|
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: 969.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 1 MTTHRSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 81 LAGNHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREAL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 161 IPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHP 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 241 QYAVRVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 321 MPGKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQ 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695764396 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVGSMA 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: 956.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 1 MTTHRSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 81 LAGNHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREAL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 161 IPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHP 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 241 QYAVRVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 321 MPGKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQ 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695764396 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVG 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: 900.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 4 HRSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAG 83
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 84 NHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREALIPR 163
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 164 LRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYA 243
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 244 VRVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPG 323
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 324 KVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLN 403
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 695764396 404 ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVG 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: 898.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGN 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREALIPRL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 165 RVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAV 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 245 RVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 325 VNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 695764396 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEM 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: 824.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGN 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGmERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREALIPRL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 165 RVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAV 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 245 RVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 325 VNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 695764396 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVR 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: 733.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 11 MGAIEVPADKLWGAQTQRSLEHFRIS--TEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGNHPDE 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 89 FPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREALIPRLRVLK 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 169 QTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAVRVAE 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 249 ELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 329 QCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 695764396 409 VTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVG 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: 626.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGN 84
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREALIPRL 164
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 165 RVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAV 244
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 245 RVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 325 VNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNE 404
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 695764396 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVGS 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: 620.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPG--ELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLA 82
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 83 GNHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREaLIP 162
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 163 RLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQY 242
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 243 AVRVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMP 322
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 323 GKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLL 402
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 695764396 403 NESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVG 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: 604.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 1 MTTHRSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKM--PGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAAD 78
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 79 EVLAGNHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALRE 158
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 159 aLIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNT 238
Cdd:PRK12273 162 -LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 239 HPQYAVRVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGS 318
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 319 SIMPGKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERI 398
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695764396 399 AQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMVG 461
Cdd:PRK12273 401 REYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTH 463
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-451 |
0e+00 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 589.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGN 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREaLIPRL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 165 RVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAV 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 245 RVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 325 VNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 695764396 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFD 451
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELD 446
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
5-460 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 558.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGN 84
Cdd:PRK13353 6 RIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILAGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALrEALIPRL 164
Cdd:PRK13353 86 LHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL-EGLLAAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 165 RVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAV 244
Cdd:PRK13353 165 GALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYIE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 245 RVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:PRK13353 245 RVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPGK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 325 VNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNE 404
Cdd:PRK13353 325 VNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVEK 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 695764396 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMV 460
Cdd:PRK13353 405 SVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-460 |
5.31e-149 |
|
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: 433.10 E-value: 5.31e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPG--ELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVL- 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 82 AGNHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAaIIALREALI 161
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIA-VYSSLIKLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 162 PRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQ 241
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 242 YAVRVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIM 321
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 322 PGKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQL 401
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 695764396 402 LNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEMV 460
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLM 458
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
1.27e-142 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 410.61 E-value: 1.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 12 GAIEVPADKLWGAQTQRSLEHFRISTEKmpgelIYALALTKRAAAKVNQDlgllTAEKAEAIIQAADEVLA-GNHPDEFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVI----LKEEAAAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 91 LAIWQTGSGTQSNMNMNEVLAnrasELLGgvrgmeRKVHPNDDVNKSQSSNDVFPTAMHVAAIIALREALIPRLRVLKQT 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 171 LSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHL-ELSLPHLSELALGGTAVGTGLNTHPQYAVRVAEE 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLqQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 250 LAALSGQPfVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPrCGIGEIAIPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 695764396 330 CEALTMLCCQVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
5-459 |
4.75e-139 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 407.85 E-value: 4.75e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 5 RSERDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGN 84
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAIIALrEALIPRL 164
Cdd:PRK14515 92 WHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNAL-EGLLQTM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 165 RVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAV 244
Cdd:PRK14515 171 GYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 245 RVAEELAALSGQPFVTAPNKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGK 324
Cdd:PRK14515 251 AVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 325 VNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFNEHCATGIEPNRERIAQLLNE 404
Cdd:PRK14515 331 VNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEK 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 695764396 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEM 459
Cdd:PRK14515 411 SVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEM 465
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-394 |
1.46e-123 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 362.59 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 45 IYALALTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGNHPDEFplaiWQTGSGTQSNMNMNEVLANRASELLGGVrgm 124
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGGY--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 125 erkvhpnddVNKSQSSNDVFPTaMHVAAIIALREALIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGW 204
Cdd:cd01334 74 ---------VHTGRSSNDIVDT-ALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 205 VAMLEHNLRHLELSLPHLSELALGGTAVGTGLNTHPQYAVRVAEELAAlsgqpFVTAPNKFEALATCDALVHAHGALKGL 284
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 285 AASLMKIANDVRWLASGprcGIGEIAIPEN-EPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNFELNVYRP 363
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 695764396 364 MVIHNFLQSVRLLADGMESFNEHCAtGIEPN 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 |
1.51e-58 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 192.44 E-value: 1.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 104 MNMNEVLANRASELLGGVrgmerkvHPNDDVNKSQSSNDVFPTAMHVAAIIALREaLIPRLRVLKQTLSDKATAFNDIVK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDIGTTALRLALRDALDD-LLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 184 IGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLElslphlselalggtavgtglnthpqyAVRVAEelaalsgqpfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLE--------------------------EAAVAE--------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 264 kfealatcdalvhAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPeNEPGSSIMPGKVNPTQCEALTMLCCQVMGN 343
Cdd:cd01594 125 -------------ALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 695764396 344 DVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMESFN 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
140-461 |
2.39e-28 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 116.34 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 140 SNDVFPTAMhvaaIIALREA---LIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLE 216
Cdd:COG0015 99 SQDINDTAL----ALQLREAlelLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 217 LSLPHLSELALGGtAVGTgLNTHPQYAVRVAEELAA---LSGQPFVT--APNKFEAlatcdALVHahgALKGLAASLMKI 291
Cdd:COG0015 175 EARERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEklgLKPNPVTTqiEPRDRHA-----ELFS---ALALIAGSLEKI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 292 ANDVRWLAsgpRCGIGEIA--IPENEPGSSIMPGKVNPTQCEaltmlccqvmgndvavNIGGASGnfelnVYRPMVIH-- 367
Cdd:COG0015 245 ARDIRLLQ---RTEVGEVEepFAKGQVGSSAMPHKRNPIDSE----------------NIEGLAR-----LARALAAAll 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 368 ------------------NFLQSVRLLADGM-ESFNEhCATGIEPNRERIAQLLNESLMLV------TALNTH-IG---- 417
Cdd:COG0015 301 ealaswherdlsdssverNILPDAFLLLDGAlERLLK-LLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreea 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 695764396 418 YDKAAEIAKKAHKEGLTLKASALA----LGYLTEAEFDSWVRPEEMVG 461
Cdd:COG0015 380 YELVKELARGAWEEGNDLRELLAAdpeiPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
140-429 |
1.41e-26 |
|
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: 110.67 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 140 SNDVFPTAMhvaaIIALREAL---IPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLE 216
Cdd:cd01595 89 SQDINDTAL----ALQLRDALdiiLPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 217 LSLPHLSELALGGtAVGTGLNTHPQyAVRVAEELAALSGQPFVTAPNKFEAlatCDALVHAHGALKGLAASLMKIANDVR 296
Cdd:cd01595 165 EARERVLVGGISG-AVGTHASLGPK-GPEVEERVAEKLGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 297 WLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGndvavNIGGASGNFELNVYRPM----VIHNFL 370
Cdd:cd01595 240 LLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRA-----LAAPALENLVQWHERDLsdssVERNIL 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695764396 371 QSVRLLADGMESFNEHCATGIEPNRERIAQLLNESLMLV------TAL-NTHIGYDKAAEIAKKAH 429
Cdd:cd01595 312 PDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALaKKGLGRQEAYELVKEEN 377
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
2.71e-25 |
|
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: 97.78 E-value: 2.71e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 695764396 408 LVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDSWVRPEEM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
156-462 |
1.24e-21 |
|
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.
Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 96.93 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 156 LREALI---PRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGGtAV 232
Cdd:cd01597 111 LRDALDlleRDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 233 GT--GLNTHpqyAVRVAEELAALSGQPFVTAPnkfeALATCDALVHAHGALKGLAASLMKIANDVRWLAsgpRCGIGEIA 310
Cdd:cd01597 190 GTlaSLGDQ---GLAVQEALAAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 311 IP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGnDVAVNIGGASGNFElnvyRP----MVIHNFLQSVRLLADGMESFN 384
Cdd:cd01597 260 EPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLDAMVQEHE----RDagawHAEWIALPEIFLLASGALEQA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 385 EHCATGIEPNRERIAQLLN--------ESLMLvtALNTHIGYDKA----AEIAKKAHKEGLTLKASALA----LGYLTEA 448
Cdd:cd01597 335 EFLLSGLEVNEDRMRANLDltgglilsEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpevAAYLSDE 412
|
330
....*....|....
gi 695764396 449 EFDSWVRPEEMVGS 462
Cdd:cd01597 413 ELDALLDPANYLGS 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
140-466 |
2.39e-20 |
|
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: 93.18 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 140 SNDVFPTAMHvaaiIALREAL---IPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLE 216
Cdd:TIGR00928 97 SNDIVDTALA----LLLRDALeiiLPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 217 lSLPHLseLALGGT--AVGTGLNTHPQYAV---RVAEELAaLSGQPFVTA--PNKFEAlATCDALVHahgalkgLAASLM 289
Cdd:TIGR00928 173 -QAKER--IKVGGIsgAVGTHAAAYPLVEEveeRVTEFLG-LKPVPISTQiePRDRHA-ELLDALAL-------LATTLE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 290 KIANDVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAVNIGGASGNfELNVYRPMVIH 367
Cdd:TIGR00928 241 KFAVDIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWH-ERDLTDSSVER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 368 NFLQSVRLLADGM-ESFNEhCATGIEPNRERIAQLLNESLMLVTALNTHI-------GYDKAAEIAKK-----AHKEGLT 434
Cdd:TIGR00928 317 VILPDAFILADIMlKTTLK-VVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRElamgaAEVDEPD 395
|
330 340 350
....*....|....*....|....*....|....*.
gi 695764396 435 LKASALALG----YLTEAEFDSWVRPEEMVGSMATR 466
Cdd:TIGR00928 396 LLEFLLEDEritkYLKEEELAELLDPETYIGNAGEI 431
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
140-337 |
8.12e-18 |
|
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: 84.91 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 140 SNDVFPTAMHVAaiiaLREA---LIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLE 216
Cdd:cd01360 91 SSDVVDTALALQ----LREAldiILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 217 LSLPHLSELALGGtAVGTGLNTHPQYAVRVAEEL----AALSGQpfVTAPNKFEALATcdalvhahgALKGLAASLMKIA 292
Cdd:cd01360 167 EARERILVGKISG-AVGTYANLGPEVEERVAEKLglkpEPISTQ--VIQRDRHAEYLS---------TLALIASTLEKIA 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695764396 293 NDVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMLC 337
Cdd:cd01360 235 TEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
53-460 |
2.09e-17 |
|
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: 84.14 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 53 RAAAKVNQDLGLLTAEKAEAIIQAADEVLAGNHPDEFPLaiwqTGSGTQSNMNmNEvlaNRASELLGGVRGmerKVHpnd 132
Cdd:cd01359 17 IAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFEL----DPEDEDIHMA-IE---RRLIERIGDVGG---KLH--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 133 dvnKSQSSNDVFPTAMHVAAIIALREaLIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNL 212
Cdd:cd01359 83 ---TGRSRNDQVATDLRLYLRDALLE-LLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 213 RHLELSLPHLSELALGGTA-VGTGLNTHPQyavRVAEEL--AALSgqpfvtaPNKFEALATCDALVHAHGALKGLAASLM 289
Cdd:cd01359 159 ERLADAYKRVNVSPLGAGAlAGTTFPIDRE---RTAELLgfDGPT-------ENSLDAVSDRDFVLEFLSAAALLMVHLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 290 KIANDVRWLASGPRcgiGEIAIPEN-EPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAV-----NIGGASGNFELNVYRP 363
Cdd:cd01359 229 RLAEDLILWSTQEF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLlttlkGLPLAYNKDLQEDKEP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 364 M--VIHNFLQSVRLLADGMEsfnehcatGIEPNRERIAQLLNESLMLVTAL------NTHI----GYDKAAEIAKKAHKE 431
Cdd:cd01359 306 LfdAVDTLIASLRLLTGVIS--------TLTVNPERMREAAEAGFSTATDLadylvrEKGVpfreAHHIVGRAVRLAEEK 377
|
410 420 430
....*....|....*....|....*....|...
gi 695764396 432 GLTLKASALA----LGYLTEAEFDSWVRPEEMV 460
Cdd:cd01359 378 GKDLSDLTLAelqaISPLFEEDVREALDPENSV 410
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
53-343 |
2.24e-16 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 81.25 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 53 RAAAKVNQDLGLLTAEKAEAIIQAADEVLAGNHPDEFPLaiwqtgSGTQSNMNMNevLANRASELLGgvRGMERKVHpnd 132
Cdd:TIGR00838 36 IAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFIL------DPDDEDIHMA--IERELIDRVG--EDLGGKLH--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 133 dvnKSQSSNDVFPTAMHvaaiIALREA---LIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLE 209
Cdd:TIGR00838 103 ---TGRSRNDQVATDLR----LYLRDHvleLAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 210 HNLRHLELSLPHLSELALGGTAV-GTGLNTHPQYavrvaeeLAALSGQPFVTApNKFEALATCDALVHAHGALKGLAASL 288
Cdd:TIGR00838 176 RDYERLQDALKRVNVSPLGSGALaGTGFPIDREY-------LAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHL 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 695764396 289 MKIANDVRWLASGPrcgIGEIAIP-ENEPGSSIMPGKVNPTQCEALTMLCCQVMGN 343
Cdd:TIGR00838 248 SRFAEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
147-461 |
3.07e-15 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 77.75 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 147 AMHVAAIIALREA---LIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLS 223
Cdd:PRK09053 111 IIDTGLVLQLRDAldlLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 224 ELALGGtAVGT--GLNTH-PQYAVRVAEELA-ALSGQPFVTAPnkfealatcDALVHAHGALKGLAASLMKIANDVRWLA 299
Cdd:PRK09053 191 VLQFGG-AAGTlaSLGEQaLPVAQALAAELQlALPALPWHTQR---------DRIAEFASALGLLAGTLGKIARDVSLLM 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 300 sgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEAL------------TMLCCQVMGNDVAVniGGASGNFELnvyrpmv 365
Cdd:PRK09053 261 ---QTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERAL--GGWHAEWDT------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 366 ihnfLQSVRLLADGMESFNEHCATGIEPNRERIAQ--------LLNESLMLvtALNTHIGYDKAAEI----AKKAHKEGL 433
Cdd:PRK09053 329 ----LPELACLAAGALAQMAQIVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEGR 402
|
330 340 350
....*....|....*....|....*....|..
gi 695764396 434 TLK----ASALALGYLTEAEFDSWVRPEEMVG 461
Cdd:PRK09053 403 HLRdvlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
151-342 |
2.87e-13 |
|
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: 71.19 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 151 AAIIALREAL---IPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELAL 227
Cdd:cd03302 103 TDLIQIRDALdliLPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 228 GGTaVGTG-----LNTHPQYAVRVAEELAA----------LSGQpfvTAPNKFEALATCdalvhahgALKGLAASLMKIA 292
Cdd:cd03302 183 KGT-TGTQasfldLFEGDHDKVEALDELVTkkagfkkvypVTGQ---TYSRKVDIDVLN--------ALSSLGATAHKIA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695764396 293 NDVRWLAsgprcGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMG 342
Cdd:cd03302 251 TDIRLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
1-347 |
3.36e-13 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 71.29 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 1 MTTHRSERDSMGAIEVpadKLWGAQTQRS----LEHF--------RISTEKMPGELIYALALTKRaaakvnqdlGLLTAE 68
Cdd:PLN02646 1 ASTSMSASEEEAAKEK---KLWGGRFEEGvtpaVEKFnesisfdkRLYKEDIMGSKAHASMLAKQ---------GIITDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 69 KAEAIIQAADEVLAGNHPDEFplaIWQTGsgtQSNMNMNevLANRASELLGGVRGmerKVHpnddvnKSQSSNDVFPTAM 148
Cdd:PLN02646 69 DRDSILDGLDEIEKEIEAGKF---EWRPD---REDVHMN--NEARLTELIGEPAK---KLH------TARSRNDQVATDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 149 HVAAIIALREaLIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALG 228
Cdd:PLN02646 132 RLWCRDAIDV-IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 229 GTAV-GTGLNTHPQYavrVAEELAalsgqpfVTAP--NKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRCG 305
Cdd:PLN02646 211 SCALaGTGLPIDRFM---TAKDLG-------FTAPmrNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGF 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 695764396 306 IgeiaIPEN--EPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAV 347
Cdd:PLN02646 281 V----TPSDavSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTV 320
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-327 |
2.54e-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: 68.42 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 155 ALREALIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLElSLPHLseLALGGtAVGT 234
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK-QIEIL--GKFNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 235 gLNTH---------PQYAVRVAEELaALSGQPFVT--APNKFEAlATCDALVHAHGALKGLAA------SLMKIANDVRw 297
Cdd:cd01598 192 -FNAHlvaypdvdwRKFSEFFVTSL-GLTWNPYTTqiEPHDYIA-ELFDALARINTILIDLCRdiwgyiSLGYFKQKVK- 267
|
170 180 190
....*....|....*....|....*....|
gi 695764396 298 lasgprcgigeiaipENEPGSSIMPGKVNP 327
Cdd:cd01598 268 ---------------KGEVGSSTMPHKVNP 282
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
63-327 |
6.72e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 64.02 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 63 GLLTAEKAEAIIQAADEVLAGNHPDEFPLAIwqtgsgtqSNMNMNEVLANRASELLGGVRGmerKVHpnddvnKSQSSND 142
Cdd:PRK00855 51 GILSEEEAEKILAGLDEILEEIEAGKFEFSP--------ELEDIHMAIEARLTERIGDVGG---KLH------TGRSRND 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 143 vfptamHVAAII--ALREAL---IPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLEL 217
Cdd:PRK00855 114 ------QVATDLrlYLRDEIdeiAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 218 SLPHLSELALGGTA-VGTGLNTHPQYavrVAEEL----------AALSGQPFVtapnkFEALAtcdalvhahgALKGLAA 286
Cdd:PRK00855 188 ARKRVNRSPLGSAAlAGTTFPIDRER---TAELLgfdgvtenslDAVSDRDFA-----LEFLS----------AASLLMV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 695764396 287 SLMKIAND-VRWlaSGPRCGIgeIAIPEN-EPGSSIMPGKVNP 327
Cdd:PRK00855 250 HLSRLAEElILW--SSQEFGF--VELPDAfSTGSSIMPQKKNP 288
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
121-336 |
2.06e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 58.91 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 121 VRGMERKVHPN--DDVNKSQSSNDVFPTAMhVAAIIALREALIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLG 198
Cdd:PRK05975 87 VRQLRAAVGEEaaAHVHFGATSQDVIDTSL-MLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 199 QEFSGWVAMLEHNLRHLELSLPHLSELALGGtAVGTGLNTHPQyAVRVAEELAALSGqpFVTAPnkfEALATCDALVHAH 278
Cdd:PRK05975 166 DRLASWRAPLLRHRDRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--LEDAP---QWHSQRDFIADFA 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695764396 279 GALKGLAASLMKIANDVRWLASGPrcgiGEIAIPENEpGSSIMPGKVNPTQCEALTML 336
Cdd:PRK05975 239 HLLSLVTGSLGKFGQDIALMAQAG----DEISLSGGG-GSSAMPHKQNPVAAETLVTL 291
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
155-327 |
3.76e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 55.53 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 155 ALREALIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLElSLPHLSElaLGGtAVGT 234
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLE-AVEILGK--ING-AVGN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 235 gLNTH----PQYA-VRVAEElaalsgqpFVTAPN-KFEALAT----CDALVHAHGALKGLAASLMKIANDVrWlasgprc 304
Cdd:PRK09285 214 -YNAHlaayPEVDwHAFSRE--------FVESLGlTWNPYTTqiepHDYIAELFDAVARFNTILIDLDRDV-W------- 276
|
170 180 190
....*....|....*....|....*....|
gi 695764396 305 giGEIA-------IPENEPGSSIMPGKVNP 327
Cdd:PRK09285 277 --GYISlgyfkqkTKAGEIGSSTMPHKVNP 304
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-461 |
3.19e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 50.80 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 280 ALKGLAASLMKIANDVRWLAsgpRCGIGEIAIP--ENEPGSSIMPGKVNPTQCEALTMLCCQVMGNdVAVNIGGASGNFE 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIGSERITGLARVLRSY-LVTALENVPLWHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 358 LNVY-----RPMVIHNFlqsvrLLADGMESFNEHCATGIEPNRERIAQLLNESL-------MLVTALNTHIG----YDKA 421
Cdd:PRK08937 98 RDLShssaeRIALPDAF-----LALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaHELI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695764396 422 AEIAKKAHKEGLTLKASALA----LGYLTEAEFDSWVRPEEMVG 461
Cdd:PRK08937 173 REKAMEAWKNQKDLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
110-327 |
1.77e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 50.62 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 110 LANRASELLGGVrgmerkvhpnddVNKSQSSNDVFPTAmhvaAIIALREAL---IPRLRVLKQTLSDKATAFNDIVKIGR 186
Cdd:PRK02186 498 LIERLGEDVGGV------------LQTARSRNDINATT----TKLHLREATsraFDALWRLRRALVFKASANVDCALPIY 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 187 THLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALG-GTAVGTGLNTHPqyavrvaEELAALSG--QPFvtaPN 263
Cdd:PRK02186 562 SQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGaGAGGGTTFPIDP-------EFVARLLGfeQPA---PN 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695764396 264 KFEALATCDALVHAHGALKGLAASLMKIANDVR-WLASgprcGIGEIAIPEN-EPGSSIMPGKVNP 327
Cdd:PRK02186 632 SLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQlWTTR----EFALVSLPDAlTGGSSMLPQKKNP 693
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
21-342 |
1.08e-05 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 47.86 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 21 LWGAQ-TQRSLEHFRISTEKMPGEliYALA----LTKRAAAKVNQDLGLLTAEKAEAIIQAADEVLAGNHPDefPLAIWQ 95
Cdd:PRK12308 3 LWGGRfSQAADTRFKQFNDSLRFD--YRLAeqdiVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMED--PEQILL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 96 TGSgtqsnmnmNEVLANRASELLGGVRGMERKVHpnddvnKSQSSNDvfptamHVAAIIAL-----REALIPRLRVLKQT 170
Cdd:PRK12308 79 SDA--------EDIHSWVEQQLIGKVGDLGKKLH------TGRSRND------QVATDLKLwcrqqGQQLLLALDQLQQQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 171 LSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALG-GTAVGTGlnthpqYAVRvAEE 249
Cdd:PRK12308 139 MVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTA------YPID-REA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 250 LAALSGqpFVTAP-NKFEALATCDALVHAHGALKGLAASLMKIANDVRWLASGPRcgiGEIAIPEN-EPGSSIMPGKVNP 327
Cdd:PRK12308 212 LAHNLG--FRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSGES---GFIELADTvTSGSSLMPQKKNP 286
|
330
....*....|....*
gi 695764396 328 TQCEALTMLCCQVMG 342
Cdd:PRK12308 287 DALELIRGKTGRVYG 301
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
185-362 |
2.11e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 43.73 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 185 GRTHLQDATPLTLGQEFSGWVAMLEHNLRHLELSLPHLSELALGgtaVGTGLNTHPQYAVRVAEELaaLSGQPFVTAPnK 264
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYG---YGSGYGSPSSVKFNQMSEL--LGMEKNIKNP-V 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 265 FEALATCDALVHAHGALKGLAASLMKIANDvrwLASGPRCGIGEIAiPENEPGSSIMPGKVNPTQCEALTMLCCQVMGnd 344
Cdd:PRK06389 221 YSSSLYIKTIENISYLISSLAVDLSRICQD---IIIYYENGIITIP-DEFTTGSSLMPNKRNPDYLELFQGIAAESIS-- 294
|
170
....*....|....*...
gi 695764396 345 VAVNIGGASGNFELNVYR 362
Cdd:PRK06389 295 VLSFIAQSELNKTTGYHR 312
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
159-342 |
2.86e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 43.05 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 159 ALIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTlgqeFSGW----VAMLEHNLRHLELSLPHL--SEL---ALGG 229
Cdd:PRK04833 127 ELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVT----FAHWclayVEMLARDESRLQDALKRLdvSPLgsgALAG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 230 TAvgtglnthpqYAV-RvaEELAALSGqpFVTAP-NKFEALATCDALVHahgALKGLAASLM---KIANDVRWLASGpRC 304
Cdd:PRK04833 203 TA----------YEIdR--EQLAGWLG--FASATrNSLDSVSDRDHVLE---LLSDASISMVhlsRFAEDLIFFNSG-EA 264
|
170 180 190
....*....|....*....|....*....|....*...
gi 695764396 305 GIGEIAiPENEPGSSIMPGKVNPTQCEALTMLCCQVMG 342
Cdd:PRK04833 265 GFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQG 301
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
154-331 |
7.43e-04 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 41.65 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 154 IALREA----LIPRLRVLKQTLSDKATAFNDIVKIGRTHLQDATPLTLGQEFSGWVAMLEHNLRHLElSLPHLSELAlgg 229
Cdd:PLN02848 136 LMLKEGvnsvVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLS-EVKIKGKFA--- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764396 230 TAVGTgLNTH----PQYA-VRVAEELA---ALSGQPFVTA--PNkfealatcDALVHAHGALKGLAASLMKIANDVRWLA 299
Cdd:PLN02848 212 GAVGN-YNAHmsayPEVDwPAVAEEFVtslGLTFNPYVTQiePH--------DYMAELFNAVSRFNNILIDFDRDIWSYI 282
|
170 180 190
....*....|....*....|....*....|....*
gi 695764396 300 SgprcgIG---EIAIPeNEPGSSIMPGKVNPTQCE 331
Cdd:PLN02848 283 S-----LGyfkQITKA-GEVGSSTMPHKVNPIDFE 311
|
|
| |
