|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-463 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 936.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 1 MSQTRTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 81 IDGKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 161 LPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRK 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 241 GFAEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 321 MPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDK 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219463173 401 LMKESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGPK 463
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-461 |
0e+00 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 924.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 1 MSQTRTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 81 IDGKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 161 LPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRK 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 241 GFAEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 321 MPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDK 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219463173 401 LMKESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIG 461
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
5-459 |
0e+00 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 870.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 5 RTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDGK 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 85 FDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTLLPGL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 165 RKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFAE 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 245 KVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 325 VNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLMKE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1219463173 405 SLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENM 459
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
5-455 |
0e+00 |
|
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 800.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 5 RTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDGK 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 85 FDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGsKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTLLPGL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 165 RKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFAE 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 245 KVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 325 VNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLMKE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1219463173 405 SLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVR 455
Cdd:cd01596 400 SLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
11-462 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 790.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 11 FGPLEVPSDKYWGAQTQRSILNFPIG--WEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDGKFDDN 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 89 FPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTLLPGLRKLH 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 169 DALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFAEKVAG 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 249 EIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 329 QAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLMKESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1219463173 409 VTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGP 462
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
5-461 |
0e+00 |
|
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]
Pssm-ID: 130052 [Multi-domain] Cd Length: 458 Bit Score: 785.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 5 RTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDGK 84
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 85 FDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTLLPGL 164
Cdd:TIGR00979 82 LDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 165 RKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFAE 244
Cdd:TIGR00979 162 ENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 245 KVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMPGK 324
Cdd:TIGR00979 242 KVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 325 VNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLMKE 404
Cdd:TIGR00979 322 VNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1219463173 405 SLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIG 461
Cdd:TIGR00979 402 SLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
5-463 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 611.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 5 RTETDSFGPLEVPSDKYWGAQTQRSILNFPIGweKQPVA----IVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEV 80
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPIS--GRPISdhpeLIRALAMVKKAAALANRELGLLDKEKADAIVAACDEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 81 IDGKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIgMVARDTL 160
Cdd:COG1027 79 IAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 161 LPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRK 240
Cdd:COG1027 158 LEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 241 GFAEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSI 320
Cdd:COG1027 238 GYIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 321 MPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDK 400
Cdd:COG1027 318 MPGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCRE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219463173 401 LMKESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGPK 463
Cdd:COG1027 398 YVENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
4-462 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 609.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 4 TRTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDG 83
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 84 KFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTLLPG 163
Cdd:PRK12425 82 QHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 164 LRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFA 243
Cdd:PRK12425 162 IAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 244 EKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMPG 323
Cdd:PRK12425 242 EAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 324 KVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLMK 403
Cdd:PRK12425 322 KVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1219463173 404 ESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGP 462
Cdd:PRK12425 402 RGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-463 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 588.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 1 MSQTRTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEK--QPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQ 78
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKisDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 79 EVIDGKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIgMVARD 158
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 159 TLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNT 238
Cdd:PRK12273 161 KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 239 RKGFAEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGS 318
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 319 SIMPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARI 398
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219463173 399 DKLMKESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGPK 463
Cdd:PRK12273 401 REYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-453 |
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: 563.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 5 RTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDGK 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 85 FDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDtLLPGL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 165 RKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFAE 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 245 KVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 325 VNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLMKE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1219463173 405 SLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRV 453
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEI 448
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
3-463 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 544.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 3 QTRTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEKQPVAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVID 82
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 83 GKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDtLLP 162
Cdd:PRK13353 84 GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG-LLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 163 GLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGF 242
Cdd:PRK13353 163 AMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 243 AEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMP 322
Cdd:PRK13353 243 IERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 323 GKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLM 402
Cdd:PRK13353 323 GKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219463173 403 KESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGPK 463
Cdd:PRK13353 403 EKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-462 |
3.25e-144 |
|
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: 420.78 E-value: 3.25e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 5 RTETDSFGPLEVPSDKYWGAQTQRSILNFPIGWEK---QPVaIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVI 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKisdIPE-FVRGMVMVKKAAALANKELGTIPESIANAIVAACDEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 82 D-GKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIgMVARDTL 160
Cdd:TIGR00839 80 NnGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAV-YSSLIKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 161 LPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRK 240
Cdd:TIGR00839 159 VDAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 241 GFAEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSI 320
Cdd:TIGR00839 239 EYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 321 MPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDK 400
Cdd:TIGR00839 319 MPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219463173 401 LMKESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGP 462
Cdd:TIGR00839 399 YVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
4-462 |
1.83e-140 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 411.32 E-value: 1.83e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 4 TRTETDSFGPLEVPSDKYWGAQTQRSILNFPI-GWEKQPvAIVRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVID 82
Cdd:PRK14515 11 VRIEKDFLGEKEVPNYAYYGVQTMRAVENFPItGYKIHE-GLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 83 GKFDDNFPLVVWQTGSGTQSNMNANEVISNRAIEIMGGEMGSKTPVHPNDHCNMGQSSNDTFPTAMHVAIgMVARDTLLP 162
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALEGLLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 163 GLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGF 242
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 243 AEKVAGEIAAITGLPFVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPENEPGSSIMP 322
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 323 GKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFTDNMVVGTQANVARIDKLM 402
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 403 KESLMLVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENMIGP 462
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
2.47e-134 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 389.42 E-value: 2.47e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 12 GPLEVPSDKYWGAQTQRSILNFPIGWEKqpvaiVRALGVIKKACAAVNLEFgdldAELAPAIDQAAQEVI-DGKFDDNFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 91 LVVWQTGSGTQSNMNANEVISnraiEIMGgemgskTPVHPNDHCNMGQSSNDTFPTAMHVAIGMVARDTLLPGLRKLHDA 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 171 LAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARV-EACLPDIYELAQGGTAVGTGLNTRKGFAEKVAGE 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLqQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 250 IAAITGLPfVTAPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPrSGLGELILPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 1219463173 330 AEALTMVCAHVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-394 |
4.86e-121 |
|
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: 356.04 E-value: 4.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 45 VRALGVIKKACAAVNLEFGDLDAELAPAIDQAAQEVIDGKFDDnfplVVWQTGSGTQSNMNANEVISNRAIEImggemgs 124
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAAD----QVEQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 125 ktpvhPNDHCNMGQSSNDTFPTAMHVAIgMVARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGY 204
Cdd:cd01334 70 -----NGGYVHTGRSSNDIVDTALRLAL-RDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 205 AHQVAKGIARVEACLPDIYELAQGGTAVGTGLNTRKGFAEKVAGEIaaitGLpFVTAPNKFEALAAHDAMVMFSGALKTV 284
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELL----GF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 285 AASLFKIANDMRLLGSGprsGLGELILPEN-EPGSSIMPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHFELNVYNP 363
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 1219463173 364 MMSYNVLQSMQLLGDAAGSFTdNMVVGTQAN 394
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLT-GVLEGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
104-384 |
6.04e-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: 198.60 E-value: 6.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 104 MNANEVISNRAIEIMGGEmgsktpvHPNDHCNMGQSSNDtFPTAMHVAIGMVARDTLLPGLRKLHDALAAKSDEFKDIIK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 184 IGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEAClpdiyelaqggtavgtglntrkgfaekvageiaaitglpfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 264 kfealaahdAMVMFSGALKTVAASLFKIANDMRLLGSGPRSGLGELILPeNEPGSSIMPGKVNPTQAEALTMVCAHVMGN 343
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1219463173 344 DAAVGFAGSQGHFELNVYNPMMSYNVLQSMQLLGDAAGSFT 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
156-461 |
1.38e-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: 114.03 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 156 ARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGtAVGTg 235
Cdd:COG0015 114 ALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 236 LNTRKGFAEKVAGEIAAITGLpfvtapnKFEALA----AHDAMVMFSGALKTVAASLFKIANDMRLLGsgpRSGLGEL-- 309
Cdd:COG0015 192 YAAHGEAWPEVEERVAEKLGL-------KPNPVTtqiePRDRHAELFSALALIAGSLEKIARDIRLLQ---RTEVGEVee 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 310 ILPENEPGSSIMPGKVNPtqaealtMVCAHVMGNdAAVgfagsqghfeLNVYNPMMSYNVLQSMQ-----------LLGD 378
Cdd:COG0015 262 PFAKGQVGSSAMPHKRNP-------IDSENIEGL-ARL----------ARALAAALLEALASWHErdlsdssvernILPD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 379 AAG-------SFT---DNMVVgtqaNVARIDK--------LMKESLMlvTALAPT-IGYDNA----TKVAKTAHKNGTTL 435
Cdd:COG0015 324 AFLlldgaleRLLkllEGLVV----NPERMRAnldltgglVLSEAVL--MALVRRgLGREEAyelvKELARGAWEEGNDL 397
|
330 340 350
....*....|....*....|....*....|.
gi 1219463173 436 KE-----EAIAlGFVDAETFDRVVRPENMIG 461
Cdd:COG0015 398 REllaadPEIP-AELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
156-343 |
5.87e-25 |
|
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: 105.66 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 156 ARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGtAVGTG 235
Cdd:cd01595 104 ALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 236 LNTRKGfAEKVAGEIAAITGLPFVTAPNKFEAlaaHDAMVMFSGALKTVAASLFKIANDMRLLGsgpRSGLGELILP--E 313
Cdd:cd01595 183 ASLGPK-GPEVEERVAEKLGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeK 255
|
170 180 190
....*....|....*....|....*....|
gi 1219463173 314 NEPGSSIMPGKVNPTQAEALTMVCAHVMGN 343
Cdd:cd01595 256 GQVGSSTMPHKRNPIDSENIEGLARLVRAL 285
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
4.27e-24 |
|
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: 94.31 E-value: 4.27e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1219463173 408 LVTALAPTIGYDNATKVAKTAHKNGTTLKEEAIALGFVDAETFDRVVRPENM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
133-343 |
3.26e-20 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 92.41 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 133 HCNMGQSSNDTFPTAMHVAIgMVARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGI 212
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLL-RDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 213 ARVEAClPDIYELAQGGTAVGTGLNTRKGFAEkVAGEIAAITGLPFVTAPNKFEAlaaHDAMVMFSGALKTVAASLFKIA 292
Cdd:TIGR00928 169 ERLLQA-KERIKVGGISGAVGTHAAAYPLVEE-VEERVTEFLGLKPVPISTQIEP---RDRHAELLDALALLATTLEKFA 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1219463173 293 NDMRLLgsgPRSGLGEL--ILPENEPGSSIMPGKVNPTQAEALTMVCAHVMGN 343
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVeePFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGY 293
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
136-334 |
3.54e-18 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 86.07 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 136 MGQSSNDTFPTAMhvAIGMV-ARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIAR 214
Cdd:cd01360 87 FGLTSSDVVDTAL--ALQLReALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLER 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 215 VEACLPDIyELAQGGTAVGTGLNtrkgFAEKVAGEIAAITGLPFVTAPNKfeaLAAHDAMVMFSGALKTVAASLFKIAND 294
Cdd:cd01360 165 LKEARERI-LVGKISGAVGTYAN----LGPEVEERVAEKLGLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATE 236
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1219463173 295 MRLLgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQAEALT 334
Cdd:cd01360 237 IRHL---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENIC 275
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
67-343 |
8.76e-15 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 76.24 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 67 AELAPAIDQAAQEVIDGKFDDNFPLvvwqtgsgtqsnMNANEVISNRAIEIMGGEMGSKtpVHpndhcnMGQSSNDTFPT 146
Cdd:TIGR00838 54 AKIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGK--LH------TGRSRNDQVAT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 147 AMHvaigMVARD---TLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARveacLPDIY 223
Cdd:TIGR00838 114 DLR----LYLRDhvlELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYER----LQDAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 224 E------LAQGGTAvGTGLNTRKGFaekvageIAAITGLPFVTApNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRL 297
Cdd:TIGR00838 186 KrvnvspLGSGALA-GTGFPIDREY-------LAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLIL 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1219463173 298 LGSGPrsgLGELILP-ENEPGSSIMPGKVNPTQAEALTMVCAHVMGN 343
Cdd:TIGR00838 257 WSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
136-461 |
2.89e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 74.67 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 136 MGQSSNDTFPTAMHVAIGMvARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARV 215
Cdd:PRK09053 104 WGATSQDIIDTGLVLQLRD-ALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 216 EACLPDIYELaQGGTAVGTgLNTRKGFAEKVAGEIAAITGLPFVTAPNKfealAAHDAMVMFSGALKTVAASLFKIANDM 295
Cdd:PRK09053 183 AALRPRALVL-QFGGAAGT-LASLGEQALPVAQALAAELQLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 296 RLLgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQAEALtMVCAHVMGNDAAVGFAG-SQGHfELNVYNPMMSYNVLQS 372
Cdd:PRK09053 257 SLL---MQTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAV-LTAATRAPGLVATLFAAmPQEH-ERALGGWHAEWDTLPE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 373 MQLLgdAAGSFtDNMVV---GTQANVARIDK--------LMKESLMLvtALAPTIGYDNATKV----AKTAHKNGTTLK- 436
Cdd:PRK09053 332 LACL--AAGAL-AQMAQiveGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEGRHLRd 406
|
330 340
....*....|....*....|....*...
gi 1219463173 437 ---EEAIALGFVDAETFDRVVRPENMIG 461
Cdd:PRK09053 407 vlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
156-327 |
5.55e-12 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 67.47 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 156 ARDT-LLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEAClpDIyeLAQGGTAVGT 234
Cdd:PRK09285 138 AREEvLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV--EI--LGKINGAVGN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 235 ---------GLNTRKgFAEKVageiaaITGL-----PFVTA--PnkfealaaHDAMVMFSGALKTVAASLFKIANDMRLL 298
Cdd:PRK09285 214 ynahlaaypEVDWHA-FSREF------VESLgltwnPYTTQieP--------HDYIAELFDAVARFNTILIDLDRDVWGY 278
|
170 180 190
....*....|....*....|....*....|.
gi 1219463173 299 GSgprsgLGEL--ILPENEPGSSIMPGKVNP 327
Cdd:PRK09285 279 IS-----LGYFkqKTKAGEIGSSTMPHKVNP 304
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
137-413 |
1.26e-11 |
|
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: 66.42 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 137 GQSSNDTFPTAMHvaigMVARD---TLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIA 213
Cdd:cd01359 84 GRSRNDQVATDLR----LYLRDallELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 214 RVEACLPDIYELAQGGTA-VGTGLNTRKgfaEKVAGEI--AAITglpfvtaPNKFEALAAHDAMVMFSGALKTVAASLFK 290
Cdd:cd01359 160 RLADAYKRVNVSPLGAGAlAGTTFPIDR---ERTAELLgfDGPT-------ENSLDAVSDRDFVLEFLSAAALLMVHLSR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 291 IANDMRLLGSGPRsglGELILPEN-EPGSSIMPGKVNPTQAEALTMVCAHVMGNDAAVgfagsqghfeLNVY-NPMMSYN 368
Cdd:cd01359 230 LAEDLILWSTQEF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGL----------LTTLkGLPLAYN 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1219463173 369 -VLQSMQ-LLGDAAGSFTD------NMVVGTQANVARIDKLMKESLMLVTALA 413
Cdd:cd01359 297 kDLQEDKePLFDAVDTLIAslrlltGVISTLTVNPERMREAAEAGFSTATDLA 349
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
156-342 |
2.00e-11 |
|
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: 65.80 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 156 ARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDI-YELAQGgtAVGT 234
Cdd:cd03302 111 ALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLrFRGVKG--TTGT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 235 G---LNTRKGFAEKV----------AG--EIAAITGLpfvTAPNKfealaaHDAMVMFsgALKTVAASLFKIANDMRLLg 299
Cdd:cd03302 189 QasfLDLFEGDHDKVealdelvtkkAGfkKVYPVTGQ---TYSRK------VDIDVLN--ALSSLGATAHKIATDIRLL- 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1219463173 300 sgprSGLGELILP--ENEPGSSIMPGKVNPTQAEALTMVCAHVMG 342
Cdd:cd03302 257 ----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
150-327 |
1.36e-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: 59.94 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 150 VAIGMVARDT----LLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEaclpDIYEL 225
Cdd:cd01598 107 LAYALMIKEArnevILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK----QIEIL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 226 AQGGTAVGT---------GLNTRKgFAEKVAGEIaaitGL---PFVTapnkfeALAAHDAMVMFSGALKTVAASLFKIAN 293
Cdd:cd01598 183 GKFNGAVGNfnahlvaypDVDWRK-FSEFFVTSL----GLtwnPYTT------QIEPHDYIAELFDALARINTILIDLCR 251
|
170 180 190
....*....|....*....|....*....|....
gi 1219463173 294 DMRLLGSgprSGLGELILPENEPGSSIMPGKVNP 327
Cdd:cd01598 252 DIWGYIS---LGYFKQKVKKGEVGSSTMPHKVNP 282
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
137-413 |
2.63e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 59.48 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 137 GQSSNDTFPTAMHvaigMVARDTLLPGLRKLHD---ALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIA 213
Cdd:PRK02186 513 ARSRNDINATTTK----LHLREATSRAFDALWRlrrALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETH 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 214 RVEACLPDIYELAQG-GTAVGTGLNTRKGFAEKVAGeiaaitglpFVT-APNKFEALAAHDAMVMFSGALKTVAASLFKI 291
Cdd:PRK02186 589 ALFALFEHIDVCPLGaGAGGGTTFPIDPEFVARLLG---------FEQpAPNSLDAVASRDGVLHFLSAMAAISTVLSRL 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 292 ANDMRLLGSgprSGLGELILPEN-EPGSSIMPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGHF--ELNVYNPMMSyN 368
Cdd:PRK02186 660 AQDLQLWTT---REFALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFsnSFEAGSPMNG-P 735
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1219463173 369 VLQSMQLLGDAAgSFTDNMVVGTQANVARIDKLMKESLMLVTALA 413
Cdd:PRK02186 736 IAQACAAIEDAA-AVLVLLIDGLEADQARMRAHLEDGGVSATAVA 779
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
73-343 |
5.49e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 73 IDQAAQEVIDGKFddnfplvVWQTGSgTQSNMNaNEvisnRAIEIMGGEMGSKtpVHpndhcnMGQSSNDTFPTAMHVAI 152
Cdd:PLN02646 77 LDEIEKEIEAGKF-------EWRPDR-EDVHMN-NE----ARLTELIGEPAKK--LH------TARSRNDQVATDTRLWC 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 153 gMVARDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEACLPDIYELAQGGTAV 232
Cdd:PLN02646 136 -RDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 233 -GTGLNTRKGFaekvageIAAITGLPFVTaPNKFEALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSGPrsgLGELIL 311
Cdd:PLN02646 215 aGTGLPIDRFM-------TAKDLGFTAPM-RNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---FGFVTP 283
|
250 260 270
....*....|....*....|....*....|...
gi 1219463173 312 PEN-EPGSSIMPGKVNPTQAEALTMVCAHVMGN 343
Cdd:PLN02646 284 SDAvSTGSSIMPQKKNPDPMELVRGKSARVIGD 316
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
132-333 |
5.38e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 51.59 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 132 DHCNMGQSSNDTFPTAMHVAIGMVArDTLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKG 211
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRLKAAS-EILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 212 IARVEACLPDIYELAQGGtAVGTgLNTRKGFAEKVAGEIAAITGLPfvTAPnkfEALAAHDAMVMFSGALKTVAASLFKI 291
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLGKF 251
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1219463173 292 ANDMRLLgsgprSGLGELILPENEPGSSIMPGKVNPTQAEAL 333
Cdd:PRK05975 252 GQDIALM-----AQAGDEISLSGGGGSSAMPHKQNPVAAETL 288
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
160-331 |
2.01e-06 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 50.12 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 160 LLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVEAClpDIYELAQGgtAVGtglNTR 239
Cdd:PLN02848 146 VLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEV--KIKGKFAG--AVG---NYN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 240 KGFA-------EKVAGEIAAITGL---PFVTapnkfeALAAHDAMVMFSGALKTVAASLFKIANDMRLLGSgprSGLGEL 309
Cdd:PLN02848 219 AHMSaypevdwPAVAEEFVTSLGLtfnPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRDIWSYIS---LGYFKQ 289
|
170 180
....*....|....*....|..
gi 1219463173 310 ILPENEPGSSIMPGKVNPTQAE 331
Cdd:PLN02848 290 ITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
137-331 |
2.30e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 46.68 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 137 GQSSNDtfptamHVA--IGMVARD---TLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKG 211
Cdd:PRK00855 108 GRSRND------QVAtdLRLYLRDeidEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 212 IARVEACLPDIYELAQGGTA-VGTGLNTRKgfaEKVAGEiaaitgLPF--VTApNKFEALAAHDAMVMFSGALKTVAASL 288
Cdd:PRK00855 182 LERLRDARKRVNRSPLGSAAlAGTTFPIDR---ERTAEL------LGFdgVTE-NSLDAVSDRDFALEFLSAASLLMVHL 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1219463173 289 FKIANDMRLLGSgPRSGLGELilpeneP-----GSSIMPGKVNPTQAE 331
Cdd:PRK00855 252 SRLAEELILWSS-QEFGFVEL------PdafstGSSIMPQKKNPDVAE 292
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-355 |
3.84e-04 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 41.55 E-value: 3.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219463173 280 ALKTVAASLFKIANDMRLLgSGPRSGLGELILPENEPGSSIMPGKVNPTQAEALTMVCAHVMGNDAAVGFAGSQGH 355
Cdd:PRK08937 22 VLALIATSLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWH 96
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
137-347 |
6.51e-04 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 42.08 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 137 GQSSNDTFPTAMHVAIGMVARDtLLPGLRKLHDALAAKSDEFKDIIKIGRTHTQDATPLTLGQEFGGYAHQVAKGIARVE 216
Cdd:PRK12308 106 GRSRNDQVATDLKLWCRQQGQQ-LLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219463173 217 ACLP--DIYELAQGGTAvGTGLNTRKgfaEKVAgeiaaiTGLPFVTAP-NKFEALAAHDAMVMFSGALKTVAASLFKIAN 293
Cdd:PRK12308 185 DALTrlDTCPLGSGALA-GTAYPIDR---EALA------HNLGFRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAE 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1219463173 294 DMRLLGSGpRSGLGEliLPEN-EPGSSIMPGKVNPTQAEALTMVCAHVMGNDAAV 347
Cdd:PRK12308 255 DLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALELIRGKTGRVYGALAGM 306
|
|
| |
