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 2553831256 330 CEAVTMLCAQVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
57-394 |
7.64e-119 |
|
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: 350.65 E-value: 7.64e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 57 QVNLDLGLLSEEKAEAIMQAAQEVIDGFryqeFPLAVWQTGSGTQSNMNMNEVLANRASELLGGergnerKVHpnddvnk 136
Cdd:cd01334 13 KALAELGLLPKEAAEAILAALDEILEGI----AADQVEQEGSGTHDVMAVEEVLAERAGELNGG------YVH------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 137 SQSSNDVFPTAMHVAAVVAIRQQLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIE 216
Cdd:cd01334 76 TGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 217 YGLEHLYELALGGTAVGTGLNTHPEYAVRVAKAIAQlsgcdFVTAPNKFEALASCDGLVQAHGALKGLAASMMKIANDVR 296
Cdd:cd01334 156 EALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 297 WLASGprcGIGEISIPEN-EPGSSIMPGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNFELNVFRPLVIHNFLQSVRL 375
Cdd:cd01334 231 LLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDL 307
|
330
....*....|....*....
gi 2553831256 376 LADGIESFNEHCaRGIEPN 394
Cdd:cd01334 308 LDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
104-384 |
2.22e-59 |
|
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: 194.36 E-value: 2.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 104 MNMNEVLANRASELLGGErgnerkvHPNDDVNKSQSSNDVFPTAMHVAAVVAIRQqLLPQMDVLIQTLQGKSDQFRHIVK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDIGTTALRLALRDALDD-LLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 184 IGRTHLQDATPLTLGQEISGWVAMLvhskkhiEYGLEHLYELALggtavgtglnthpeyavrvakaiaqlsgcdfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVL-------GRDLERLEEAAV------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 264 kfealascdglVQAHGALKGLAASMMKIANDVRWLASGPRCGIGEISIPeNEPGSSIMPGKVNPTQCEAVTMLCAQVMGN 343
Cdd:cd01594 123 -----------AEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2553831256 344 DVAVNIGGASGNFELNVFRPLVIHNFLQSVRLLADGIESFN 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
140-461 |
9.58e-27 |
|
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: 111.71 E-value: 9.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 140 SNDVFPTAMhvaaVVAIRQ---QLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIE 216
Cdd:COG0015 99 SQDINDTAL----ALQLREaleLLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 217 YGLEHLYELALGGtAVGTgLNTHPEYAVRVAKAIAQLSGcdfvtapnkFEAL------ASCDGLVQAHGALKGLAASMMK 290
Cdd:COG0015 175 EARERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEKLG---------LKPNpvttqiEPRDRHAELFSALALIAGSLEK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 291 IANDVRWLAsgpRCGIGEIS--IPENEPGSSIMPGKVNPTQCEAVTMLCAQVMGNdVAV---NI-------GGASGNfEL 358
Cdd:COG0015 244 IARDIRLLQ---RTEVGEVEepFAKGQVGSSAMPHKRNPIDSENIEGLARLARAL-AAAlleALaswherdLSDSSV-ER 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 359 NVFRPLVIHnFLQSVRLLADGIEsfnehcarGIEPNRPRINQLLNESLMLV------TALNTH-IG----YDKAAEIAKK 427
Cdd:COG0015 319 NILPDAFLL-LDGALERLLKLLE--------GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARG 389
|
330 340 350
....*....|....*....|....*....|....*...
gi 2553831256 428 AHHEGLTLKE----SALMLGYVTAAQFDEWVRPQDMVG 461
Cdd:COG0015 390 AWEEGNDLREllaaDPEIPAELSKEELEALFDPANYLG 427
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
5.04e-26 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 99.70 E-value: 5.04e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2553831256 408 LVTALNTHIGYDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
160-433 |
2.72e-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: 106.82 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 160 LLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGtAVGTGLNTH 239
Cdd:cd01595 108 ILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHASLG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 240 PEyAVRVAKAIAQLSGCDFVTAPNKFEalaSCDGLVQAHGALKGLAASMMKIANDVRWLAsgpRCGIGEISIP--ENEPG 317
Cdd:cd01595 187 PK-GPEVEERVAEKLGLKVPPITTQIE---PRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQVG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 318 SSIMPGKVNPTQCEAVTMLCAQVMGNdvaVNIGGASGNFELNvfRPL----VIHNFLQSVRLLADGIESFNEHCARGIEP 393
Cdd:cd01595 260 SSTMPHKRNPIDSENIEGLARLVRAL---AAPALENLVQWHE--RDLsdssVERNILPDAFLLLDAALSRLQGLLEGLVV 334
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2553831256 394 NRPRINQLLNESLMLV------TAL-NTHIGYDKAAEIAKKAHHEGL 433
Cdd:cd01595 335 NPERMRRNLDLTWGLIlseavmMALaKKGLGRQEAYELVKEENYLGL 381
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
160-462 |
8.13e-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: 97.31 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 160 LLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGtAVGTgLNTH 239
Cdd:cd01597 118 LERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT-LASL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 240 PEYAVRVAKAIAQLSGCDFVTAPnkfeALASCDGLVQAHGALKGLAASMMKIANDVRWLAsgpRCGIGEISIP--ENEPG 317
Cdd:cd01597 196 GDQGLAVQEALAAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 318 SSIMPGKVNPTQCEAVTMLCAQVMGNdVAVNIGGASGNFElnvfRPL-VIHNFLQSVR---LLADGIESFNEHCARGIEP 393
Cdd:cd01597 269 SSTMPHKRNPVGCELIVALARRVPGL-AALLLDAMVQEHE----RDAgAWHAEWIALPeifLLASGALEQAEFLLSGLEV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 394 NRPRINQLLN--------ESLMLvtALNTHIGYDKA----AEIAKKAHHEGLTLKE----SALMLGYVTAAQFDEWVRPQ 457
Cdd:cd01597 344 NEDRMRANLDltgglilsEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREvlleDPEVAAYLSDEELDALLDPA 421
|
....*
gi 2553831256 458 DMVGS 462
Cdd:cd01597 422 NYLGS 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
134-465 |
5.94e-18 |
|
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: 85.86 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 134 VNKSQSSNDVFPTAMhvaaVVAIRQQL---LPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVA-MLV 209
Cdd:TIGR00928 91 IHFGATSNDIVDTAL----ALLLRDALeiiLPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEeMLR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 210 HskkhieygLEHLYEL----ALGGT--AVGTGLNTHPEYAvRVAKAIAQLSGCDFVTAPNKFEalaSCDGLVQAHGALKG 283
Cdd:TIGR00928 167 Q--------LERLLQAkeriKVGGIsgAVGTHAAAYPLVE-EVEERVTEFLGLKPVPISTQIE---PRDRHAELLDALAL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 284 LAASMMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAVTMLCAQVMGNDVAVNIGGASGNfELNVF 361
Cdd:TIGR00928 235 LATTLEKFAVDIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWH-ERDLT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 362 RPLVIHNFLQSVRLLADGI-----------ESFNEHCARGIEPNRPrinqLLNESLMLVTALNTHIGYDKAAEIAKK--- 427
Cdd:TIGR00928 311 DSSVERVILPDAFILADIMlkttlkvvkklVVNPENILRNLDLTLG----LIASERVLIALVERGMGREEAYEIVRElam 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2553831256 428 --AHHEGLTLKESALMLG----YVTAAQFDEWVRPQDMVGSTIR 465
Cdd:TIGR00928 387 gaAEVDEPDLLEFLLEDEritkYLKEEELAELLDPETYIGNAGE 430
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
62-343 |
6.75e-15 |
|
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: 76.62 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 62 LGLLSEEKAEAIMQAAQEVIDGFRYQEFPLAVwqtgsgTQSNMNMNevLANRASELLGGERGneRKVHpnddvnKSQSSN 141
Cdd:TIGR00838 45 AGILTEEEAAKIIEGLNELKEEGREGPFILDP------DDEDIHMA--IERELIDRVGEDLG--GKLH------TGRSRN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 142 DVFPTAMHVAA---VVAIRQQLLPQMDVLIQTLQGKSDqfrhIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYG 218
Cdd:TIGR00838 109 DQVATDLRLYLrdhVLELAEALLDLQDALIELAEKHVE----TLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 219 LEHLYELALGGTAV-GTGLNTHPEYavrvakaIAQLSGCDFVTApNKFEALASCDGLVQAHGALKGLAASMMKIANDVRW 297
Cdd:TIGR00838 185 LKRVNVSPLGSGALaGTGFPIDREY-------LAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLIL 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2553831256 298 LASGPrcgIGEISIP-ENEPGSSIMPGKVNPTQCEAVTMLCAQVMGN 343
Cdd:TIGR00838 257 WSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
140-337 |
5.68e-14 |
|
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: 73.36 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 140 SNDVFPTAMHVAAVVAIRQqLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVA-------MLVHSK 212
Cdd:cd01360 91 SSDVVDTALALQLREALDI-ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAefkrhleRLKEAR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 213 KHIEYGlehlyelALGGtAVGTGLNTHPEyavrVAKAIAQLSGCDFVTAPNKfeaLASCDGLVQAHGALKGLAASMMKIA 292
Cdd:cd01360 170 ERILVG-------KISG-AVGTYANLGPE----VEERVAEKLGLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIA 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2553831256 293 NDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAVTMLC 337
Cdd:cd01360 235 TEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
147-461 |
2.75e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 68.50 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 147 AMHVAAVVAIRQ---QLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLY 223
Cdd:PRK09053 111 IIDTGLVLQLRDaldLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 224 ELALGGtAVGTgLNTHPEYAVRVAKAIAQLSGCDFVTAPNKFEAlascDGLVQAHGALKGLAASMMKIANDVRWLAsgpR 303
Cdd:PRK09053 191 VLQFGG-AAGT-LASLGEQALPVAQALAAELQLALPALPWHTQR----DRIAEFASALGLLAGTLGKIARDVSLLM---Q 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 304 CGIGEISIP--ENEPGSSIMPGKVNPTQCEAV------------TMLCAQVMGNDVAVniGGASGNFELnvfrplvihnf 369
Cdd:PRK09053 262 TEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERAL--GGWHAEWDT----------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 370 LQSVRLLADGIESFNEHCARGIEPNRPRINQ--------LLNESLMLvtALNTHIGYDKAAEI----AKKAHHEGLTLK- 436
Cdd:PRK09053 329 LPELACLAAGALAQMAQIVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEGRHLRd 406
|
330 340
....*....|....*....|....*...
gi 2553831256 437 ---ESALMLGYVTAAQFDEWVRPQDMVG 461
Cdd:PRK09053 407 vlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
63-412 |
3.77e-12 |
|
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.
Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 67.96 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 63 GLLSEEKAEAIMQAAQEVIDGFRYQEFPLavwqTGSGTQSNMNMNEVLANRASELlGGergnerKVHpnddvnKSQSSND 142
Cdd:cd01359 27 GILTEEEAAKILAGLAKIRAEIEAGAFEL----DPEDEDIHMAIERRLIERIGDV-GG------KLH------TGRSRND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 143 VFPTAMHVAAVVAIRQqLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHL 222
Cdd:cd01359 90 QVATDLRLYLRDALLE-LLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 223 YELALGGTA-VGTGLNTHPEYavrvakaIAQLSGCDFVTaPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWLASG 301
Cdd:cd01359 169 NVSPLGAGAlAGTTFPIDRER-------TAELLGFDGPT-ENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 302 PRcgiGEISIPEN-EPGSSIMPGKVNPTQCEAVTMLCAQVMGNDVAV-----NIGGASGNFELNVFRPL--VIHNFLQSV 373
Cdd:cd01359 241 EF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLlttlkGLPLAYNKDLQEDKEPLfdAVDTLIASL 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 2553831256 374 RLLADgiesfnehCARGIEPNRPRINQLLNESLMLVTAL 412
Cdd:cd01359 318 RLLTG--------VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-327 |
5.43e-11 |
|
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: 64.18 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 155 AIRQQLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEyglEHLYELALGGtAVGT 234
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK---QIEILGKFNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 235 gLNTH----PEYAVRVAKAiaqlsgcDFVTAPN-KFEALA----SCDGLVQAHGALKGLAASMMKIANDVrWlasgprcg 305
Cdd:cd01598 192 -FNAHlvayPDVDWRKFSE-------FFVTSLGlTWNPYTtqiePHDYIAELFDALARINTILIDLCRDI-W-------- 254
|
170 180
....*....|....*....|....*....
gi 2553831256 306 iGEISI-------PENEPGSSIMPGKVNP 327
Cdd:cd01598 255 -GYISLgyfkqkvKKGEVGSSTMPHKVNP 282
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
160-342 |
6.79e-11 |
|
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: 63.88 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 160 LLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALGGTaVGTG---- 235
Cdd:cd03302 115 ILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQasfl 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 236 --LNTHPEYAVRVAKAIAQLSGCDFV------TAPNKFEalascdglVQAHGALKGLAASMMKIANDVRWLAsgprcGIG 307
Cdd:cd03302 194 dlFEGDHDKVEALDELVTKKAGFKKVypvtgqTYSRKVD--------IDVLNALSSLGATAHKIATDIRLLA-----NLK 260
|
170 180 190
....*....|....*....|....*....|....*..
gi 2553831256 308 EISIP--ENEPGSSIMPGKVNPTQCEAVTMLCAQVMG 342
Cdd:cd03302 261 EVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
155-327 |
3.57e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 55.53 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 155 AIRQQLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEyGLEHLYElaLGGtAVGT 234
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLE-AVEILGK--ING-AVGN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 235 gLNTH----PEYAVRvakAIAQlsgcDFVTA----PNKF----EalaSCDGLVQAHGALKGLAASMMKIANDVrWlasgp 302
Cdd:PRK09285 214 -YNAHlaayPEVDWH---AFSR----EFVESlgltWNPYttqiE---PHDYIAELFDAVARFNTILIDLDRDV-W----- 276
|
170 180 190
....*....|....*....|....*....|..
gi 2553831256 303 rcgiGEIS-------IPENEPGSSIMPGKVNP 327
Cdd:PRK09285 277 ----GYISlgyfkqkTKAGEIGSSTMPHKVNP 304
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
61-336 |
1.42e-06 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 50.05 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 61 DLGLLSEEKAEAIMQAAQEvidgfryqeFPLAVWQTGSGTQSNMNMNEVLANRASELLGGERGneRKVHPNddvnksQSS 140
Cdd:PRK05975 46 EHGIIPAEAAERIAAACET---------FEPDLAALRHATARDGVVVPALVRQLRAAVGEEAA--AHVHFG------ATS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 141 NDVFPT--AMHVAAVVAIrqqLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYG 218
Cdd:PRK05975 109 QDVIDTslMLRLKAASEI---LAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 219 LEHLYELALGGtAVGTGLNTHPEyAVRVAKAIAQLSGcdFVTAPnkfEALASCDGLVQAHGALKGLAASMMKIANDVRWL 298
Cdd:PRK05975 186 RADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--LEDAP---QWHSQRDFIADFAHLLSLVTGSLGKFGQDIALM 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 2553831256 299 ASGPrcgiGEISIPENEpGSSIMPGKVNPTQCEAVTML 336
Cdd:PRK05975 259 AQAG----DEISLSGGG-GSSAMPHKQNPVAAETLVTL 291
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
63-327 |
1.94e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 50.15 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 63 GLLSEEKAEAIMQAAQEVIDGFRYQEFPLAVwqtgsgtqSNMNMNEVLANRASELLGgERGneRKVHpnddvnKSQSSND 142
Cdd:PRK00855 51 GILSEEEAEKILAGLDEILEEIEAGKFEFSP--------ELEDIHMAIEARLTERIG-DVG--GKLH------TGRSRND 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 143 vfptamHVAavVAIR-------QQLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHI 215
Cdd:PRK00855 114 ------QVA--TDLRlylrdeiDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 216 EYGLEHLYELALGGTA-VGTGLNTHPEYavrvakaIAQLSGCDFVTApNKFEALASCDGLVQAHGALKGLAASMMKIAND 294
Cdd:PRK00855 186 RDARKRVNRSPLGSAAlAGTTFPIDRER-------TAELLGFDGVTE-NSLDAVSDRDFALEFLSAASLLMVHLSRLAEE 257
|
250 260 270
....*....|....*....|....*....|....*
gi 2553831256 295 -VRWlaSGPRCGIgeISIPEN-EPGSSIMPGKVNP 327
Cdd:PRK00855 258 lILW--SSQEFGF--VELPDAfSTGSSIMPQKKNP 288
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
158-342 |
4.24e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 49.01 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 158 QQLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALG-GTAVGTGl 236
Cdd:PRK12308 126 QQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTA- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 237 nthpeYAVRvAKAIAQLSGcdFVTAP-NKFEALASCDGLVQahgALKGLAASMM---KIANDVRWLASGPRcgiGEISIP 312
Cdd:PRK12308 205 -----YPID-REALAHNLG--FRRATrNSLDSVSDRDHVME---LMSVASISMLhlsRLAEDLIFYNSGES---GFIELA 270
|
170 180 190
....*....|....*....|....*....|.
gi 2553831256 313 EN-EPGSSIMPGKVNPTQCEAVTMLCAQVMG 342
Cdd:PRK12308 271 DTvTSGSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-461 |
9.55e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 46.56 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 280 ALKGLAASMMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAVTMLCAQVMGNdVAVNIGGASGNFE 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIGSERITGLARVLRSY-LVTALENVPLWHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 358 LNVF-----RPLVIHNFlqsvrLLADGIESFNEHCARGIEPNRPRINQLLNESL-------MLVTALNTHIG-------- 417
Cdd:PRK08937 98 RDLShssaeRIALPDAF-----LALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaheli 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553831256 418 YDKAAEIAKKAHHEGLTLKESALMLGYVTAAQFDEWVRPQDMVG 461
Cdd:PRK08937 173 REKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
63-347 |
9.27e-05 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 44.72 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 63 GLLSEEKAEAIMQAAQEVIDGFRYQEFplaVWQTGsgtQSNMNMNevLANRASELLGGERGnerKVHpnddvnKSQSSND 142
Cdd:PLN02646 63 GIITDEDRDSILDGLDEIEKEIEAGKF---EWRPD---REDVHMN--NEARLTELIGEPAK---KLH------TARSRND 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 143 VFPTAMH---VAAVVAIRQQLlpqmDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHIEYGL 219
Cdd:PLN02646 126 QVATDTRlwcRDAIDVIRKRI----KTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 220 EHLYELALGGTAV-GTGLNTHPEYavrVAKAIaqlsGCDFVTaPNKFEALASCDGLVQAHGALKGLAASMMKIANDVRWL 298
Cdd:PLN02646 202 PRVNFCPLGSCALaGTGLPIDRFM---TAKDL----GFTAPM-RNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLW 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2553831256 299 ASGPRCGIgeisIPEN--EPGSSIMPGKVNPTQCEAVTMLCAQVMGNDVAV 347
Cdd:PLN02646 274 ASEEFGFV----TPSDavSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTV 320
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
190-342 |
4.24e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 42.91 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553831256 190 QDATPLTLGQEISGWVAMLVHSKKHIEYGLEHLYELALG-GTAVGTGLNTHPEYavrvakaIAQLSGcdFVT-APNKFEA 267
Cdd:PRK02186 565 QPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGaGAGGGTTFPIDPEF-------VARLLG--FEQpAPNSLDA 635
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553831256 268 LASCDGLVQAHGALKGLAASMMKIANDVR-WLASGprcgIGEISIPEN-EPGSSIMPGKVNPTQCEAVTMLCAQVMG 342
Cdd:PRK02186 636 VASRDGVLHFLSAMAAISTVLSRLAQDLQlWTTRE----FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAG 708
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
155-215 |
4.41e-04 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 42.42 E-value: 4.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553831256 155 AIRQQLLPQMDVLIQTLQGKSDQFRHIVKIGRTHLQDATPLTLGQEISGWVAMLVHSKKHI 215
Cdd:PLN02848 141 GVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQL 201
|
|
| |
