|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-451 |
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: 923.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:COG0114 11 MGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVIAGKLDDHFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:COG0114 91 LDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERLLPALEHLRDT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:COG0114 171 LEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPGFAERVAAEL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:COG0114 251 AELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMPGKVNPTQC 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:COG0114 331 EALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELLERSLMLVT 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIG 451
Cdd:COG0114 411 ALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-453 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 922.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:PRK00485 11 MGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVIAGKHDDHFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:PRK00485 91 LDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERLLPALEHLRDT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:PRK00485 171 LAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPGFAERVAEEL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:PRK00485 251 AELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMPGKVNPTQC 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:PRK00485 331 EALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELLERSLMLVT 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGPR 453
Cdd:PRK00485 411 ALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
1-449 |
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: 884.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:cd01362 7 MGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGKLDDHFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:cd01362 87 LVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPALKHLIDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:cd01362 167 LDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAEKVAAEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:cd01362 247 AELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:cd01362 327 EALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLERSLMLVT 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDM 449
Cdd:cd01362 407 ALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
1-445 |
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: 810.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:cd01596 7 LGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGKLDDQFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGsKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:cd01596 87 LDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALEQLQDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:cd01596 166 LDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEKVAAEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:cd01596 246 AELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKVNPVIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:cd01596 326 EAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENSLMLVT 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVR 445
Cdd:cd01596 406 ALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
1-451 |
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: 807.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:TIGR00979 8 MGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAGKLDDHFP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:TIGR00979 88 LVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPALENLKKT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:TIGR00979 168 LDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDEKVAEEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:TIGR00979 248 AKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGKVNPTQC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:TIGR00979 328 EALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNNSLMLVT 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIG 451
Cdd:TIGR00979 408 ALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
1-454 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 778.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDT--MPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEH 78
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERerMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 79 FPLRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLR 158
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 159 SALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAG 238
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 239 HIAEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPT 318
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 319 QVEAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLML 398
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 663503220 399 VTALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGPRD 454
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPSD 456
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
1-452 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 616.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:PRK12425 9 LGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQHDDQFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:PRK12425 89 LVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAIAELSGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:PRK12425 169 LAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAEAIAAEL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:PRK12425 249 AALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGKVNPTQC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:PRK12425 329 EALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLERGLMLVT 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGP 452
Cdd:PRK12425 409 ALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
1-453 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 608.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMP--RSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEH 78
Cdd:COG1027 7 LGEREVPADAYYGIQTLRALENFPISGRPISdhPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIAGKLHDQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 79 FPLRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLR 158
Cdd:COG1027 87 FVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLR-ELLEALERLQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 159 SALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAG 238
Cdd:COG1027 166 EAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYIELVVE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 239 HIAEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPT 318
Cdd:COG1027 246 HLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 319 QVEAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLML 398
Cdd:COG1027 326 IPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVENSIGL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 663503220 399 VTALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGPR 453
Cdd:COG1027 406 VTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-453 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTM--PRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEH 78
Cdd:PRK12273 12 LGEREVPADAYYGIHTLRAVENFPISGVKIsdYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACDEILAGKLHDQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 79 FPLRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLR 158
Cdd:PRK12273 92 FVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR-KLLDALEQLQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 159 SALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAG 238
Cdd:PRK12273 171 EAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPPGYIELVVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 239 HIAEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPT 318
Cdd:PRK12273 251 KLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIMPGKVNPV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 319 QVEAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLML 398
Cdd:PRK12273 331 IPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREYVENSIGI 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 663503220 399 VTALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGPR 453
Cdd:PRK12273 411 VTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
1-440 |
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: 562.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:cd01357 7 LGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGKLHDQFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLRSA 160
Cdd:cd01357 87 VDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLR-KLLDALAALQEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:cd01357 166 FQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIELVVEKL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:cd01357 246 SEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:cd01357 326 EVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENSIGIVT 405
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQF 440
Cdd:cd01357 406 ALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEEL 445
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
1-453 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 545.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:PRK13353 12 LGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILAGKLHDQFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVnHRLLPAVSHLRSA 160
Cdd:PRK13353 92 VDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL-EGLLAAMGALQDV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:PRK13353 171 FEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYIERVVKHL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:PRK13353 251 AAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPGKVNPVMP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:PRK13353 331 EVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVEKSVGIAT 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGPR 453
Cdd:PRK13353 411 ALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
1-452 |
1.02e-153 |
|
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: 444.27 E-value: 1.02e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPR--SVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVI-SGSLDE 77
Cdd:TIGR00839 7 LGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILnNGKCHD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 78 HFPLRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNhRLLPAVSHL 157
Cdd:TIGR00839 87 QFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLI-KLVDAINQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 158 RSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVA 237
Cdd:TIGR00839 166 RDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEYSPLVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 238 GHIAEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNP 317
Cdd:TIGR00839 246 KKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 318 TQVEAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLM 397
Cdd:TIGR00839 326 VVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYVFNSIG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 663503220 398 LVTALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGP 452
Cdd:TIGR00839 406 IVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
1-452 |
8.20e-145 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 422.10 E-value: 8.20e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 1 MGDVEVPADRYYGAQTARSLLNFDIGEDTMPRSVIRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFP 80
Cdd:PRK14515 18 LGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDGKWHDHFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIANRAIEISGGTVGSKTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLRSA 160
Cdd:PRK14515 98 VDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALE-GLLQTMGYMHDV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAGHI 240
Cdd:PRK14515 177 FELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIEAVVKHL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 241 AEKTSLGFVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQV 320
Cdd:PRK14515 257 AAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGKVNPVMP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 321 EAMTMVCCQVMGNHTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVT 400
Cdd:PRK14515 337 EVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEKSVGIIT 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 663503220 401 ALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDMIGP 452
Cdd:PRK14515 417 AVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
2-332 |
7.31e-132 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 382.87 E-value: 7.31e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 2 GDVEVPADRYYGAQTARSLLNFDIGEDTmprsvIRAFGILKQAACETNVELdqmdQNIGSLISSACDEVI-SGSLDEHFP 80
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 81 LRIWQTGSGTQTNMNANEVIAnraiEISGgtvgskTPVHPNDHVNRAQSSNDTFPTAMHIAAAEEVNHRLLPAVSHLRSA 160
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 161 LASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRV-ESAMGDLLELALGGTAVGTGLNTHPEFADTVAGH 239
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLqQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 240 IAEKTSLGfVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPrCGFGELSLPANEPGSSIMPGKVNPTQ 319
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 663503220 320 VEAMTMVCCQVMG 332
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
35-384 |
8.35e-122 |
|
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: 357.58 E-value: 8.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 35 IRAFGILKQAACETNVELDQMDQNIGSLISSACDEVISGSLDEHFplriWQTGSGTQTNMNANEVIANRAIEIsggtvgs 114
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 115 ktpvhPNDHVNRAQSSNDtFPTAMHIAAAEEVNHRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGY 194
Cdd:cd01334 70 -----NGGYVHTGRSSND-IVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 195 VSMLDADISRVESAMGDLLELALGGTAVGTGLNTHPEFADTVAghiaekTSLGF-VSAENKFAQLAAHDALVAASGALNT 273
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVA------ELLGFfGPAPNSTQAVSDRDFLVELLSALAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 274 LAASLMKIANDIRWLGSGprcGFGELSLPAN-EPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAISIGGSQGNFELNVYK 352
Cdd:cd01334 218 LAVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDS 294
|
330 340 350
....*....|....*....|....*....|..
gi 663503220 353 PMMIHNFLHSVRLLSDTCRSFTDKCvVGLEAN 384
Cdd:cd01334 295 PVEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
94-374 |
1.00e-61 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 200.14 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 94 MNANEVIANRAIEISGGtvgsktpVHPNDHVNRAQSSNDtFPTAMHIAAAEEVNHRLLPAVSHLRSALASKSRDFRSIVK 173
Cdd:cd01594 14 ALVEEVLAGRAGELAGG-------LHGSALVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 174 IGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAmgdllelalggtavgtglnthpefadtvaghiaektslgfvsaen 253
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 254 kfaqlaahdALVAASGALNTLAASLMKIANDIRWLGSGPRCGFGELSLPaNEPGSSIMPGKVNPTQVEAMTMVCCQVMGN 333
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 663503220 334 HTAISIGGSQGNFELNVYKPMMIHNFLHSVRLLSDTCRSFT 374
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
145-448 |
1.20e-27 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 114.41 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 145 EVNHRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGtAVGT 224
Cdd:COG0015 113 EALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 225 gLNTHPEFADTVAGHIAEKTSLGFVSAENkfaQLAAHDALVAASGALNTLAASLMKIANDIRWLGsgpRCGFGELSLP-- 302
Cdd:COG0015 192 -YAAHGEAWPEVEERVAEKLGLKPNPVTT---QIEPRDRHAELFSALALIAGSLEKIARDIRLLQ---RTEVGEVEEPfa 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 303 ANEPGSSIMPGKVNP---TQVEAMT-MVCCQVMGNHTAI------SIGGSQgnfelnVYKPMMIHNFLHSVRLLsdtcRS 372
Cdd:COG0015 265 KGQVGSSAMPHKRNPidsENIEGLArLARALAAALLEALaswherDLSDSS------VERNILPDAFLLLDGAL----ER 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 373 FTdKCVVGLEANEDRIATHLENSLMLV------TALNPH-IGYDNA-AKIAKNAHAKGTTlRQSALELgLLSDEQFTQWV 444
Cdd:COG0015 335 LL-KLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAyELVKELARGAWEE-GNDLREL-LAADPEIPAEL 411
|
....
gi 663503220 445 RAED 448
Cdd:COG0015 412 SKEE 415
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
398-449 |
6.32e-26 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 99.32 E-value: 6.32e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 663503220 398 LVTALNPHIGYDNAAKIAKNAHAKGTTLRQSALELGLLSDEQFTQWVRAEDM 449
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
150-317 |
1.49e-22 |
|
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: 98.73 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 150 LLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGtAVGTGLNTH 229
Cdd:cd01595 108 ILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHASLG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 230 PEfADTVAGHIAEKtsLGFvsAENKFA-QLAAHDALVAASGALNTLAASLMKIANDIRWLGsgpRCGFGELSLP--ANEP 306
Cdd:cd01595 187 PK-GPEVEERVAEK--LGL--KVPPITtQIEPRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQV 258
|
170
....*....|.
gi 663503220 307 GSSIMPGKVNP 317
Cdd:cd01595 259 GSSTMPHKRNP 269
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
157-451 |
2.73e-20 |
|
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.
Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 92.69 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 157 LRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGtAVGTgLNTHPEFADTV 236
Cdd:cd01597 125 LLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT-LASLGDQGLAV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 237 AGHIAEKTSLGfvsaENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGsgpRCGFGELSLP--ANEPGSSIMPGK 314
Cdd:cd01597 203 QEALAAELGLG----VPAIPWHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGGSSTMPHK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 315 VNPTQVEAMTmVCCQVMGNHTAISIGGSQGNFELN--------VYKPMMihnFLHSVRLLSDTCRsftdkCVVGLEANED 386
Cdd:cd01597 276 RNPVGCELIV-ALARRVPGLAALLLDAMVQEHERDagawhaewIALPEI---FLLASGALEQAEF-----LLSGLEVNED 346
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663503220 387 RIATHLE--NSLML----VTALNPHIGYDNA----AKIAKNAHAKGTTLRQSALE----LGLLSDEQFTQWVRAEDMIG 451
Cdd:cd01597 347 RMRANLDltGGLILseavMMALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpevAAYLSDEELDALLDPANYLG 425
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
68-337 |
4.34e-19 |
|
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: 89.34 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 68 DEVISGSLDEHFPLRiwqtgsgtqtnmNANEVIANRAIEISGGTVGSKTpvhpndHVNRaqSSNDTFPTAMHIAAAEEVN 147
Cdd:TIGR00838 65 EEGREGPFILDPDDE------------DIHMAIERELIDRVGEDLGGKL------HTGR--SRNDQVATDLRLYLRDHVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 148 HrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTAV-GTGL 226
Cdd:TIGR00838 125 E-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALaGTGF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 227 NTHPEFadtvaghIAEktSLGFVSA-ENKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGPrcgFGELSLP-AN 304
Cdd:TIGR00838 204 PIDREY-------LAE--LLGFDAVtENSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---FGFVELPdEF 271
|
250 260 270
....*....|....*....|....*....|...
gi 663503220 305 EPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAI 337
Cdd:TIGR00838 272 SSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM 304
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
123-448 |
4.89e-17 |
|
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: 82.78 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 123 HVNRAQSSNDTFPTA--MHIAAAEEVnhrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDA 200
Cdd:TIGR00928 90 FIHFGATSNDIVDTAlaLLLRDALEI---ILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 201 DISRVESAMGDLLelaLGGT--AVGTGLNTHPEFADtVAGHIAEKTSLGFVSAENkfaQLAAHDALVAASGALNTLAASL 278
Cdd:TIGR00928 167 QLERLLQAKERIK---VGGIsgAVGTHAAAYPLVEE-VEERVTEFLGLKPVPIST---QIEPRDRHAELLDALALLATTL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 279 MKIANDIRWLgsgPRCGFGELSLPA--NEPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAISIGGSQGNfELNVYKPMMI 356
Cdd:TIGR00928 240 EKFAVDIRLL---QRTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWH-ERDLTDSSVE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 357 HNFLHSVRLLSDTCRSFTDKCVVGLEANEDRIATHLENSLMLVTALNPHI-------GYDNAAKIAK-----NAHAKGTT 424
Cdd:TIGR00928 316 RVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRelamgAAEVDEPD 395
|
330 340
....*....|....*....|....
gi 663503220 425 LRQSALElgllsDEQFTQWVRAED 448
Cdd:TIGR00928 396 LLEFLLE-----DERITKYLKEEE 414
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
130-324 |
8.19e-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: 81.83 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 130 SNDTFPTA--MHIAAAEEVnhrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVES 207
Cdd:cd01360 91 SSDVVDTAlaLQLREALDI---ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 208 AMGDLLELALGGtAVGTGLNTHPEfadtVAGHIAEKTSLGFVSAENKFAQLAAHDALVAasgALNTLAASLMKIANDIRW 287
Cdd:cd01360 168 ARERILVGKISG-AVGTYANLGPE----VEERVAEKLGLKPEPISTQVIQRDRHAEYLS---TLALIASTLEKIATEIRH 239
|
170 180 190
....*....|....*....|....*....|....*....
gi 663503220 288 LgsgPRCGFGELSLP--ANEPGSSIMPGKVNPTQVEAMT 324
Cdd:cd01360 240 L---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENIC 275
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
127-402 |
9.03e-14 |
|
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: 72.96 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 127 AQSSNDTFPTAMHIAAAEEVNHrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVE 206
Cdd:cd01359 84 GRSRNDQVATDLRLYLRDALLE-LLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 207 SAMGDLLELALGGTA-VGTGLNTHPEFadtVAghiaekTSLGFVS-AENKFAQLAAHDALVAASGALNTLAASLMKIAND 284
Cdd:cd01359 163 DAYKRVNVSPLGAGAlAGTTFPIDRER---TA------ELLGFDGpTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAED 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 285 IRWLGSGPrcgFGELSLPAN-EPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAISigGSQGNFELNVYKPMM---IHNFL 360
Cdd:cd01359 234 LILWSTQE---FGFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLL--TTLKGLPLAYNKDLQedkEPLFD 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 663503220 361 hSVRLLSDTCRSFTDkCVVGLEANEDRIATHLENSLMLVTAL 402
Cdd:cd01359 309 -AVDTLIASLRLLTG-VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
127-317 |
6.97e-13 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 70.18 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 127 AQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVE 206
Cdd:PRK00855 108 GRSRNDQVATDLRLYLRDEID-EIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 207 SAMGDLLELALGGTA-VGTGLNTHPEFadtvaghIAEKtsLGFVS-AENKFAQLAAHDALVAASGALNTLAASLMKIAND 284
Cdd:PRK00855 187 DARKRVNRSPLGSAAlAGTTFPIDRER-------TAEL--LGFDGvTENSLDAVSDRDFALEFLSAASLLMVHLSRLAEE 257
|
170 180 190
....*....|....*....|....*....|....
gi 663503220 285 -IRWlgSGPRCGFGELSlPANEPGSSIMPGKVNP 317
Cdd:PRK00855 258 lILW--SSQEFGFVELP-DAFSTGSSIMPQKKNP 288
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
150-427 |
1.10e-10 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 63.50 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 150 LLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGtAVGTgLNTH 229
Cdd:PRK09053 127 LEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGT-LASL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 230 PEFADTVAGHIAEKTSLGFVSAenkfAQLAAHDALVAASGALNTLAASLMKIANDIRWLgsgPRCGFGELSLPA--NEPG 307
Cdd:PRK09053 205 GEQALPVAQALAAELQLALPAL----PWHTQRDRIAEFASALGLLAGTLGKIARDVSLL---MQTEVGEVFEPAaaGKGG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 308 SSIMPGKVNPtqVEAMTMVCCQV------------MGNHTAISIGGSQGNFELnvyKPMMihnflhsVRLLSDTCRSFTD 375
Cdd:PRK09053 278 SSTMPHKRNP--VGCAAVLTAATrapglvatlfaaMPQEHERALGGWHAEWDT---LPEL-------ACLAAGALAQMAQ 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663503220 376 kCVVGLEANEDRIATHLENSLMLV------TALNPHIGYDNAAKI----AKNAHAKGTTLRQ 427
Cdd:PRK09053 346 -IVEGLEVDAARMRANLDLTHGLIlaeavmLALADRIGRLDAHHLveqaSKRAVAEGRHLRD 406
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
127-317 |
3.21e-10 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 62.04 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 127 AQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVE 206
Cdd:COG0165 107 GRSRNDQVATDFRLYLRDEIL-ELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 207 SAMGDLLELALGGTAV-GTGLNTHPEFadtvaghIAEKtsLGFVS-AENKFAQLAAHDALVAASGALNTLAASLMKIAND 284
Cdd:COG0165 186 DAYKRLNVSPLGAAALaGTTFPIDRER-------TAEL--LGFDGpTENSLDAVSDRDFALEFLSAASLIMVHLSRLAEE 256
|
170 180 190
....*....|....*....|....*....|....
gi 663503220 285 IRWLGSGPrcgFGELSLP-ANEPGSSIMPGKVNP 317
Cdd:COG0165 257 LILWSSSE---FGFVELPdAFSTGSSIMPQKKNP 287
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
123-337 |
4.05e-10 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 61.72 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 123 HVNRaqSSNDTFPTAMHIAAAEEvNHRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADI 202
Cdd:PRK12308 104 HTGR--SRNDQVATDLKLWCRQQ-GQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDY 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 203 SRVESAMGDLLELALG-GTAVGTGLNTHPE-FADTVAGHIAEKTSLGFVSAENKFAQLAAhdalVAASGALNtlaasLMK 280
Cdd:PRK12308 181 SRLEDALTRLDTCPLGsGALAGTAYPIDREaLAHNLGFRRATRNSLDSVSDRDHVMELMS----VASISMLH-----LSR 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663503220 281 IANDIRWLGSGpRCGFGELSLPANEpGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAI 337
Cdd:PRK12308 252 LAEDLIFYNSG-ESGFIELADTVTS-GSSLMPQKKNPDALELIRGKTGRVYGALAGM 306
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
123-337 |
7.04e-10 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 60.77 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 123 HVNRaqSSNDTFPTAMHIAAAEEVNHrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADI 202
Cdd:PRK04833 104 HTGR--SRNDQVATDLKLWCKDQVAE-LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 203 SRVESAMGDLLELALG-GTAVGTglnTHPEFADTVAGhiaektSLGFVSA-ENKFAQLAAHDALVAasgALNTLAASLM- 279
Cdd:PRK04833 181 SRLQDALKRLDVSPLGsGALAGT---AYEIDREQLAG------WLGFASAtRNSLDSVSDRDHVLE---LLSDASISMVh 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 280 --KIANDIRWLGSGpRCGFGELSlPANEPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAI 337
Cdd:PRK04833 249 lsRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGM 306
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
150-324 |
1.70e-08 |
|
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: 56.56 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 150 LLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAMGDLLELALGGTavgTGlnTH 229
Cdd:cd03302 115 ILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT---TG--TQ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 230 PEFADTVAGH----------IAEKtsLGFVSAENKFAQLAA--HDALVAAsgALNTLAASLMKIANDIRWLGsgprcGFG 297
Cdd:cd03302 190 ASFLDLFEGDhdkvealdelVTKK--AGFKKVYPVTGQTYSrkVDIDVLN--ALSSLGATAHKIATDIRLLA-----NLK 260
|
170 180
....*....|....*....|....*....
gi 663503220 298 ELSLP--ANEPGSSIMPGKVNPTQVEAMT 324
Cdd:cd03302 261 EVEEPfeKGQIGSSAMPYKRNPMRSERCC 289
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
127-402 |
3.46e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 56.01 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 127 AQSSNDTFPTAMHIAAAEEVNHrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVE 206
Cdd:PRK02186 513 ARSRNDINATTTKLHLREATSR-AFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALF 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 207 SAMGDLLELALG-GTAVGTGLNTHPEFADTVaghiaektsLGF-VSAENKFAQLAAHDALVAASGALNTLAASLMKIAND 284
Cdd:PRK02186 592 ALFEHIDVCPLGaGAGGGTTFPIDPEFVARL---------LGFeQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQD 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 285 IR-WLGSGprcgFGELSLPAN-EPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAISIGGSQGNF--ELNVYKPMmihnfl 360
Cdd:PRK02186 663 LQlWTTRE----FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFsnSFEAGSPM------ 732
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 663503220 361 hsVRLLSDTCRSFTDKCVV------GLEANEDRIATHLENSLMLVTAL 402
Cdd:PRK02186 733 --NGPIAQACAAIEDAAAVlvllidGLEADQARMRAHLEDGGVSATAV 778
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
141-317 |
1.20e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 53.60 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 141 AAAEEVnhrLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVESAmgdllELA--LG 218
Cdd:PRK09285 137 EAREEV---LLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EILgkIN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 219 GtAVGTgLNTH----PEFaDTVAghIAEK--TSLGFVsaENKFA-QLAAHDALVAASGALNTLAASLMKIANDIrWlgsg 291
Cdd:PRK09285 209 G-AVGN-YNAHlaayPEV-DWHA--FSREfvESLGLT--WNPYTtQIEPHDYIAELFDAVARFNTILIDLDRDV-W---- 276
|
170 180 190
....*....|....*....|....*....|...
gi 663503220 292 prcgfGELSL-------PANEPGSSIMPGKVNP 317
Cdd:PRK09285 277 -----GYISLgyfkqktKAGEIGSSTMPHKVNP 304
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
144-321 |
1.32e-07 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 53.59 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 144 EEVNHRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVsmldadiSRVESAMGDLLELALGGT--- 220
Cdd:PLN02848 140 EGVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFA-------YRLSRQRKQLSEVKIKGKfag 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 221 AVGTgLNTH-PEFADTVAGHIAEK--TSLGfVSAENKFAQLAAHDALVAASGALNTLAASLMKIANDIrWlgSGPRCGFG 297
Cdd:PLN02848 213 AVGN-YNAHmSAYPEVDWPAVAEEfvTSLG-LTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDI-W--SYISLGYF 287
|
170 180
....*....|....*....|....
gi 663503220 298 ELSLPANEPGSSIMPGKVNPTQVE 321
Cdd:PLN02848 288 KQITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
137-317 |
2.77e-07 |
|
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: 52.62 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 137 AMHIAAAeeVNHRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVsmldadiSRVESAMGDLLELA 216
Cdd:cd01598 110 ALMIKEA--RNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFV-------YRLERQYKQLKQIE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 217 LGGT---AVGTgLNTHpefadTVA------GHIAEK--TSLGFvsAENKF-AQLAAHDALVAASGALNTLAASLMKIAND 284
Cdd:cd01598 181 ILGKfngAVGN-FNAH-----LVAypdvdwRKFSEFfvTSLGL--TWNPYtTQIEPHDYIAELFDALARINTILIDLCRD 252
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 663503220 285 IrWlgsgprcgfGELSL-------PANEPGSSIMPGKVNP 317
Cdd:cd01598 253 I-W---------GYISLgyfkqkvKKGEVGSSTMPHKVNP 282
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
122-326 |
5.93e-06 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 48.13 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 122 DHVNRAQSSNDTFPTAMHI---AAAEEVNHRLlpavSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSML 198
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLrlkAASEILAARL----GALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 199 DADISRVESAMGDLLELALGGtAVGTGLNTHPEfADTVAGHIAEKtsLGFVSAENKFAQlaaHDALVAASGALNTLAASL 278
Cdd:PRK05975 176 LRHRDRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKR--LGLEDAPQWHSQ---RDFIADFAHLLSLVTGSL 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663503220 279 MKIANDIRWLGSGPrcgfGELSLpANEPGSSIMPGKVNPtqVEAMTMV 326
Cdd:PRK05975 249 GKFGQDIALMAQAG----DEISL-SGGGGSSAMPHKQNP--VAAETLV 289
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
270-449 |
7.80e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 46.95 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 270 ALNTLAASLMKIANDIRwLGSGPRCGFGELSLPANEPGSSIMPGKVNPTQVEAMTMVCCQVMGNHTAISIGGSQGNfELN 349
Cdd:PRK08937 22 VLALIATSLEKFANEIR-LLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWH-ERD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 350 V-YKPM----MIHNFLhsvrLLSDTCRSFTDkCVVGLEANEDRIATHLENSLMLVTALNPHIGYDNAAKIAKNAHAkgtT 424
Cdd:PRK08937 100 LsHSSAeriaLPDAFL----ALDYILNRFVN-ILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHE---L 171
|
170 180 190
....*....|....*....|....*....|....
gi 663503220 425 LRQSALELG---------LLSDEQFTQWVRAEDM 449
Cdd:PRK08937 172 IREKAMEAWknqkdlrelLEADERFTKQLTKEEL 205
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
127-321 |
1.60e-05 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 47.03 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 127 AQSSNDTFPTAMHIAAAEEVNhRLLPAVSHLRSALASKSRDFRSIVKIGRTHLMDAVPLTLGQEFSGYVSMLDADISRVE 206
Cdd:PLN02646 120 ARSRNDQVATDTRLWCRDAID-VIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 207 SAMGDLLELALGGTAV-GTGLNTHPEFadtvaghIAEktSLGFVSA-ENKFAQLAAHDALVAASGALNTLAASLMKIAND 284
Cdd:PLN02646 199 DCRPRVNFCPLGSCALaGTGLPIDRFM-------TAK--DLGFTAPmRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEE 269
|
170 180 190
....*....|....*....|....*....|....*...
gi 663503220 285 IRWLGSGPrcgFGELSLP-ANEPGSSIMPGKVNPTQVE 321
Cdd:PLN02646 270 WVLWASEE---FGFVTPSdAVSTGSSIMPQKKNPDPME 304
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
175-321 |
5.07e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 42.19 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 175 GRTHLMDAVPLTLgQEFSGYV-SMLDADISRVESAMGDLLELALG-GTAVGTglnthPEFADTvaGHIAEKTSLGFVSAE 252
Cdd:PRK06389 147 GYTHFRQAMPMTV-NTYINYIkSILYHHINNLDSFLMDLREMPYGyGSGYGS-----PSSVKF--NQMSELLGMEKNIKN 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503220 253 NKFAQLAAHDALVAASGALNTLAASLMKIANDIRWLGSGprcgfGELSLPAN-EPGSSIMPGKVNPTQVE 321
Cdd:PRK06389 219 PVYSSSLYIKTIENISYLISSLAVDLSRICQDIIIYYEN-----GIITIPDEfTTGSSLMPNKRNPDYLE 283
|
|
| |
