|
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: 978.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 1 MTTVRHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 81 LAGKHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 161 IPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHP 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 241 EYAVRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 321 MPGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQ 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1452266132 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVGSLK 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: 965.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 1 MTTVRHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 81 LAGKHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 161 IPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHP 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 241 EYAVRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 321 MPGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQ 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1452266132 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVG 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: 905.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 4 VRHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAG 83
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 84 KHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQLIPQ 163
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 164 LNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYA 243
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 244 VRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG 323
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 324 KVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLN 403
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1452266132 404 ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVG 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: 902.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 5 RHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAGK 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQLIPQL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 165 NVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 245 RVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 325 VNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLNE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1452266132 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAM 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: 829.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 5 RHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAGK 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGmERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQLIPQL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 165 NVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 245 RVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 325 VNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLNE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1452266132 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVR 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: 738.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 11 MGAIAVPADKLWGAQTQRSLEHFRIS--TEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAGKHPDE 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 89 FPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQLIPQLNVLK 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 169 STLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYAVRVAE 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 249 ELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 329 QCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLNESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1452266132 409 VTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVG 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: 625.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 5 RHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAGK 84
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQLIPQL 164
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 165 NVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 245 RVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 325 VNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLNE 404
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1452266132 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVGS 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: 620.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 5 RHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPV--SLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLA 82
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 83 GKHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREqLIP 162
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 163 QLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEY 242
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 243 AVRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMP 322
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 323 GKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLL 402
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1452266132 403 NESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVG 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: 604.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 1 MTTVRHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKM---PvSLIQALALTKRAAAKVNQDLGLLDADKATAIINAA 77
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdyP-ELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 78 DEVLAGKHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIR 157
Cdd:PRK12273 81 DEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 158 EqLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLN 237
Cdd:PRK12273 161 K-LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 238 THPEYAVRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPG 317
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 318 SSIMPGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRER 397
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1452266132 398 ISQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMVG 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: 593.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 5 RHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAGK 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 85 HPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREqLIPQL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 165 NVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 245 RVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 325 VNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLNE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1452266132 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFD 451
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELD 446
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
2-460 |
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 1452266132 2 TTVRHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVL 81
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 82 AGKHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIrEQLI 161
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL-EGLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 162 PQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPE 241
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 242 YAVRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 322 PGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQL 401
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1452266132 402 LNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMV 460
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-460 |
1.04e-150 |
|
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]
Pssm-ID: 213564 [Multi-domain] Cd Length: 468 Bit Score: 437.34 E-value: 1.04e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 5 RHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKM---PVsLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVL 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKIsdiPE-FVRGMVMVKKAAALANKELGTIPESIANAIVAACDEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 82 -AGKHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAaVIAIREQL 160
Cdd:TIGR00839 80 nNGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIA-VYSSLIKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 161 IPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHP 240
Cdd:TIGR00839 159 VDAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 241 EYAVRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:TIGR00839 239 EYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 321 MPGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQ 400
Cdd:TIGR00839 319 MPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 401 LLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAMV 460
Cdd:TIGR00839 399 YVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLM 458
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
1.85e-147 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 422.93 E-value: 1.85e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 12 GAIAVPADKLWGAQTQRSLEHFRISTEKmpvslIQALALTKRAAAKVNQDLglldADKATAIINAADEVLA-GKHPDEFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 91 LAIWQTGSGTQSNMNMNEVLAnrasELLGgvrgmeRKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIREQLIPQLNVLKST 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 171 LNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLP-HLAELALGGTAVGTGLNTHPEYAVRVAEE 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPrLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 250 LASITGQPfVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPrCGIGEISIPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 1452266132 330 CEAMTMLCCQVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
4-459 |
5.75e-138 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 405.15 E-value: 5.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 4 VRHEKDSMGAIAVPADKLWGAQTQRSLEHFRISTEKMPVSLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAG 83
Cdd:PRK14515 11 VRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 84 KHPDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAVIAIrEQLIPQ 163
Cdd:PRK14515 91 KWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNAL-EGLLQT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 164 LNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYA 243
Cdd:PRK14515 170 MGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 244 VRVAEELASITGQPFVTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG 323
Cdd:PRK14515 250 EAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 324 KVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLN 403
Cdd:PRK14515 330 KVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVE 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1452266132 404 ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAM 459
Cdd:PRK14515 410 KSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEM 465
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-394 |
3.68e-126 |
|
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: 369.14 E-value: 3.68e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 45 IQALALTKRAAAKVNQDLGLLDADKATAIINAADEVLAGKHPDEFplaiWQTGSGTQSNMNMNEVLANRASELLGGVrgm 124
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGGY--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 125 erkvhpnddVNKSQSSNDVFPTaMHVAAVIAIREQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGW 204
Cdd:cd01334 74 ---------VHTGRSSNDIVDT-ALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 205 VAMLEHNLKHIENSLPHLAELALGGTAVGTGLNTHPEYAVRVAEELASitgqpFVTAPNKFEALATCDALVHTHGALKGL 284
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 285 AASLMKIANDVRWLASGprcGIGEISIPEN-EPGSSIMPGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASGNFELNVYRP 363
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 1452266132 364 MVIHNVLQSVRLLADGMESFNEHCAvGIEPN 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 |
2.07e-59 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 194.36 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 104 MNMNEVLANRASELLGGVrgmerkvHPNDDVNKSQSSNDVFPTAMHVAAVIAIREqLIPQLNVLKSTLNEKAQAFRDIVK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDIGTTALRLALRDALDD-LLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 184 IGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSlphlaelalggtavgtglnthpeyavrvaeelasitgqpfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 264 kfealatcdALVHTHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPeNEPGSSIMPGKVNPTQCEAMTMLCCQVMGN 343
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1452266132 344 DVAVNMGGASGNFELNVYRPMVIHNVLQSVRLLADGMESFN 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
140-461 |
3.98e-30 |
|
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: 121.34 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 140 SNDVFPTAMhvaaVIAIRE---QLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIE 216
Cdd:COG0015 99 SQDINDTAL----ALQLREaleLLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 217 NSLPHLAELALGGtAVGTgLNTHPEYAVRVAEELAS--------ITGQpfvTAPNKFEAlatcdALVHthgALKGLAASL 288
Cdd:COG0015 175 EARERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEklglkpnpVTTQ---IEPRDRHA-----ELFS---ALALIAGSL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 289 MKIANDVRWLAsgpRCGIGEIS--IPENEPGSSIMPGKVNPTQCEAMTMLCCQVMGNdVAV---NM-------GGASGNf 356
Cdd:COG0015 242 EKIARDIRLLQ---RTEVGEVEepFAKGQVGSSAMPHKRNPIDSENIEGLARLARAL-AAAlleALaswherdLSDSSV- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 357 ELNVYRPMVIHnVLQSVRLLADGMEsfnehcavGIEPNRERISQLLNESLMLV------TALNTH-IG----YDKAAEIA 425
Cdd:COG0015 317 ERNILPDAFLL-LDGALERLLKLLE--------GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELA 387
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1452266132 426 KKAHKEGLTLKASALA----LGYLTEAEFDAWVRPEAMVG 461
Cdd:COG0015 388 RGAWEEGNDLRELLAAdpeiPAELSKEELEALFDPANYLG 427
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
9.55e-26 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 98.93 E-value: 9.55e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1452266132 408 LVTALNTHIGYDKAAEIAKKAHKEGLTLKASALALGYLTEAEFDAWVRPEAM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
140-429 |
6.00e-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: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 140 SNDVFPTAMhvaaVIAIREQL---IPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIE 216
Cdd:cd01595 89 SQDINDTAL----ALQLRDALdiiLPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 217 NSLPHLAELALGGtAVGTGLNTH---PEYAVRVAEEL----ASITGQpfvTAPNkfealatcDALVHTHGALKGLAASLM 289
Cdd:cd01595 165 EARERVLVGGISG-AVGTHASLGpkgPEVEERVAEKLglkvPPITTQ---IEPR--------DRIAELLSALALIAGTLE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 290 KIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAMTMLCCQVMGNDVAVNMGGASgNFElnvyRPM--- 364
Cdd:cd01595 233 KIATDIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQ-WHE----RDLsds 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1452266132 365 -VIHNVLQSVRLLADGMESFNEHCAVGIEPNRERISQLLNESLMLV------TAL-NTHIGYDKAAEIAKKAH 429
Cdd:cd01595 305 sVERNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALaKKGLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
43-462 |
3.38e-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: 95.39 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 43 SLIQALALTKRAAAKVNQDLGLLDADKATAIINAADEvlagKHPDEFPLAIwQTGSGTQSNMNMNEVLANRASELLGgvr 122
Cdd:cd01597 19 NRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADV----ERLDLEALAE-ATARTGHPAIPLVKQLTAACGDAAG--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 123 gmeRKVHpnddvnKSQSSNDVFPTAMhvaaVIAIREQLI---PQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQ 199
Cdd:cd01597 91 ---EYVH------WGATTQDIIDTAL----VLQLRDALDlleRDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 200 EISGWVAMLEHNLKHIENSLPHLAELALGGtAVGTglnthpeyavrvaeeLASITGQPFVTAPNKFEAL----------A 269
Cdd:cd01597 158 KVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT---------------LASLGDQGLAVQEALAAELglgvpaipwhT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 270 TCDALVHTHGALKGLAASLMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAMTMLCCQVMGnDVAV 347
Cdd:cd01597 222 ARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 348 NMGGASGNFElnvyRP-MVIHN----VLQSVRLLADGMESFnEHCAVGIEPNRERISQLLN--------ESLMLvtALNT 414
Cdd:cd01597 298 LLDAMVQEHE----RDaGAWHAewiaLPEIFLLASGALEQA-EFLLSGLEVNEDRMRANLDltgglilsEAVMM--ALAP 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1452266132 415 HIGYDKA----AEIAKKAHKEGLTLKASALA----LGYLTEAEFDAWVRPEAMVGS 462
Cdd:cd01597 371 KLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpevAAYLSDEELDALLDPANYLGS 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
140-462 |
6.34e-21 |
|
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: 94.72 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 140 SNDVFPTAMHVAAVIAIrEQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVA-MLEH--NLKHIE 216
Cdd:TIGR00928 97 SNDIVDTALALLLRDAL-EIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEeMLRQleRLLQAK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 217 NSLPhlaelaLGGT--AVGTGLNTHPEYAV---RVAEEL----ASITGQpfvTAPNKFEAlATCDALVHthgalkgLAAS 287
Cdd:TIGR00928 176 ERIK------VGGIsgAVGTHAAAYPLVEEveeRVTEFLglkpVPISTQ---IEPRDRHA-ELLDALAL-------LATT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 288 LMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAMTMLCCQVMGNDVAVnMGGASGNFELNVYRPMV 365
Cdd:TIGR00928 239 LEKFAVDIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPA-LENAPLWHERDLTDSSV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 366 IHNVLQSVRLLADGM-ESFNEHCAvGIEPNRERISQLLNESLMLVTALNTHI-------GYDKAAEIAKK-----AHKEG 432
Cdd:TIGR00928 315 ERVILPDAFILADIMlKTTLKVVK-KLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRElamgaAEVDE 393
|
330 340 350
....*....|....*....|....*....|....
gi 1452266132 433 LTLKASALALG----YLTEAEFDAWVRPEAMVGS 462
Cdd:TIGR00928 394 PDLLEFLLEDEritkYLKEEELAELLDPETYIGN 427
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
53-460 |
2.30e-19 |
|
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: 89.91 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 53 RAAAKVNQDLGLLDADKATAIINAADEVLAGKHPDEFPLaiwqTGSGTQSNMNmNEvlaNRASELLGGVRGmerKVHpnd 132
Cdd:cd01359 17 IAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFEL----DPEDEDIHMA-IE---RRLIERIGDVGG---KLH--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 133 dvnKSQSSNDVFPTAMHVAAVIAIREqLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNL 212
Cdd:cd01359 83 ---TGRSRNDQVATDLRLYLRDALLE-LLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 213 KHIENSLPHLAELALGGTA-VGTGLNTHPEyavRVAEEL--ASITgqpfvtaPNKFEALATCDALVHTHGALKGLAASLM 289
Cdd:cd01359 159 ERLADAYKRVNVSPLGAGAlAGTTFPIDRE---RTAELLgfDGPT-------ENSLDAVSDRDFVLEFLSAAALLMVHLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 290 KIANDVRWLASGPRcgiGEISIPEN-EPGSSIMPGKVNPTQCEAMTMLCCQVMGNDVAV-----NMGGASGNFELNVYRP 363
Cdd:cd01359 229 RLAEDLILWSTQEF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLlttlkGLPLAYNKDLQEDKEP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 364 M--VIHNVLQSVRLLADGMEsfnehcavGIEPNRERISQLLNESLMLVTAL------NTHI----GYDKAAEIAKKAHKE 431
Cdd:cd01359 306 LfdAVDTLIASLRLLTGVIS--------TLTVNPERMREAAEAGFSTATDLadylvrEKGVpfreAHHIVGRAVRLAEEK 377
|
410 420 430
....*....|....*....|....*....|...
gi 1452266132 432 GLTLKASALA----LGYLTEAEFDAWVRPEAMV 460
Cdd:cd01359 378 GKDLSDLTLAelqaISPLFEEDVREALDPENSV 410
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
140-337 |
1.47e-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: 84.14 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 140 SNDVFPTAMHVAAVIAIREqLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSL 219
Cdd:cd01360 91 SSDVVDTALALQLREALDI-ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEAR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 220 PHLAELALGGtAVGTGLNTHPEYAVRVAEEL----ASITGQpfVTAPNKFEALATcdalvhthgALKGLAASLMKIANDV 295
Cdd:cd01360 170 ERILVGKISG-AVGTYANLGPEVEERVAEKLglkpEPISTQ--VIQRDRHAEYLS---------TLALIASTLEKIATEI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1452266132 296 RWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAMTMLC 337
Cdd:cd01360 238 RHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
53-343 |
1.43e-14 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 75.47 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 53 RAAAKVNQDLGLLDADKATAIINAADEVLagKHPDEFPLaIWQTgsgTQSNMNMNevLANRASELLGgvRGMERKVHpnd 132
Cdd:TIGR00838 36 IAHTKMLKKAGILTEEEAAKIIEGLNELK--EEGREGPF-ILDP---DDEDIHMA--IERELIDRVG--EDLGGKLH--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 133 dvnKSQSSNDVFPTAMHVAAVIAIREqLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNL 212
Cdd:TIGR00838 103 ---TGRSRNDQVATDLRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 213 KHIENSLPHLAELALGGTAV-GTGLNTHPEYAvrvAEELasitGQPFVTApNKFEALATCDALVHTHGALKGLAASLMKI 291
Cdd:TIGR00838 179 ERLQDALKRVNVSPLGSGALaGTGFPIDREYL---AELL----GFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRF 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1452266132 292 ANDVRWLASGPrcgIGEISIP-ENEPGSSIMPGKVNPTQCEAMTMLCCQVMGN 343
Cdd:TIGR00838 251 AEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
147-461 |
1.71e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 75.05 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 147 AMHVAAVIAIRE---QLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLA 223
Cdd:PRK09053 111 IIDTGLVLQLRDaldLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 224 ELALGGtAVGTgLNTHPEYAVRVAEELASITGQPFVTAPNKFEAlatcDALVHTHGALKGLAASLMKIANDVRWLAsgpR 303
Cdd:PRK09053 191 VLQFGG-AAGT-LASLGEQALPVAQALAAELQLALPALPWHTQR----DRIAEFASALGLLAGTLGKIARDVSLLM---Q 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 304 CGIGEISIP--ENEPGSSIMPGKVNPTQCEAM------------TMLCCQVMGNDVAvnMGGASGNFElnvyrpmvihnV 369
Cdd:PRK09053 262 TEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERA--LGGWHAEWD-----------T 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 370 LQSVRLLADGMESFNEHCAVGIEPNRERISQ--------LLNESLMLvtALNTHIGYDKAAEI----AKKAHKEGLTLK- 436
Cdd:PRK09053 329 LPELACLAAGALAQMAQIVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEGRHLRd 406
|
330 340
....*....|....*....|....*...
gi 1452266132 437 ---ASALALGYLTEAEFDAWVRPEAMVG 461
Cdd:PRK09053 407 vlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-327 |
3.02e-13 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 71.11 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 155 AIREQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENsLPHLAelALGGtAVGT 234
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQ-IEILG--KFNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 235 gLNTH---------PEYAVRVAEELAsITGQPFVT--APNKFEAlATCDALVHTHGALKGLaaslmkiANDVrWlasgpr 303
Cdd:cd01598 192 -FNAHlvaypdvdwRKFSEFFVTSLG-LTWNPYTTqiEPHDYIA-ELFDALARINTILIDL-------CRDI-W------ 254
|
170 180 190
....*....|....*....|....*....|.
gi 1452266132 304 cgiGEISI-------PENEPGSSIMPGKVNP 327
Cdd:cd01598 255 ---GYISLgyfkqkvKKGEVGSSTMPHKVNP 282
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
151-342 |
3.55e-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: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 151 AAVIAIREQL---IPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELAL 227
Cdd:cd03302 103 TDLIQIRDALdliLPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 228 GGTaVGTG-----LNTHPEYAVRVAEELAS----------ITGQpfvTAPNKFEALATCdalvhthgALKGLAASLMKIA 292
Cdd:cd03302 183 KGT-TGTQasfldLFEGDHDKVEALDELVTkkagfkkvypVTGQ---TYSRKVDIDVLN--------ALSSLGATAHKIA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1452266132 293 NDVRWLAsgprcGIGEISIP--ENEPGSSIMPGKVNPTQCEAMTMLCCQVMG 342
Cdd:cd03302 251 TDIRLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
155-327 |
2.21e-11 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 65.54 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 155 AIREQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENsLPHLAElaLGGtAVGT 234
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEA-VEILGK--ING-AVGN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 235 gLNTH----PEYA-VRVAEElasitgqpFVTAPN-KFEALAT----CDALVHTHGALKGLAASLMKIANDVrWlasgprc 304
Cdd:PRK09285 214 -YNAHlaayPEVDwHAFSRE--------FVESLGlTWNPYTTqiepHDYIAELFDAVARFNTILIDLDRDV-W------- 276
|
170 180 190
....*....|....*....|....*....|
gi 1452266132 305 giGEIS-------IPENEPGSSIMPGKVNP 327
Cdd:PRK09285 277 --GYISlgyfkqkTKAGEIGSSTMPHKVNP 304
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
63-327 |
9.74e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 63.63 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 63 GLLDADKATAIINAADEVLAGKHPDEFPLAIwqtgsgtqSNMNMNEVLANRASELLGGVRGmerKVHpnddvnKSQSSND 142
Cdd:PRK00855 51 GILSEEEAEKILAGLDEILEEIEAGKFEFSP--------ELEDIHMAIEARLTERIGDVGG---KLH------TGRSRND 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 143 vfptamHVAAviAIR-------EQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHI 215
Cdd:PRK00855 114 ------QVAT--DLRlylrdeiDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 216 ENSLPHLAELALGGTA-VGTGLNTHPEYavrVAEEL--ASITgqpfvtaPNKFEALATCDALVHTHGALKGLAASLMKIA 292
Cdd:PRK00855 186 RDARKRVNRSPLGSAAlAGTTFPIDRER---TAELLgfDGVT-------ENSLDAVSDRDFALEFLSAASLLMVHLSRLA 255
|
250 260 270
....*....|....*....|....*....|....*..
gi 1452266132 293 ND-VRWlaSGPRCGIgeISIPEN-EPGSSIMPGKVNP 327
Cdd:PRK00855 256 EElILW--SSQEFGF--VELPDAfSTGSSIMPQKKNP 288
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
20-347 |
3.41e-10 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 62.05 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 20 KLWGAQTQRS----LEHFRIStekmpVSLIQALA----LTKRAAAKVNQDLGLLDADKATAIINAADEVLAGKHPDEFpl 91
Cdd:PLN02646 17 KLWGGRFEEGvtpaVEKFNES-----ISFDKRLYkediMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 92 aIWQTGsgtQSNMNMNevLANRASELLGGVRGmerKVHpnddvnKSQSSNDVFPTAMHVAAVIAIREqLIPQLNVLKSTL 171
Cdd:PLN02646 90 -EWRPD---REDVHMN--NEARLTELIGEPAK---KLH------TARSRNDQVATDTRLWCRDAIDV-IRKRIKTLQVAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 172 NEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGGTAV-GTGLNTHPEYavrVAEEL 250
Cdd:PLN02646 154 VELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALaGTGLPIDRFM---TAKDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 251 AsITGqpfvTAPNKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRCGIgeisIPEN--EPGSSIMPGKVNPT 328
Cdd:PLN02646 231 G-FTA----PMRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFV----TPSDavSTGSSIMPQKKNPD 301
|
330
....*....|....*....
gi 1452266132 329 QCEAMTMLCCQVMGNDVAV 347
Cdd:PLN02646 302 PMELVRGKSARVIGDLVTV 320
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
121-336 |
1.06e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 53.52 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 121 VRGMERKVHPN--DDVNKSQSSNDVFPTAMhVAAVIAIREQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLG 198
Cdd:PRK05975 87 VRQLRAAVGEEaaAHVHFGATSQDVIDTSL-MLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 199 QEISGWVAMLEHNLKHIENSLPHLAELALGGtAVGTGLNTHPEyAVRVAEELASITGqpFVTAPnkfEALATCDALVHTH 278
Cdd:PRK05975 166 DRLASWRAPLLRHRDRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--LEDAP---QWHSQRDFIADFA 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1452266132 279 GALKGLAASLMKIANDVRWLASGPrcgiGEISIPENEpGSSIMPGKVNPTQCEAMTML 336
Cdd:PRK05975 239 HLLSLVTGSLGKFGQDIALMAQAG----DEISLSGGG-GSSAMPHKQNPVAAETLVTL 291
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-461 |
1.16e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 52.34 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 280 ALKGLAASLMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAMTMLCCQVMGNdVAVNMGGASGNFE 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIGSERITGLARVLRSY-LVTALENVPLWHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 358 LNVYrpmviHNVLQSVRLL-----ADGMESFNEHCAVGIEPNRERISQLLNESL-------MLVTALNTHIG----YDKA 421
Cdd:PRK08937 98 RDLS-----HSSAERIALPdaflaLDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaHELI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1452266132 422 AEIAKKAHKEGLTLKASALA----LGYLTEAEFDAWVRPEAMVG 461
Cdd:PRK08937 173 REKAMEAWKNQKDLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
158-349 |
1.03e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 50.94 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 158 EQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALG-GTAVGTGl 236
Cdd:PRK12308 126 QQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTA- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 237 nthpeYAVRvAEELASITGqpFVTAP-NKFEALATCDALVHTHGALKGLAASLMKIANDVRWLASGPRcgiGEISIPEN- 314
Cdd:PRK12308 205 -----YPID-REALAHNLG--FRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSGES---GFIELADTv 273
|
170 180 190
....*....|....*....|....*....|....*
gi 1452266132 315 EPGSSIMPGKVNPTQCEAMTMLCCQVMGNDVAVNM 349
Cdd:PRK12308 274 TSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMM 308
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
41-327 |
3.57e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.46 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 41 PVSLIQALALTKRAAAKVNQDLGLLDADKATAIInaaDEVLAGKHPDEFPLAIWQTGSGTQsnMNMNEVLANRASELLGG 120
Cdd:PRK02186 434 PLAELDHLAAIDEAHLVMLGDTGIVAPERARPLL---DAHRRLRDAGFAPLLARPAPRGLY--MLYEAYLIERLGEDVGG 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 121 VrgmerkvhpnddVNKSQSSNDVFPTAmhvaAVIAIREQL---IPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTL 197
Cdd:PRK02186 509 V------------LQTARSRNDINATT----TKLHLREATsraFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 198 GQEISGWVAMLEHNLKHIENSLPHLAELALG-GTAVGTGLNTHPEyavRVAEELASITGqpfvtAPNKFEALATCDALVH 276
Cdd:PRK02186 573 GHYLLAVDGALARETHALFALFEHIDVCPLGaGAGGGTTFPIDPE---FVARLLGFEQP-----APNSLDAVASRDGVLH 644
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1452266132 277 THGALKGLAASLMKIANDVR-WLASgprcGIGEISIPEN-EPGSSIMPGKVNP 327
Cdd:PRK02186 645 FLSAMAAISTVLSRLAQDLQlWTTR----EFALVSLPDAlTGGSSMLPQKKNP 693
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
155-331 |
1.72e-04 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 43.96 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 155 AIREQLIPQLNVLKSTLNEKAQAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIeNSLPHLAELAlggTAVGT 234
Cdd:PLN02848 141 GVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQL-SEVKIKGKFA---GAVGN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 235 gLNTH----PEYA-VRVAEELASITG---QPFVTAPNKFEALATCDALVHTHGALkglaasLMKIANDVRWLASgprcgI 306
Cdd:PLN02848 217 -YNAHmsayPEVDwPAVAEEFVTSLGltfNPYVTQIEPHDYMAELFNAVSRFNNI------LIDFDRDIWSYIS-----L 284
|
170 180
....*....|....*....|....*...
gi 1452266132 307 G---EISIPeNEPGSSIMPGKVNPTQCE 331
Cdd:PLN02848 285 GyfkQITKA-GEVGSSTMPHKVNPIDFE 311
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
185-331 |
1.97e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 43.73 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452266132 185 GRTHLQDATPLTLGQEISGWVAMLEHNLKHIENSLPHLAELALGgtaVGTGLNTHPEYAVRVAEELASItgQPFVTAPnK 264
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYG---YGSGYGSPSSVKFNQMSELLGM--EKNIKNP-V 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1452266132 265 FEALATCDALVHTHGALKGLAASLMKIANDvrwLASGPRCGIGEISiPENEPGSSIMPGKVNPTQCE 331
Cdd:PRK06389 221 YSSSLYIKTIENISYLISSLAVDLSRICQD---IIIYYENGIITIP-DEFTTGSSLMPNKRNPDYLE 283
|
|
| G-alpha |
pfam00503 |
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ... |
357-419 |
4.95e-03 |
|
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular signaling pathways. The G protein alpha subunit binds guanyl nucleotide and is a weak GTPase. A set of residues that are unique to G-alpha as compared to its ancestor the Arf-like family form a ring of residues centered on the nucleotide binding site. A Ggamma is found fused to an inactive Galpha in the Dictyostelium protein gbqA.
Pssm-ID: 459835 [Multi-domain] Cd Length: 316 Bit Score: 38.72 E-value: 4.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1452266132 357 ELNVYRPMVIHNVLQSVRLLADGMESFNEHCAvgIEPNRERISQLLN--ESLMLVTALNTHIGYD 419
Cdd:pfam00503 37 ERKQYRPVIYSNILRSLKTLIEAMERLGIELS--NPENKERLDDLLSldSSLKNETEFTPELAED 99
|
|
| |
