|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-458 |
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: 930.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 1 MEYRIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVI 80
Cdd:COG0114 2 METRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 81 AGKWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENHVL 159
Cdd:COG0114 82 AGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLgGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 160 PAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPK 239
Cdd:COG0114 162 PALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 240 FGEMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIM 319
Cdd:COG0114 242 FAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 320 PGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKEN 399
Cdd:COG0114 322 PGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEEL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 822529177 400 VNRSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMI 458
Cdd:COG0114 402 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-462 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 924.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 1 MEYRIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVI 80
Cdd:PRK00485 2 METRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 81 AGKWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENHVL 159
Cdd:PRK00485 82 AGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLgGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 160 PAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPK 239
Cdd:PRK00485 162 PALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 240 FGEMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIM 319
Cdd:PRK00485 242 FAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 320 PGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKEN 399
Cdd:PRK00485 322 PGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKEL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822529177 400 VNRSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAPKE 462
Cdd:PRK00485 402 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
4-457 |
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: 852.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGK 83
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 84 WNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQILKEK-ESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENHVLPAI 162
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVlGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 163 TKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGE 242
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 243 MVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPGK 322
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 323 VNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNR 402
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 822529177 403 SLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKM 457
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
3-459 |
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: 822.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 3 YRIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAG 82
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 83 KWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQILKEKESDVH-IHPNDDVNMSQSSNDTFPTALHVACVIAVENHVLPA 161
Cdd:TIGR00979 81 KLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQpVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 162 ITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFG 241
Cdd:TIGR00979 161 LENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 242 EMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPG 321
Cdd:TIGR00979 241 EKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 322 KVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVN 401
Cdd:TIGR00979 321 KVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 822529177 402 RSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIA 459
Cdd:TIGR00979 401 NSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
4-453 |
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: 800.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGK 83
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 84 WNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQILKEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENHVLPAIT 163
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 164 KLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGEM 243
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 244 VSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPGKV 323
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 324 NPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNRS 403
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 822529177 404 LMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVD 453
Cdd:cd01596 401 LMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
10-460 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 686.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 10 IGEIKVPADKLWAAQTQRSKENFPIG--TEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGKWNEH 87
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 88 FPLVVWQTGSGTQSNMNVNEVIANRGNQILKEKESDVH-IHPNDDVNMSQSSNDTFPTALHVACVIAVENHVLPAITKLK 166
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSpVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 167 ETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGEMVSE 246
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 247 EISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPGKVNPT 326
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 327 QSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNRSLML 406
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 822529177 407 VTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAP 460
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
4-461 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 616.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPL--EIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIA 81
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 82 GKWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQILKEKESDV-HIHPNDDVNMSQSSNDTFPTALHVACVIAVEnHVLP 160
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYdYVHPNDHVNMSQSTNDVYPTAIRLALLLLLR-ELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 161 AITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKF 240
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 241 GEMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMP 320
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 321 GKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENV 400
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822529177 401 NRSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAPK 461
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-461 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 597.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 1 MEYRIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQM--PLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADE 78
Cdd:PRK12273 3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 79 VIAGKWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVEnH 157
Cdd:PRK12273 83 ILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLgHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR-K 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 158 VLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAH 237
Cdd:PRK12273 162 LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 238 PKFGEMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSS 317
Cdd:PRK12273 242 PGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 318 IMPGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIK 397
Cdd:PRK12273 322 IMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822529177 398 ENVNRSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAPK 461
Cdd:PRK12273 402 EYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
4-453 |
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: 587.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGK 83
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 84 WNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENhVLPAI 162
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLgHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 163 TKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGE 242
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 243 MVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPGK 322
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 323 VNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNR 402
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 822529177 403 SLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVD 453
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
1-461 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 578.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 1 MEYRIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVI 80
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 81 AGKWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVEnHVL 159
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLgGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLE-GLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 160 PAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPK 239
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 240 FGEMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIM 319
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 320 PGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKEN 399
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822529177 400 VNRSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAPK 461
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
4-460 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 577.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGK 83
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 84 WNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENHVLPAI 162
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAgNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 163 TKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGE 242
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 243 MVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPGK 322
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 323 VNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNR 402
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 822529177 403 SLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAP 460
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
4-460 |
6.12e-157 |
|
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: 453.13 E-value: 6.12e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPL--EIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVI- 80
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 81 AGKWNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQILKEKESD-VHIHPNDDVNMSQSSNDTFPTALHVACVIAVENhVL 159
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEyQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIK-LV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 160 PAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPK 239
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 240 FGEMVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIM 319
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 320 PGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKEN 399
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822529177 400 VNRSLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAP 460
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
4-460 |
4.88e-153 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 443.67 E-value: 4.88e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 4 RIERDTIGEIKVPADKLWAAQTQRSKENFPIGTEQMPLEIVKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGK 83
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 84 WNEHFPLVVWQTGSGTQSNMNVNEVIANRGNQIL-KEKESDVHIHPNDDVNMSQSSNDTFPTALHVACVIAVENhVLPAI 162
Cdd:PRK14515 92 WHDHFIVDPIQGGAGTSMNMNANEVIANRALELLgMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG-LLQTM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 163 TKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGE 242
Cdd:PRK14515 171 GYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 243 MVSEEISQFTGKQFISAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPANEPGSSIMPGK 322
Cdd:PRK14515 251 AVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 323 VNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNR 402
Cdd:PRK14515 331 VNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEK 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 822529177 403 SLMLVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKMIAP 460
Cdd:PRK14515 411 SVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
11-340 |
1.15e-134 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 390.19 E-value: 1.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 11 GEIKVPADKLWAAQTQRSKENFPIGTEQmpleiVKAFAILKKSAAlsnqKLGKLSEEKAEAIVAAADEVIA-GKWNEHFP 89
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAA----KANVILKEEAAAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 90 LVVWQTGSGTQSNMNVNEVIANRGNQilkekesdvHIHPNDDVNMSQSSNDTFPTALHVACVIAVENHVLPAITKLKETL 169
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIGELLGQ---------LVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 170 AEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNT-YMKELAIGGTAVGTGINAHPKFGEMVSEEI 248
Cdd:pfam00206 143 KEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPrLLVLPLGGGTAVGTGLNADPEFAELVAKEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 249 SQFTGKQFIsAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRWLASGPrSGLGEIIIPANEPGSSIMPGKVNPTQS 328
Cdd:pfam00206 223 GFFTGLPVK-APNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQL 300
|
330
....*....|..
gi 822529177 329 EALTMVVAQVMG 340
Cdd:pfam00206 301 ELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
44-392 |
1.29e-116 |
|
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: 344.87 E-value: 1.29e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 44 VKAFAILKKSAALSNQKLGKLSEEKAEAIVAAADEVIAGKWNEHFplvvWQTGSGTQSNMNVNEVIANRGNQIlkekesd 123
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 124 vhihPNDDVNMSQSSNDTFPTALHVACVIAVEnHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWH 203
Cdd:cd01334 70 ----NGGYVHTGRSSNDIVDTALRLALRDALD-ILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 204 RMLEKTERMIAESNTYMKELAIGGTAVGTGINAHPKFGEMVSEEISQFTgkqfiSAPNKFHALTSHDEVVYTHGALKALA 283
Cdd:cd01334 145 AELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGFFG-----PAPNSTQAVSDRDFLVELLSALALLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 284 ADLMKIANDVRWLASGprsGLGEIIIPAN-EPGSSIMPGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPV 362
Cdd:cd01334 220 VSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPV 296
|
330 340 350
....*....|....*....|....*....|
gi 822529177 363 IAYNFLQSAHLLADAIVSFNDNCAvGIEAD 392
Cdd:cd01334 297 EREALPDSFDLLDAALRLLTGVLE-GLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
103-382 |
2.01e-55 |
|
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: 183.96 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 103 MNVNEVIANRGNQILKekesdvHIHPNDDVNMSQSSNDtFPTALHVACVIAVENHVLPAITKLKETLAEKVTAFEHIIKI 182
Cdd:cd01594 14 ALVEEVLAGRAGELAG------GLHGSALVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 183 GRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNtymkelaiggtavgtginahpkfgemvseeisqftgkqfisapnk 262
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 263 fhaltshdeVVYTHGALKALAADLMKIANDVRWLASGPRSGLGEIIIPaNEPGSSIMPGKVNPTQSEALTMVVAQVMGND 342
Cdd:cd01594 122 ---------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 822529177 343 ATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSFN 382
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
406-457 |
8.72e-28 |
|
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: 104.71 E-value: 8.72e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 822529177 406 LVTALNPHIGYENAAKIAKHAHKEGLTLKEAALQSGLLTEEQFNEIVDPKKM 457
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
156-458 |
3.86e-22 |
|
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: 98.23 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 156 NHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGW-HRMLEKTERmIAESNTYMKELAIGGtAVGTGi 234
Cdd:COG0015 116 ELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWaAELLRQLER-LEEARERVLVGKIGG-AVGTY- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 235 NAHPKFGEMVSEEISQFTGKQFISA-----PNKFHAltshdEVVythGALKALAADLMKIANDVRWLAsgpRSGLGEI-- 307
Cdd:COG0015 193 AAHGEAWPEVEERVAEKLGLKPNPVttqiePRDRHA-----ELF---SALALIAGSLEKIARDIRLLQ---RTEVGEVee 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 308 IIPANEPGSSIMPGKVNPTQSEALTMVVAQVMGNdATIGFAASQGNFE--------LNVFKPVIaynFLQSAHLLADAIV 379
Cdd:COG0015 262 PFAKGQVGSSAMPHKRNPIDSENIEGLARLARAL-AAALLEALASWHErdlsdssvERNILPDA---FLLLDGALERLLK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 380 SFNdncavGIEADEEVIKENVNRSLMLV------TALNPH-IGYENA----AKIAKHAHKEGLTLKEAALQ----SGLLT 444
Cdd:COG0015 338 LLE-----GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAyelvKELARGAWEEGNDLRELLAAdpeiPAELS 412
|
330
....*....|....
gi 822529177 445 EEQFNEIVDPKKMI 458
Cdd:COG0015 413 KEELEALFDPANYL 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
117-455 |
1.28e-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: 96.65 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 117 LKEKESDVHIHpnddVNMSQSSNDTFPTALHVACVIAVEnHVLPAITKLKETLAEKvtAFEH--IIKIGRTHLQDATPLT 194
Cdd:TIGR00928 80 LKEKCGAEGEF----IHFGATSNDIVDTALALLLRDALE-IILPKLKQLIDRLKEL--AVEYkdTVMLGRTHGQHAEPTT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 195 LGQEISGWH-RMLEKTERMIAESNTYmkelAIGGT--AVGTGINAHPKFGEmVSEEISQFTGKQFISAPNKFHALTSHDE 271
Cdd:TIGR00928 153 LGKRFALWAeEMLRQLERLLQAKERI----KVGGIsgAVGTHAAAYPLVEE-VEERVTEFLGLKPVPISTQIEPRDRHAE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 272 VVYthgALKALAADLMKIANDVRWLAsgpRSGLGEIIIPA--NEPGSSIMPGKVNPTQSE---ALTMVVAQVMGndatig 346
Cdd:TIGR00928 228 LLD---ALALLATTLEKFAVDIRLLQ---RTEHFEVEEPFgkGQVGSSAMPHKRNPIDFEnvcGLARVIRGYAS------ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 347 fAASQGN---FELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNRSLMLVTALNPHI-------GY 416
Cdd:TIGR00928 296 -PALENAplwHERDLTDSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGR 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 822529177 417 ENA-AKIAKHAHK----EGLTLKEAALQSG----LLTEEQFNEIVDPK 455
Cdd:TIGR00928 375 EEAyEIVRELAMGaaevDEPDLLEFLLEDEritkYLKEEELAELLDPE 422
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
156-427 |
8.28e-21 |
|
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: 93.72 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 156 NHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGtAVGTGIN 235
Cdd:cd01595 106 DIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 236 AHPKfGEMVSEEISQFTGKQFISAPNKFHALTSHDEVVythGALKALAADLMKIANDVRWLAsgpRSGLGEIIIP--ANE 313
Cdd:cd01595 185 LGPK-GPEVEERVAEKLGLKVPPITTQIEPRDRIAELL---SALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 314 PGSSIMPGKVNPTQSEALTMVVAQVMGNDATIGFAASQgNFELNVFKPVIAYNFLQSAHLLADAIVSFNDNCAVGIEADE 393
Cdd:cd01595 258 VGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQ-WHERDLSDSSVERNILPDAFLLLDAALSRLQGLLEGLVVNP 336
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 822529177 394 EVIKENVNRSLMLV------TALNPH-IGYENAAKIAKHAH 427
Cdd:cd01595 337 ERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
157-455 |
1.61e-18 |
|
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: 87.30 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 157 HVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGtAVGTgina 236
Cdd:cd01597 117 LLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT---- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 237 HPKFGE---MVSEEISQFTGKQFISAPnkFHalTSHDEVVYTHGALKALAADLMKIANDVRWLAsgpRSGLGEIIIP--A 311
Cdd:cd01597 192 LASLGDqglAVQEALAAELGLGVPAIP--WH--TARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 312 NEPGSSIMPGKVNPTQSEALTmVVAQVMGNDATIGFAASQGNFElnvfKPVIAY----NFLQSAHLLADAIVSFNDNCAV 387
Cdd:cd01597 265 GRGGSSTMPHKRNPVGCELIV-ALARRVPGLAALLLDAMVQEHE----RDAGAWhaewIALPEIFLLASGALEQAEFLLS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 388 GIEADEEVIKEN--VNRSLML----VTALNPHIGYENA----AKIAKHAHKEGLTLKEAALQ----SGLLTEEQFNEIVD 453
Cdd:cd01597 340 GLEVNEDRMRANldLTGGLILseavMMALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpevAAYLSDEELDALLD 419
|
..
gi 822529177 454 PK 455
Cdd:cd01597 420 PA 421
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
59-454 |
2.82e-13 |
|
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: 71.62 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 59 QKLGKLSEEKAEAIVAA----ADEVIAGKWNEHFPLvvwqtgsgTQSNMNV-NEVIANRGNQILKEkesdvhihpnddVN 133
Cdd:TIGR00838 43 KKAGILTEEEAAKIIEGlnelKEEGREGPFILDPDD--------EDIHMAIeRELIDRVGEDLGGK------------LH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 134 MSQSSNDTFPTALHVACVIAVeNHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMI 213
Cdd:TIGR00838 103 TGRSRNDQVATDLRLYLRDHV-LELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 214 AESNTYMKELAIGGTAV-GTGINAHPKFgemvSEEISQFTGkqfiSAPNKFHALTSHDEVVYTHGALKALAADLMKIAND 292
Cdd:TIGR00838 182 QDALKRVNVSPLGSGALaGTGFPIDREY----LAELLGFDA----VTENSLDAVSDRDFILELLFVAALIMVHLSRFAED 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 293 VRWLASGPrsgLGEIIIP-ANEPGSSIMPGKVNPTQSEALTMVVAQVMGNDATIgfaasqgnfeLNVFKPV-IAYN--FL 368
Cdd:TIGR00838 254 LILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM----------LMTLKALpLAYNrdLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 369 QSAHLLADAIvsfnDNCAVGIEADEEVIKE-NVNRSLMLVTALNphiGYENAAKIAKHAHKEGLTLKEA----------A 437
Cdd:TIGR00838 321 EDKEPLFDAL----KTVELSLEMATGMLDTiTVNKERMEEAASA---GFSNATELADYLVRKGVPFREAhhivgelvatA 393
|
410 420
....*....|....*....|....
gi 822529177 438 LQSGLLTEE-------QFNEIVDP 454
Cdd:TIGR00838 394 IERGKGLEEltleelqKFSPEFDE 417
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
156-458 |
3.08e-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: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 156 NHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGTaVGTGIN 235
Cdd:cd03302 113 DLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQAS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 236 AHPKFG------EMVSEEISQFTG--KQFISA----PNKFHAltshdEVVythGALKALAADLMKIANDVRWLAsgprsG 303
Cdd:cd03302 192 FLDLFEgdhdkvEALDELVTKKAGfkKVYPVTgqtySRKVDI-----DVL---NALSSLGATAHKIATDIRLLA-----N 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 304 LGEIIIP--ANEPGSSIMPGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNFELNVFKPVIAYNFLQSAHLLADAIVSF 381
Cdd:cd03302 259 LKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSANRRIAIPEAFLAADAILIT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 382 NDNCAVGIEADEEVIKENVNRSLmlvtalnPHIGYENA---------------AKIAKHAHKEGLTLKEAALQSGLL--- 443
Cdd:cd03302 339 LQNISEGLVVYPKVIERHIRQEL-------PFMATENIimaavkaggdrqdahERIRVLSHQAAAVVKQEGGDNDLIeri 411
|
330 340
....*....|....*....|...
gi 822529177 444 --------TEEQFNEIVDPKKMI 458
Cdd:cd03302 412 kndayfkpIWDELDALLDPKTFI 434
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
138-332 |
1.76e-11 |
|
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: 65.65 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 138 SNDTFPTALHVACVIAVEnHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWH----RMLEKTERMI 213
Cdd:cd01360 91 SSDVVDTALALQLREALD-IILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYaefkRHLERLKEAR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 214 aESNTYMKelaIGGtAVGTGINAHPKFGEMV-------SEEISQftgkQFIsaPNKFHAltshdEVVYThgaLKALAADL 286
Cdd:cd01360 170 -ERILVGK---ISG-AVGTYANLGPEVEERVaeklglkPEPIST----QVI--QRDRHA-----EYLST---LALIASTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822529177 287 MKIANDVRWLAsgpRSGLGEIIIP--ANEPGSSIMPGKVNPTQSEALT 332
Cdd:cd01360 231 EKIATEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENIC 275
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
158-454 |
4.52e-10 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 61.57 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 158 VLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGtAVGTgINAH 237
Cdd:PRK09053 127 LEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGT-LASL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 238 PKFGEMVSEEISQFTGKQFISAPnkFHalTSHDEVVYTHGALKALAADLMKIANDVRWLAsgpRSGLGEIIIPA--NEPG 315
Cdd:PRK09053 205 GEQALPVAQALAAELQLALPALP--WH--TQRDRIAEFASALGLLAGTLGKIARDVSLLM---QTEVGEVFEPAaaGKGG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 316 SSIMPGKVNPTQSEALTMVVAQVMGNDATIgFAASQGNFELNVFKPVIAYNFL-QSAHLLADAIVSFNDnCAVGIEADEE 394
Cdd:PRK09053 278 SSTMPHKRNPVGCAAVLTAATRAPGLVATL-FAAMPQEHERALGGWHAEWDTLpELACLAAGALAQMAQ-IVEGLEVDAA 355
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822529177 395 VIKEN--VNRSLML----VTALNPHIGYENAAKIAKHAHK----EGLTLKEA----ALQSGLLTEEQFNEIVDP 454
Cdd:PRK09053 356 RMRANldLTHGLILaeavMLALADRIGRLDAHHLVEQASKravaEGRHLRDVlaedPQVSAHLSPAALDRLLDP 429
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
153-356 |
6.39e-09 |
|
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: 57.63 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 153 AVENHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKelaIGGtAVGT 232
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQIEILGK---FNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 233 gINAHpkfgeMVS------EEISQFtgkqFISAPN-KFHALT----SHDEVVYTHGALKALAADLMKIANDVrWL-ASgp 300
Cdd:cd01598 192 -FNAH-----LVAypdvdwRKFSEF----FVTSLGlTWNPYTtqiePHDYIAELFDALARINTILIDLCRDI-WGyIS-- 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822529177 301 rSGLGEIIIPANEPGSSIMPGKVNPtqsealtmvvaqvmgndatIGFAASQGNFEL 356
Cdd:cd01598 259 -LGYFKQKVKKGEVGSSTMPHKVNP-------------------IDFENAEGNLGL 294
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
278-458 |
3.27e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 53.88 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 278 ALKALAADLMKIANDVRWLAsGPRSGLGEIIIPANEPGSSIMPGKVNPTQSEALTMVVAQVMGNDATIGFAASQGNfELN 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWH-ERD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 358 VF-KPV--IAynfLQSAHLLADAIVSFNDNCAVGIEADEEVIKENVNRSL-------MLVTALNPHIGYENA-AKIAKHA 426
Cdd:PRK08937 100 LShSSAerIA---LPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGREEAhELIREKA 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 822529177 427 ---HKEGLTLKEAALQ----SGLLTEEQFNEIVDPKKMI 458
Cdd:PRK08937 177 meaWKNQKDLRELLEAderfTKQLTKEELDELFDPEAFV 215
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
52-410 |
6.56e-08 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 54.73 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 52 KSAALSNQKLGKLSEEKAEAIVAAADEvIAGKW-NEHFplvVWQTGsgtqsNMNVNEVIANRGNQILKEKESDVHihpnd 130
Cdd:PLN02646 53 KAHASMLAKQGIITDEDRDSILDGLDE-IEKEIeAGKF---EWRPD-----REDVHMNNEARLTELIGEPAKKLH----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 131 dvnMSQSSNDTFPTALHVACVIAVENhVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQ----EISGWHRML 206
Cdd:PLN02646 119 ---TARSRNDQVATDTRLWCRDAIDV-IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHwllsHVEQLERDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 207 EKTERMIAESNTymkeLAIGGTAV-GTGInahPKFGEMVSEEISqFTGkqfiSAPNKFHALTSHDEVVYTHGALKALAAD 285
Cdd:PLN02646 195 GRLVDCRPRVNF----CPLGSCALaGTGL---PIDRFMTAKDLG-FTA----PMRNSIDAVSDRDFVLEFLFANSITAIH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 286 LMKIANDVRWLASGPRSGLgeIIIPANEPGSSIMPGKVNPTQSEALTMVVAQVMGNDATIgfaasqgnfeLNVFKPV-IA 364
Cdd:PLN02646 263 LSRLGEEWVLWASEEFGFV--TPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTV----------LALCKGLpTA 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 822529177 365 YN--FLQSAHLLADAIVSFND------NCAVGIEADEEVIKENVNRSLMLVTAL 410
Cdd:PLN02646 331 YNrdLQEDKEPLFDSVDTVSDmlevatEFAQNITFNPERIKKSLPAGMLDATTL 384
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
153-329 |
6.65e-07 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 51.66 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 153 AVENHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKelaIGGtAVGT 232
Cdd:PLN02848 141 GVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVKIKGK---FAG-AVGN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 233 gINAH----PKFG-EMVSEEISQFTGKQFisapNKF-HALTSHDEVVYTHGALKALAADLMKIANDVrWlaSGPRSGLGE 306
Cdd:PLN02848 217 -YNAHmsayPEVDwPAVAEEFVTSLGLTF----NPYvTQIEPHDYMAELFNAVSRFNNILIDFDRDI-W--SYISLGYFK 288
|
170 180
....*....|....*....|...
gi 822529177 307 IIIPANEPGSSIMPGKVNPTQSE 329
Cdd:PLN02848 289 QITKAGEVGSSTMPHKVNPIDFE 311
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
137-459 |
2.35e-06 |
|
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: 49.85 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 137 SSNDTFPTALHVACVIAVEnHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAES 216
Cdd:cd01359 86 SRNDQVATDLRLYLRDALL-ELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 217 NTYMKELAIGGTA-VGTGINAHPkfgEMVSEEISqFTGkqfiSAPNKFHALTSHDEVVYTHGALKALAADLMKIANDVRW 295
Cdd:cd01359 165 YKRVNVSPLGAGAlAGTTFPIDR---ERTAELLG-FDG----PTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 296 LASGPRSglgeIIIPANE--PGSSIMPGKVNPTQSEALTMVVAQVMGNDATIgFAASQG-----NFELNVFKPVI--AYN 366
Cdd:cd01359 237 WSTQEFG----FVELPDAysTGSSIMPQKKNPDVLELIRGKAGRVIGALAGL-LTTLKGlplayNKDLQEDKEPLfdAVD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 367 FLQSAHLLADAIVSfndncavGIEADEEVIKENVNRSLMLVTALN---------P-HIGYENAAKIAKHAHKEGLTLKEA 436
Cdd:cd01359 312 TLIASLRLLTGVIS-------TLTVNPERMREAAEAGFSTATDLAdylvrekgvPfREAHHIVGRAVRLAEEKGKDLSDL 384
|
330 340
....*....|....*....|....*..
gi 822529177 437 AL----QSGLLTEEQFNEIVDPKKMIA 459
Cdd:cd01359 385 TLaelqAISPLFEEDVREALDPENSVE 411
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
153-356 |
1.11e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 47.44 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 153 AVENHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGW-HRMlektERMIA--ESNTYM-KelaIGGt 228
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVaYRL----ERQLKqlEAVEILgK---ING- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 229 AVGTgINAH---------PKFGEmvseeisqftgkQFISA----PNkfhALT----SHDEVVYTHGALKALAADLMKIAN 291
Cdd:PRK09285 210 AVGN-YNAHlaaypevdwHAFSR------------EFVESlgltWN---PYTtqiePHDYIAELFDAVARFNTILIDLDR 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 292 DVrWLAS-----GPRSGLGEIiipanepGSSIMPGKVNPtqsealtmvvaqvmgndatIGFAASQGNFEL 356
Cdd:PRK09285 274 DV-WGYIslgyfKQKTKAGEI-------GSSTMPHKVNP-------------------IDFENSEGNLGL 316
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
136-453 |
1.95e-04 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 44.00 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 136 QSSNDTFPTALHVACViAVENHVLPAITKLKETLAEKVTAFEHIIKIGRTHLQDATPLTLGQEISGWHRMLEKTERMIAE 215
Cdd:PRK12308 107 RSRNDQVATDLKLWCR-QQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLED 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 216 SNTYMKELAIG-GTAVGTginAHPkfgeMVSEEISQFTGkqFISAP-NKFHALTSHDEVVythgALKALAADLM----KI 289
Cdd:PRK12308 186 ALTRLDTCPLGsGALAGT---AYP----IDREALAHNLG--FRRATrNSLDSVSDRDHVM----ELMSVASISMlhlsRL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 290 ANDVRWLASGpRSGLGEIIIPANEpGSSIMPGKVNPTQSEALTMVVAQVMGNDATIgfaasqgnfeLNVFKPV-IAYN-- 366
Cdd:PRK12308 253 AEDLIFYNSG-ESGFIELADTVTS-GSSLMPQKKNPDALELIRGKTGRVYGALAGM----------MMTVKALpLAYNkd 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 367 FLQSAHLLADAIVSFNDN------CAVGIEADEEVIKENVNRslmlvtalnphiGYENAAKIAKHAHKEGLTLKEA---- 436
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCmemaalCFDGIKVNGERTLEAAKQ------------GYANATELADYLVAKGIPFREAhhiv 388
|
330 340
....*....|....*....|....*..
gi 822529177 437 ------ALQSGL----LTEEQFNEIVD 453
Cdd:PRK12308 389 gvavvgAIAKGCaleeLSLEQLKEFSD 415
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
183-331 |
3.03e-03 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 39.65 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822529177 183 GRTHLQDATPLTLGQEISGWHRMLEKTERMIAESNTYMKELAIGGtAVGTGINAHPKfGEMVSEEISQFTGkqFISAPnk 262
Cdd:PRK05975 152 GHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--LEDAP-- 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822529177 263 fHALTSHDEVVYTHGALKALAADLMKIANDVRWLASgprsgLGEIIIPANEPGSSIMPGKVNPTQSEAL 331
Cdd:PRK05975 226 -QWHSQRDFIADFAHLLSLVTGSLGKFGQDIALMAQ-----AGDEISLSGGGGSSAMPHKQNPVAAETL 288
|
|
| |
