|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-464 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 951.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 1 MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 81 LAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 161 IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 241 EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 321 MPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQ 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129569 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMK 464
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| 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: 940.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 1 MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 81 LAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 161 IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 241 EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 321 MPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQ 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129569 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVG 461
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| 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: 912.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 4 VRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAG 83
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 84 QHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQ 163
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 164 LKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYA 243
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 244 RRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG 323
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 324 KVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLN 403
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129569 404 ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVG 461
Cdd:TIGR00979 401 NSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| 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: 892.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQ 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 85 HDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 165 KTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYAR 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 245 RVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 325 VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129569 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQM 459
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| 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: 818.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQ 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 85 HDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGmERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 165 KTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYAR 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 245 RVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 325 VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16129569 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVR 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: 716.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 11 MGAIDVPADKLWGAQTQRSLEHFRIS--TEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDE 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 89 FPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLT 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 169 QTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVAD 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 249 ELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 329 QCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16129569 409 VTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVG 461
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTG 453
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
5-466 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 623.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQ 84
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 85 HDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQL 164
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 165 KTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYAR 244
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 245 RVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 325 VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE 404
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129569 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAG 466
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAGGHG 464
|
|
| 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: 607.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPT--SLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLA 82
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 83 GQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKqLIP 162
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 163 QLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEY 242
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 243 ARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMP 322
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 323 GKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLL 402
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129569 403 NESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVG 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: 596.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 1 MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKM---PTsLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAA 77
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdyPE-LIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 78 DEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALR 157
Cdd:PRK12273 81 DEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 158 KqLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLN 237
Cdd:PRK12273 161 K-LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 238 THPEYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPG 317
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 318 SSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRER 397
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129569 398 INQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVG 461
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTH 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: 585.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQ 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 85 HDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKqLIPQL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 165 KTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYAR 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 245 RVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 325 VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16129569 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFD 451
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELD 446
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
4-460 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 558.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 4 VRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAG 83
Cdd:PRK13353 5 MRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 84 QHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKqLIPQ 163
Cdd:PRK13353 85 KLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG-LLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 164 LKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYA 243
Cdd:PRK13353 164 MGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 244 RRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG 323
Cdd:PRK13353 244 ERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 324 KVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLN 403
Cdd:PRK13353 324 KVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129569 404 ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMV 460
Cdd:PRK13353 404 KSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
6.54e-150 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 429.48 E-value: 6.54e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 12 GAIDVPADKLWGAQTQRSLEHFRISTEKmptslIHALALTKRAAAKVNEDLgllsEEKASAIRQAADEVLA-GQHDDEFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 91 LAIWQTGSGTQSNMNMNEVLAnrasELLGgvrgmeRKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQT 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 171 LNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLP-HVAELALGGTAVGTGLNTHPEYARRVADE 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPrLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 250 LAVITCAPfVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPrCGIGEISIPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 16129569 330 CEALTMLCCQVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-467 |
1.24e-147 |
|
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: 429.64 E-value: 1.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 5 RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPT--SLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVL- 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 82 AGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKqLI 161
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIK-LV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 162 PQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPE 241
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 242 YARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 322 PGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQL 401
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129569 402 LNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAGR 467
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAK 465
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
2-466 |
1.42e-135 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 398.99 E-value: 1.42e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 2 NTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVL 81
Cdd:PRK14515 9 NGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 82 AGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKqLI 161
Cdd:PRK14515 89 DGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG-LL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 162 PQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPE 241
Cdd:PRK14515 168 QTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 242 YARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:PRK14515 248 YIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 322 PGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQL 401
Cdd:PRK14515 328 PGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEY 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129569 402 LNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAG 466
Cdd:PRK14515 408 VEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHPGIAG 472
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-394 |
1.93e-128 |
|
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: 375.30 E-value: 1.93e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 45 IHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFplaiWQTGSGTQSNMNMNEVLANRASELLGGVrgm 124
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGGY--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 125 erkvhpnddVNKSQSSNDVFPTaMHVAALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGW 204
Cdd:cd01334 74 ---------VHTGRSSNDIVDT-ALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 205 VAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVitcapFVTAPNKFEALATCDALVQAHGALKGL 284
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 285 AASLMKIANDVRWLASGprcGIGEISIPEN-EPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRP 363
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 16129569 364 MVIHNFLQSVRLLADGMESFNKHCAvGIEPN 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 |
3.55e-61 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 199.37 E-value: 3.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 104 MNMNEVLANRASELLGGVrgmerkvHPNDDVNKSQSSNDVFPTAMHVAALLALRKqLIPQLKTLTQTLNEKSRAFADIVK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDIGTTALRLALRDALDD-LLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 184 IGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSlphvaelalggtavgtglnthpeyarrvadelavitcapfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 264 kfealatcdALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPeNEPGSSIMPGKVNPTQCEALTMLCCQVMGN 343
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 16129569 344 DVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFN 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
54-461 |
1.05e-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: 114.41 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 54 AAAKVNEDLGLLSEEKASAIRQAADevlagqhDDEF-PLAIWQTGSGTQSNM-----NMNEVLANRASELlggvrgmerk 127
Cdd:COG0015 30 ALAEAQAELGLIPAEAAAAIRAAAD-------DFEIdAERIKEIEKETRHDVkafvyALKEKVGAEAGEY---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 128 VHpnddvnKSQSSNDVFPTAMhvaaLLALR---KQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGW 204
Cdd:COG0015 93 IH------FGATSQDINDTAL----ALQLRealELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 205 VAMLEHNLKHIEYSLPHVAELALGGtAVGTgLNTH----PEYARRVADELAvITCAPFVT--APnkfealatCDALVQAH 278
Cdd:COG0015 163 AAELLRQLERLEEARERVLVGKIGG-AVGT-YAAHgeawPEVEERVAEKLG-LKPNPVTTqiEP--------RDRHAELF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 279 GALKGLAASLMKIANDVRWLAsgpRCGIGEIS--IPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAI--NM----- 349
Cdd:COG0015 232 SALALIAGSLEKIARDIRLLQ---RTEVGEVEepFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALleALaswhe 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 350 --GGASGNfELNVFRPMVIHnFLQSVRLLADGMEsfnkhcavGIEPNRERINQLLNESLMLV------TALNTH-IG--- 417
Cdd:COG0015 309 rdLSDSSV-ERNILPDAFLL-LDGALERLLKLLE--------GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGree 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16129569 418 -YDKAAEIAKKAHKEGLT----LKAAALALGYLSEAEFDSWVRPEQMVG 461
Cdd:COG0015 379 aYELVKELARGAWEEGNDlrelLAADPEIPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
140-429 |
6.72e-24 |
|
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176467 [Multi-domain] Cd Length: 381 Bit Score: 102.97 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 140 SNDVFPTAMhvaaLLALRKQL---IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIE 216
Cdd:cd01595 89 SQDINDTAL----ALQLRDALdiiLPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 217 YSLPHVAELALGGtAVGTGLNTH---PEYARRVADELAvITCAPFVTapnkfeALATCDALVQAHGALKGLAASLMKIAN 293
Cdd:cd01595 165 EARERVLVGGISG-AVGTHASLGpkgPEVEERVAEKLG-LKVPPITT------QIEPRDRIAELLSALALIAGTLEKIAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 294 DVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGNdVAINMGGASGNFElnvfRPM----VIH 367
Cdd:cd01595 237 DIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL-AAPALENLVQWHE----RDLsdssVER 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129569 368 NFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLMLV------TAL-NTHIGYDKAAEIAKKAH 429
Cdd:cd01595 309 NILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALaKKGLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
42-462 |
1.75e-20 |
|
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: 93.46 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 42 TSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADevlagqhddefplaiwqtgsgtQSNMNMNEvLANRASE----L 117
Cdd:cd01597 18 ENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAAD----------------------VERLDLEA-LAEATARtghpA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 118 LGGVRGMERKVHPNDD--VNKSQSSNDVFPTAMhvaaLLALRKQLI---PQLKTLTQTLNEKSRAFADIVKIGRTHLQDA 192
Cdd:cd01597 75 IPLVKQLTAACGDAAGeyVHWGATTQDIIDTAL----VLQLRDALDlleRDLDALLDALARLAATHRDTPMVGRTHLQHA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 193 TPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGtAVGT-------GLNTHPEYARRVadELAVITCAPFVTApnkf 265
Cdd:cd01597 151 LPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGTlaslgdqGLAVQEALAAEL--GLGVPAIPWHTAR---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 266 ealatcDALVQAHGALKGLAASLMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGn 343
Cdd:cd01597 224 ------DRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 344 DVAINMGGASGNFElnvfRP----MVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLN--------ESLMLvtA 411
Cdd:cd01597 294 LAALLLDAMVQEHE----RDagawHAEWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDltgglilsEAVMM--A 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129569 412 LNTHIGYDKA----AEIAKKAHKEGL----TLKAAALALGYLSEAEFDSWVRPEQMVGS 462
Cdd:cd01597 368 LAPKLGRQEAhdlvYEACMRAVEEGRplreVLLEDPEVAAYLSDEELDALLDPANYLGS 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
140-430 |
1.06e-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: 91.25 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 140 SNDVFPTAMhvaALLaLRKQL---IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHie 216
Cdd:TIGR00928 97 SNDIVDTAL---ALL-LRDALeiiLPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLER-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 217 ysLPHVAE-LALGGT--AVGTGLNTHPEYA---RRVADELAvITCAPFVTA--PNKFEAlATCDALVQahgalkgLAASL 288
Cdd:TIGR00928 171 --LLQAKErIKVGGIsgAVGTHAAAYPLVEeveERVTEFLG-LKPVPISTQiePRDRHA-ELLDALAL-------LATTL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 289 MKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEaltmlccQVMGNDVAIN--MGGASGN----FELNV 360
Cdd:TIGR00928 240 EKFAVDIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFE-------NVCGLARVIRgyASPALENaplwHERDL 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129569 361 FRPMVIHNFLQSVRLLADGM-ESFNKHCAvGIEPNRERINQLLNESLMLVTALNTHI-------GYDKAAEIAK-KAHK 430
Cdd:TIGR00928 310 TDSSVERVILPDAFILADIMlKTTLKVVK-KLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVReLAMG 387
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
5.82e-19 |
|
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: 80.06 E-value: 5.82e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16129569 408 LVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
140-337 |
4.64e-17 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 82.60 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 140 SNDVFPTAMhvaALLaLR---KQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIE 216
Cdd:cd01360 91 SSDVVDTAL---ALQ-LRealDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 217 YSLPHVAELALGGtAVGTGLNTHPEYARRVADEL--AVITCAPFVTAPNKFEALATcdalvqahgALKGLAASLMKIAND 294
Cdd:cd01360 167 EARERILVGKISG-AVGTYANLGPEVEERVAEKLglKPEPISTQVIQRDRHAEYLS---------TLALIASTLEKIATE 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129569 295 VRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLC 337
Cdd:cd01360 237 IRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
43-412 |
4.54e-16 |
|
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: 79.90 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 43 SLIHALALTKRaaakvnedlGLLSEEKASAIRQAADEVLAGQHDDEFPLaiwqTGSGTQSNMNmNEvlaNRASELLGGVR 122
Cdd:cd01359 16 SIAHAVMLAEQ---------GILTEEEAAKILAGLAKIRAEIEAGAFEL----DPEDEDIHMA-IE---RRLIERIGDVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 123 GmerKVHpnddvnKSQSSNDVFPTAMHvaalLALRKQ---LIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQ 199
Cdd:cd01359 79 G---KLH------TGRSRNDQVATDLR----LYLRDAlleLLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 200 EISGWVAMLEHNLKHIEYSLPHVAELALGGTA-VGTGLNTHPEyarRVADEL---AVItcapfvtaPNKFEALATCDALV 275
Cdd:cd01359 146 YLLAYAEMLERDLERLADAYKRVNVSPLGAGAlAGTTFPIDRE---RTAELLgfdGPT--------ENSLDAVSDRDFVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 276 QAHGALKGLAASLMKIANDVRWLASGPRcgiGEISIPEN-EPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAI-----NM 349
Cdd:cd01359 215 EFLSAAALLMVHLSRLAEDLILWSTQEF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLlttlkGL 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129569 350 GGASGNFELNVFRPM--VIHNFLQSVRLLADGMEsfnkhcavGIEPNRERINQLLNESLMLVTAL 412
Cdd:cd01359 292 PLAYNKDLQEDKEPLfdAVDTLIASLRLLTGVIS--------TLTVNPERMREAAEAGFSTATDL 348
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
29-349 |
1.64e-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: 78.55 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 29 SLEH-FRISTEKMPTSLIHALALTKraaakvnedLGLLSEEKASAIRQAADEVLAGQHDDEFPLaiwqtgSGTQSNMNMN 107
Cdd:TIGR00838 20 SLSFdKELAEYDIEGSIAHTKMLKK---------AGILTEEEAAKIIEGLNELKEEGREGPFIL------DPDDEDIHMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 108 evLANRASELLGgvRGMERKVHpnddvnKSQSSNDVFPTAMHvaalLALRKQ---LIPQLKTLTQTLNEKSRAFADIVKI 184
Cdd:TIGR00838 85 --IERELIDRVG--EDLGGKLH------TGRSRNDQVATDLR----LYLRDHvleLAEALLDLQDALIELAEKHVETLMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 185 GRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAV-GTGLNTHPEYARRVADELAVITcapfvtapN 263
Cdd:TIGR00838 151 GYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALaGTGFPIDREYLAELLGFDAVTE--------N 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 264 KFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPrcgIGEISIP-ENEPGSSIMPGKVNPTQCEALTMLCCQVMG 342
Cdd:TIGR00838 223 SLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQG 299
|
....*..
gi 16129569 343 NDVAINM 349
Cdd:TIGR00838 300 NLTGMLM 306
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
147-333 |
1.15e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 69.66 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 147 AMHVAALLALRK---QLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVA 223
Cdd:PRK09053 111 IIDTGLVLQLRDaldLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 224 ELALGGtAVGT--GLNTH-PEYARRVADELAV-ITCAPFVTAPnkfealatcDALVQAHGALKGLAASLMKIANDVRWLA 299
Cdd:PRK09053 191 VLQFGG-AAGTlaSLGEQaLPVAQALAAELQLaLPALPWHTQR---------DRIAEFASALGLLAGTLGKIARDVSLLM 260
|
170 180 190
....*....|....*....|....*....|....*.
gi 16129569 300 sgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAL 333
Cdd:PRK09053 261 ---QTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAV 293
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-327 |
3.81e-12 |
|
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: 68.03 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 155 ALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEySLPHVAelALGGtAVGT 234
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK-QIEILG--KFNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 235 gLNTH---------PEYARRVADELAvITCAPFVT--APNKFEAlATCDALVQAHGALKGLaaslmkiANDVrWlasgpr 303
Cdd:cd01598 192 -FNAHlvaypdvdwRKFSEFFVTSLG-LTWNPYTTqiEPHDYIA-ELFDALARINTILIDL-------CRDI-W------ 254
|
170 180 190
....*....|....*....|....*....|.
gi 16129569 304 cgiGEISI-------PENEPGSSIMPGKVNP 327
Cdd:cd01598 255 ---GYISLgyfkqkvKKGEVGSSTMPHKVNP 282
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
43-327 |
4.52e-12 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 67.87 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 43 SLIHALALTKRaaakvnedlGLLSEEKASAIRQAADEVLAGQHDDEFPLAIwqtgsgtqSNMNMNEVLANRASELLGGVR 122
Cdd:PRK00855 40 SIAHARMLAKQ---------GILSEEEAEKILAGLDEILEEIEAGKFEFSP--------ELEDIHMAIEARLTERIGDVG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 123 GmerKVHpnddvnKSQSSNDvfptamHVAAL--LALRKQL---IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTL 197
Cdd:PRK00855 103 G---KLH------TGRSRND------QVATDlrLYLRDEIdeiAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 198 GQEISGWVAMLEHNLKHIEYSLPHVAELALGGTA-VGTGLNTHPEYarrVADELAvitcapF--VTApNKFEALATCDAL 274
Cdd:PRK00855 168 GHHLLAYAEMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIDRER---TAELLG------FdgVTE-NSLDAVSDRDFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16129569 275 VQAHGALKGLAASLMKIAND-VRWlaSGPRCGIgeISIPEN-EPGSSIMPGKVNP 327
Cdd:PRK00855 238 LEFLSAASLLMVHLSRLAEElILW--SSQEFGF--VELPDAfSTGSSIMPQKKNP 288
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
10-333 |
5.28e-12 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 67.44 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 10 SMGAIDVPAD---KLWGAQTQRS----LEHF--------RISTEKMPTSLIHALALTKRaaakvnedlGLLSEEKASAIR 74
Cdd:PLN02646 4 SMSASEEEAAkekKLWGGRFEEGvtpaVEKFnesisfdkRLYKEDIMGSKAHASMLAKQ---------GIITDEDRDSIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 75 QAADEVLAGQHDDEFplaIWQTGsgtQSNMNMNevLANRASELLGGVRGmerKVHpnddvnKSQSSNDVFPTAMH---VA 151
Cdd:PLN02646 75 DGLDEIEKEIEAGKF---EWRPD---REDVHMN--NEARLTELIGEPAK---KLH------TARSRNDQVATDTRlwcRD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 152 ALLALRKQLipqlKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTA 231
Cdd:PLN02646 138 AIDVIRKRI----KTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 232 V-GTGLnthPEYARRVADELAVitcapfvTAP--NKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIge 308
Cdd:PLN02646 214 LaGTGL---PIDRFMTAKDLGF-------TAPmrNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFV-- 281
|
330 340
....*....|....*....|....*..
gi 16129569 309 isIPEN--EPGSSIMPGKVNPTQCEAL 333
Cdd:PLN02646 282 --TPSDavSTGSSIMPQKKNPDPMELV 306
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
151-342 |
3.19e-10 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 61.95 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 151 AALLALRKQL---IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELAL 227
Cdd:cd03302 103 TDLIQIRDALdliLPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 228 GGTaVGTG----------------LNthpeyaRRVADELAVITCAPFV--TAPNKFEALATCdalvqahgALKGLAASLM 289
Cdd:cd03302 183 KGT-TGTQasfldlfegdhdkveaLD------ELVTKKAGFKKVYPVTgqTYSRKVDIDVLN--------ALSSLGATAH 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129569 290 KIANDVRWLAsgprcGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMG 342
Cdd:cd03302 248 KIATDIRLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
155-327 |
3.57e-10 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 61.69 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 155 ALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEyslpHVAELA-LGGtAVG 233
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLE----AVEILGkING-AVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 234 TgLNTH---------PEYARRVADELAVitcapfvtapnKFEALAT----CDALVQAHGALKGLAASLMKIANDVrWlas 300
Cdd:PRK09285 213 N-YNAHlaaypevdwHAFSREFVESLGL-----------TWNPYTTqiepHDYIAELFDAVARFNTILIDLDRDV-W--- 276
|
170 180 190
....*....|....*....|....*....|....
gi 16129569 301 gprcgiGEIS-------IPENEPGSSIMPGKVNP 327
Cdd:PRK09285 277 ------GYISlgyfkqkTKAGEIGSSTMPHKVNP 304
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
121-336 |
1.94e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 58.91 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 121 VRGMERKVHPN--DDVNKSQSSNDVFPTAMhVAALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLG 198
Cdd:PRK05975 87 VRQLRAAVGEEaaAHVHFGATSQDVIDTSL-MLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 199 QEISGWVAMLEHNLKHIEYSLPHVAELALGGtAVGTGLNTHPEYAR---RVADELAVITCApfvtapnkfEALATCDALV 275
Cdd:PRK05975 166 DRLASWRAPLLRHRDRLEALRADVFPLQFGG-AAGTLEKLGGKAAAvraRLAKRLGLEDAP---------QWHSQRDFIA 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129569 276 QAHGALKGLAASLMKIANDVRWLASGPrcgiGEISIPENEpGSSIMPGKVNPTQCEALTML 336
Cdd:PRK05975 236 DFAHLLSLVTGSLGKFGQDIALMAQAG----DEISLSGGG-GSSAMPHKQNPVAAETLVTL 291
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-461 |
3.12e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 48.10 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 280 ALKGLAASLMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGNdVAINMGGASGNFE 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIGSERITGLARVLRSY-LVTALENVPLWHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 358 LNVF-----RPMVIHNFlqsvrLLADGMESFNKHCAVGIEPNRERINQLLNESL-------MLVTALNTHIG----YDKA 421
Cdd:PRK08937 98 RDLShssaeRIALPDAF-----LALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaHELI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16129569 422 AEIAKKAHKEGLTLKAAALA----LGYLSEAEFDSWVRPEQMVG 461
Cdd:PRK08937 173 REKAMEAWKNQKDLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
54-349 |
1.41e-05 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 47.47 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 54 AAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDefPLAIWQTGSgtqsnmnmNEVLANRASELLGGVRGMERKVHpndd 133
Cdd:PRK12308 39 AWSKALLSVGVLSEEEQQKLELALNELKLEVMED--PEQILLSDA--------EDIHSWVEQQLIGKVGDLGKKLH---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 134 vnKSQSSNDvfptamHVAALLAL--RKQ---LIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAML 208
Cdd:PRK12308 105 --TGRSRND------QVATDLKLwcRQQgqqLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 209 EHNLKHIEYSLPHVAELALG-GTAVGTGlntHPEYARRVADELAvitcapFVTAP-NKFEALATCDALVQAHGALKGLAA 286
Cdd:PRK12308 177 ERDYSRLEDALTRLDTCPLGsGALAGTA---YPIDREALAHNLG------FRRATrNSLDSVSDRDHVMELMSVASISML 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129569 287 SLMKIANDVRWLASGPRcgiGEISIPEN-EPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINM 349
Cdd:PRK12308 248 HLSRLAEDLIFYNSGES---GFIELADTvTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMM 308
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
61-327 |
3.68e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 46.38 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 61 DLGLLSEEKASAIRQAadevLAGQHDDEF-PLAIWQTGSGTQsnMNMNEVLANRASELLGGVrgmerkvhpnddVNKSQS 139
Cdd:PRK02186 454 DTGIVAPERARPLLDA----HRRLRDAGFaPLLARPAPRGLY--MLYEAYLIERLGEDVGGV------------LQTARS 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 140 SNDVFPTAmhvaALLALRKQL---IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIE 216
Cdd:PRK02186 516 RNDINATT----TKLHLREATsraFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALF 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 217 YSLPHVAELALG-GTAVGTGLNTHPEyarRVADELAVITcapfvTAPNKFEALATCDALVQAHGALKGLAASLMKIANDV 295
Cdd:PRK02186 592 ALFEHIDVCPLGaGAGGGTTFPIDPE---FVARLLGFEQ-----PAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDL 663
|
250 260 270
....*....|....*....|....*....|....
gi 16129569 296 R-WLASGprcgIGEISIPEN-EPGSSIMPGKVNP 327
Cdd:PRK02186 664 QlWTTRE----FALVSLPDAlTGGSSMLPQKKNP 693
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
185-349 |
4.14e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 42.57 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 185 GRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGgtaVGTGLNTHPEYARRVADELavITCAPFVTAPnK 264
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYG---YGSGYGSPSSVKFNQMSEL--LGMEKNIKNP-V 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129569 265 FEALATCDALVQAHGALKGLAASLMKIANDvrwLASGPRCGIGEISiPENEPGSSIMPGKVNPTQCEALTMLCCQVMGND 344
Cdd:PRK06389 221 YSSSLYIKTIENISYLISSLAVDLSRICQD---IIIYYENGIITIP-DEFTTGSSLMPNKRNPDYLELFQGIAAESISVL 296
|
....*
gi 16129569 345 VAINM 349
Cdd:PRK06389 297 SFIAQ 301
|
|
| |
