|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
57-515 |
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: 928.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 57 EFRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEkeRLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEV 135
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGE--RMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 136 IDGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHL 215
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 216 LPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFE 295
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 296 GFDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSI 375
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 376 MPGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIAR 455
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 456 HLRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMI 515
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
57-519 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 920.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 57 EFRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEkeRLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEV 135
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGE--RMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 136 IDGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHL 215
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 216 LPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFE 295
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 296 GFDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSI 375
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 376 MPGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIAR 455
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295442792 456 HLRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMISAKK 519
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
59-514 |
0e+00 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 902.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEkeRLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGE--RMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLP 217
Cdd:cd01362 79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 218 AMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGF 297
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 298 DVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMP 377
Cdd:cd01362 239 AEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 378 GKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHL 457
Cdd:cd01362 319 GKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 295442792 458 RDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELM 514
Cdd:cd01362 399 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
65-519 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 828.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 65 FGPIQVPAEKYWGAQTQRSLQNFRIGGEKERLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVIDGRLDDN 143
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 144 FPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLPAMKHLH 223
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 224 RALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGFDVKVAE 303
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 304 KVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMPGKVNPT 383
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 384 QCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHLRDSLML 463
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 295442792 464 VTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMISAKK 519
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPSD 456
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
59-510 |
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: 823.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEkeRLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGE--RMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGsKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLP 217
Cdd:cd01596 79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 218 AMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGF 297
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 298 DVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMP 377
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 378 GKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHL 457
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 295442792 458 RDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVR 510
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
58-516 |
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 295442792 58 FRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGgeKERLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVI 136
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 137 DGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLL 216
Cdd:TIGR00979 79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 217 PAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEG 296
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 297 FDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIM 376
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 377 PGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARH 456
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 457 LRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMIS 516
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
59-517 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 610.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGgeKERLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIG--KERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLP 217
Cdd:PRK12425 81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 218 AMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGF 297
Cdd:PRK12425 161 AIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 298 DVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMP 377
Cdd:PRK12425 241 AEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 378 GKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHL 457
Cdd:PRK12425 321 GKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 458 RDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMISA 517
Cdd:PRK12425 401 ERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
59-515 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 604.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEKERLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHThLLP 217
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 218 AMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGF 297
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 298 DVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMP 377
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 378 GKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHL 457
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 295442792 458 RDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMI 515
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMT 457
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
57-516 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 573.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 57 EFRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEKERLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEV 135
Cdd:PRK12273 4 NTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 136 IDGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIAsVLQIHTHL 215
Cdd:PRK12273 84 LAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIA-LLLSLRKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 216 LPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFE 295
Cdd:PRK12273 163 LDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 296 GFDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSI 375
Cdd:PRK12273 243 GYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 376 MPGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIAR 455
Cdd:PRK12273 323 MPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCRE 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295442792 456 HLRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMIS 516
Cdd:PRK12273 403 YVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTH 463
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
59-507 |
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: 568.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEkeRLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGL--KIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIAsVLQIHTHLLP 217
Cdd:cd01357 79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLA-LILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 218 AMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGF 297
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 298 DVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMP 377
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 378 GKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHL 457
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 295442792 458 RDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDE 507
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
58-520 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 541.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 58 FRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEkeRLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVI 136
Cdd:PRK13353 5 MRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 137 DGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIAsVLQIHTHLL 216
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIA-ALNLLEGLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 217 PAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEG 296
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 297 FDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIM 376
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 377 PGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARH 456
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295442792 457 LRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELM----ISAKKV 520
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMthpgIAGATL 469
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
59-516 |
4.16e-141 |
|
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: 415.00 E-value: 4.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEKERLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 -GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIAsVLQIHTHLL 216
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIA-VYSSLIKLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 217 PAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEG 296
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 297 FDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIM 376
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 377 PGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARH 456
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 457 LRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMIS 516
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMH 459
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
66-397 |
1.10e-138 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 402.90 E-value: 1.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 66 GPIQVPAEKYWGAQTQRSLQNFRIGGEKERlplplvrAFGVLKRAAASVNREFgldPKLADAIEQAAQEVI-DGRLDDNF 144
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIK-------GLAALKKAAAKANVIL---KEEAAAIIKALDEVAeEGKLDDQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 145 PLVVFQTGSGTQSNMNSNEVIAnraiEILGgtlgskKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLPAMKHLHR 224
Cdd:pfam00206 71 PLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLID 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 225 ALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPR-LCLLAQGGTAVGTGLNTFEGFDVKVAE 303
Cdd:pfam00206 141 ALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 304 KVSKLTNIEFKtAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPrCGLGELILPANEPGSSIMPGKVNPT 383
Cdd:pfam00206 221 ELGFFTGLPVK-APNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPD 298
|
330
....*....|....
gi 295442792 384 QCEALTMVCAQVMG 397
Cdd:pfam00206 299 QLELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
59-514 |
1.51e-134 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 398.60 E-value: 1.51e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 59 RQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEKerLPLPLVRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVID 137
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYK--IHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 138 GRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASvLQIHTHLLP 217
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALEGLLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 218 AMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGF 297
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 298 DVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMP 377
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 378 GKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHL 457
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 295442792 458 RDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELM 514
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEM 465
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
101-449 |
1.41e-125 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 369.91 E-value: 1.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 101 VRAFGVLKRAAASVNREFG-LDPKLADAIEQAAQEVIDGRLDDnfplVVFQTGSGTQSNMNSNEVIANRAIEILGGtlgs 179
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGIAAD----QVEQEGSGTHDVMAVEEVLAERAGELNGG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 180 kkpvhpndHVNMSQSSNDTFPTvMHIASVLQIHTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGY 259
Cdd:cd01334 73 --------YVHTGRSSNDIVDT-ALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 260 VTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGFDVKVAEKVSkltniEFKTAPNKFEALAAHDAIVEMSGALNVI 339
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLG-----FFGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 340 ACSLMKIANDIRQLGSGprcGLGELILPAN-EPGSSIMPGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKP 418
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 295442792 419 LLAKNILSSIRLLGDACESFTDHCvVGIEPN 449
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
159-439 |
9.33e-63 |
|
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: 204.76 E-value: 9.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 159 MNSNEVIANRAIEILGGtlgskkpVHPNDHVNMSQSSNDtFPTVMHIASVLQIHTHLLPAMKHLHRALKGKEEEFKNIIK 238
Cdd:cd01594 14 ALVEEVLAGRAGELAGG-------LHGSALVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 239 IGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNAlprlcllaqggtavgtglntfegfdvkvaekvskltniefktapn 318
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 319 kfealaahdAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPaNEPGSSIMPGKVNPTQCEALTMVCAQVMGN 398
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 295442792 399 HATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFT 439
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
192-464 |
6.39e-27 |
|
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: 112.21 E-value: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 192 SQSSNDTfptvmhiASVLQI---HTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIE 268
Cdd:cd01595 89 SQDINDT-------ALALQLrdaLDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 269 RINNALPRLCLLAQGGtAVGTGLNtFEGFDVKVAEKVSKLTNIEFKTAPNKFEAlaaHDAIVEMSGALNVIACSLMKIAN 348
Cdd:cd01595 162 RLEEARERVLVGGISG-AVGTHAS-LGPKGPEVEERVAEKLGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 349 DIRQLGsgpRCGLGELILP--ANEPGSSIMPGKVNPTQCEALT----MVCAQVMGNHATITV-----AGASgHCElnvfk 417
Cdd:cd01595 237 DIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEglarLVRALAAPALENLVQwherdLSDS-SVE----- 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 295442792 418 pllaKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHLRDSLMLV 464
Cdd:cd01595 308 ----RNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLI 350
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
196-466 |
6.03e-26 |
|
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: 110.17 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 196 NDTfptvmhiASVLQI---HTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINN 272
Cdd:COG0015 103 NDT-------ALALQLreaLELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 273 ALPRLCLLAQGGtAVGTgLNTFEGFDVKVAEKVSKLTNIefktapnKFEALA----AHDAIVEMSGALNVIACSLMKIAN 348
Cdd:COG0015 176 ARERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEKLGL-------KPNPVTtqiePRDRHAELFSALALIAGSLEKIAR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 349 DIRQLGsgpRCGLGEL--ILPANEPGSSIMPGKVNPTQCE----ALTMVCAQVMgnhatitvagasghcelnvfkPLLAK 422
Cdd:COG0015 247 DIRLLQ---RTEVGEVeePFAKGQVGSSAMPHKRNPIDSEniegLARLARALAA---------------------ALLEA 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295442792 423 NIL--------SSIR--LLGDAC-------ESFTDhcVV-GIEPNYEGIARHLRDSLMLVTA 466
Cdd:COG0015 303 LASwherdlsdSSVErnILPDAFllldgalERLLK--LLeGLVVNPERMRANLDLTGGLVLS 362
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
463-514 |
8.10e-22 |
|
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: 88.53 E-value: 8.10e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 295442792 463 LVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELM 514
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
188-464 |
1.20e-19 |
|
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: 91.25 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 188 HVNMSQSSNDTFPTVMhiasVLQI---HTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVG 264
Cdd:TIGR00928 90 FIHFGATSNDIVDTAL----ALLLrdaLEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 265 YGIERINNALPRLCLLAQGGtAVGTGLNTFEGFDvKVAEKVSKLTNIEFKTAPNKFEAlaaHDAIVEMSGALNVIACSLM 344
Cdd:TIGR00928 166 RQLERLLQAKERIKVGGISG-AVGTHAAAYPLVE-EVEERVTEFLGLKPVPISTQIEP---RDRHAELLDALALLATTLE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 345 KIANDIRQLgsgPRCGLGELILPA--NEPGSSIMPGKVNPTQCEaltmvcaQVMGNhatitvAGASGhcelNVFKPLLAK 422
Cdd:TIGR00928 241 KFAVDIRLL---QRTEHFEVEEPFgkGQVGSSAMPHKRNPIDFE-------NVCGL------ARVIR----GYASPALEN 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 295442792 423 NIL--------SSIR--LLGDAC-------ESFTDhCVVGIEPNYEGIARHLRDSLMLV 464
Cdd:TIGR00928 301 APLwherdltdSSVErvILPDAFiladimlKTTLK-VVKKLVVNPENILRNLDLTLGLI 358
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
202-512 |
9.59e-19 |
|
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: 88.45 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 202 VMHIASVLQI---HTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRlC 278
Cdd:cd01597 102 IIDTALVLQLrdaLDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPR-V 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 279 LLAQGGTAVGTgLNTFEGFDVKVAEKVSKLTNIEFKTAPnkfeALAAHDAIVEMSGALNVIACSLMKIANDIRQLGsgpR 358
Cdd:cd01597 181 LVVQFGGAAGT-LASLGDQGLAVQEALAAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---Q 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 359 CGLGELILP--ANEPGSSIMPGKVNPTQCEALTMVCAQVMGNHATITVAGA--------SGHCELNVFkPLLAknilssi 428
Cdd:cd01597 253 TEIGEVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVqeherdagAWHAEWIAL-PEIF------- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 429 RLLGDACESfTDHCVVGIEPNYEGIARHLRDS--LML----VTALNPHIG--------YDNCAKIAKTALKNKSTLKHEF 494
Cdd:cd01597 325 LLASGALEQ-AEFLLSGLEVNEDRMRANLDLTggLILseavMMALAPKLGrqeahdlvYEACMRAVEEGRPLREVLLEDP 403
|
330
....*....|....*...
gi 295442792 495 VTLGFGTPEQFDEWVRPE 512
Cdd:cd01597 404 EVAAYLSDEELDALLDPA 421
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
195-389 |
2.65e-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: 86.84 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 195 SNDtfptVMHIASVLQIHTH---LLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERIN 271
Cdd:cd01360 91 SSD----VVDTALALQLREAldiILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 272 NALPRLCLLAQGGtAVGTGLNtfegFDVKVAEKVSKLTNIEFKTAPNKfeaLAAHDAIVEMSGALNVIACSLMKIANDIR 351
Cdd:cd01360 167 EARERILVGKISG-AVGTYAN----LGPEVEERVAEKLGLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIR 238
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 295442792 352 QLgsgPRCGLGELILP--ANEPGSSIMPGKVNPTQCEALT 389
Cdd:cd01360 239 HL---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENIC 275
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
123-402 |
3.99e-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: 71.23 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 123 KLADAIEQAAQEVIDGRLDDNFPLvvfqtgsgtqsnMNSNEVIANRAIEILGGTLGSKkpvhpndhVNMSQSSNDTFPTV 202
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGK--------LHTGRSRNDQVATD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 203 MHIASVLQIhTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQ 282
Cdd:TIGR00838 115 LRLYLRDHV-LELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 283 GGTAV-GTGLntfeGFDvkvAEKVSKLTNIEFKTApNKFEALAAHDAIVEMSGALNVIACSLMKIANDIrQLGSGPRCGL 361
Cdd:TIGR00838 194 GSGALaGTGF----PID---REYLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDL-ILWSTGEFGF 264
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 295442792 362 GELilpANE--PGSSIMPGKVNPTQCEALTMVCAQVMGNHATI 402
Cdd:TIGR00838 265 VEL---PDEfsSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM 304
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
206-386 |
7.28e-12 |
|
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: 67.34 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 206 ASVLQIHTHLLPAMKHLHRA---LKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQ 282
Cdd:cd03302 103 TDLIQIRDALDLILPKLAAVidrLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 283 GGTaVGTG---LNTFEG-------FDVKVAEKV--SKLTNIEFKTAPNKFEalaahdaiVEMSGALNVIACSLMKIANDI 350
Cdd:cd03302 183 KGT-TGTQasfLDLFEGdhdkveaLDELVTKKAgfKKVYPVTGQTYSRKVD--------IDVLNALSSLGATAHKIATDI 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 295442792 351 RQLGsgprcGLGELILP--ANEPGSSIMPGKVNPTQCE 386
Cdd:cd03302 254 RLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSE 286
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
189-410 |
1.98e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 66.19 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 189 VNMSQSSNDtfptVMHIASVLQIHTH---LLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGY 265
Cdd:PRK09053 102 VHWGATSQD----IIDTGLVLQLRDAldlLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 266 GIERINNALPRLCLLaQGGTAVGTgLNTFEGFDVKVAEKVSKLTNIEFKTAPNKfealAAHDAIVEMSGALNVIACSLMK 345
Cdd:PRK09053 178 HRQRLAALRPRALVL-QFGGAAGT-LASLGEQALPVAQALAAELQLALPALPWH----TQRDRIAEFASALGLLAGTLGK 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295442792 346 IANDIRQLgsgPRCGLGELILPA--NEPGSSIMPGKVNPTQCEALTMVCAQVMGNHATITVAGASGH 410
Cdd:PRK09053 252 IARDVSLL---MQTEVGEVFEPAaaGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEH 315
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
211-382 |
8.35e-11 |
|
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: 63.79 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 211 IHTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVtqvgYGIERINNALPRLCLLAQGGTAVGTg 290
Cdd:cd01598 117 RNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFV----YRLERQYKQLKQIEILGKFNGAVGN- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 291 LN----TFEGFD-VKVAEKVSKLTNIEFKTAPNKFEalaAHDAIVEMSGAL---NVIacsLMKIANDIRQLGSgprCGLG 362
Cdd:cd01598 192 FNahlvAYPDVDwRKFSEFFVTSLGLTWNPYTTQIE---PHDYIAELFDALariNTI---LIDLCRDIWGYIS---LGYF 262
|
170 180
....*....|....*....|
gi 295442792 363 ELILPANEPGSSIMPGKVNP 382
Cdd:cd01598 263 KQKVKKGEVGSSTMPHKVNP 282
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
211-386 |
1.55e-09 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 60.14 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 211 IHTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSgyvtQVGYGIERINNALPRLCLLAQGGTAVG-- 288
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMA----NFAYRLSRQRKQLSEVKIKGKFAGAVGny 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 289 -TGLNTFEGFD-VKVAEKVSKLTNIEFKTAPNKFEalaAHDAIVEMSGALNVIACSLMKIANDIRQLGSgprCGLGELIL 366
Cdd:PLN02848 218 nAHMSAYPEVDwPAVAEEFVTSLGLTFNPYVTQIE---PHDYMAELFNAVSRFNNILIDFDRDIWSYIS---LGYFKQIT 291
|
170 180
....*....|....*....|
gi 295442792 367 PANEPGSSIMPGKVNPTQCE 386
Cdd:PLN02848 292 KAGEVGSSTMPHKVNPIDFE 311
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
194-467 |
2.02e-09 |
|
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: 59.48 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 194 SSNDTFPTVMHIA---SVLQIHTHLLpamkHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERI 270
Cdd:cd01359 86 SRNDQVATDLRLYlrdALLELLELLL----DLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 271 NNALPRLCLLAQGGTA-VGTGLNTfegfDvkvAEKVSKLtnIEFKT-APNKFEALAAHDAIVEMSGALNVIACSLMKIAN 348
Cdd:cd01359 162 ADAYKRVNVSPLGAGAlAGTTFPI----D---RERTAEL--LGFDGpTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 349 DIrQLGSGPRCGLGELilpaneP-----GSSIMPGKVNPTQCEALTMVCAQVMGNHATITVA-----GASGHCELNVFKP 418
Cdd:cd01359 233 DL-ILWSTQEFGFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTlkglpLAYNKDLQEDKEP 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 295442792 419 LLAknilsSIRLLGDACESFTDhCVVGIEPNYEGIARHLRDSLMLVTAL 467
Cdd:cd01359 306 LFD-----AVDTLIASLRLLTG-VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
215-382 |
1.29e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 57.07 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 215 LLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALprlcLLAQGGTAVGT---GL 291
Cdd:PRK09285 143 LLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVE----ILGKINGAVGNynaHL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 292 NTFEGFD-VKVAEK-VSKL--------TNIEfktaPnkfealaaHDAIVEMSGALNVIACSLMKIANDI---------RQ 352
Cdd:PRK09285 219 AAYPEVDwHAFSREfVESLgltwnpytTQIE----P--------HDYIAELFDAVARFNTILIDLDRDVwgyislgyfKQ 286
|
170 180 190
....*....|....*....|....*....|
gi 295442792 353 lgsgprcglgelILPANEPGSSIMPGKVNP 382
Cdd:PRK09285 287 ------------KTKAGEIGSSTMPHKVNP 304
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
219-404 |
3.45e-08 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 55.89 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 219 MKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRL--CLLAQGGTAvGTGLntfeG 296
Cdd:PLN02646 146 IKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVnfCPLGSCALA-GTGL----P 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 297 FDVKVAEKVSKLTNIefktAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPrcgLGELILP-ANEPGSSI 375
Cdd:PLN02646 221 IDRFMTAKDLGFTAP----MRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---FGFVTPSdAVSTGSSI 293
|
170 180
....*....|....*....|....*....
gi 295442792 376 MPGKVNPTQCEALTMVCAQVMGNHATITV 404
Cdd:PLN02646 294 MPQKKNPDPMELVRGKSARVIGDLVTVLA 322
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
214-397 |
4.26e-07 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 52.48 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 214 HLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRL--CLLAQGGTAvGTGL 291
Cdd:PRK12308 127 QLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLdtCPLGSGALA-GTAY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 292 NTfegfdvkvaEKVSKLTNIEFKTAP-NKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGpRCGLGELILPANE 370
Cdd:PRK12308 206 PI---------DREALAHNLGFRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSG-ESGFIELADTVTS 275
|
170 180
....*....|....*....|....*..
gi 295442792 371 pGSSIMPGKVNPTQCEALTMVCAQVMG 397
Cdd:PRK12308 276 -GSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
245-467 |
1.79e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 50.62 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 245 QDATPLSLGQEFSGYVTQVGYGIERINNALPRL--CLLAQGGTAvGTGLNTFEGFdvkvaekVSKLTNIEfKTAPNKFEA 322
Cdd:PRK02186 565 QPALPGSLGHYLLAVDGALARETHALFALFEHIdvCPLGAGAGG-GTTFPIDPEF-------VARLLGFE-QPAPNSLDA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 323 LAAHDAIVEMSGALNVIACSLMKIANDIrQLGSGPRCGLgeLILPAN-EPGSSIMPGKVNPTQCEALTMVCAQVMGnhAT 401
Cdd:PRK02186 636 VASRDGVLHFLSAMAAISTVLSRLAQDL-QLWTTREFAL--VSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAG--AL 710
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295442792 402 ITVAGASGHCEL-NVFKpllAKNILSSirLLGDACESFTDHCVV------GIEPNYEGIARHLRDSLMLVTAL 467
Cdd:PRK02186 711 ASASAALGKTPFsNSFE---AGSPMNG--PIAQACAAIEDAAAVlvllidGLEADQARMRAHLEDGGVSATAV 778
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
214-382 |
9.79e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 44.76 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 214 HLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTA-VGTGLN 292
Cdd:PRK00855 129 EIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAAlAGTTFP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 293 -----TFE--GFDvKVAEkvskltniefktapNKFEALAAHDAIVEMSGALNVIACSLMKIANDIrQLGSGPRCGLGELi 365
Cdd:PRK00855 209 idrerTAEllGFD-GVTE--------------NSLDAVSDRDFALEFLSAASLLMVHLSRLAEEL-ILWSSQEFGFVEL- 271
|
170 180
....*....|....*....|..
gi 295442792 366 lpaneP-----GSSIMPGKVNP 382
Cdd:PRK00855 272 -----PdafstGSSIMPQKKNP 288
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
225-388 |
2.04e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 43.50 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 225 ALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGtAVGTgLNTFEGFDVKVAEK 304
Cdd:PRK05975 137 RLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRAR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 305 VSKLTNIEfkTAPnkfEALAAHDAIVEMSGALNVIACSLMKIANDI---RQLGsgprcglGELILpANEPGSSIMPGKVN 381
Cdd:PRK05975 215 LAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLGKFGQDIalmAQAG-------DEISL-SGGGGSSAMPHKQN 281
|
....*..
gi 295442792 382 PTQCEAL 388
Cdd:PRK05975 282 PVAAETL 288
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
240-414 |
1.03e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 41.42 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 240 GRTHMQDATPLSLgQEFSGYVTQVGY-GIERINNALPRLCLLAQGgtaVGTGLNTFEGFDVKvaeKVSKLTNIEFKTAPN 318
Cdd:PRK06389 147 GYTHFRQAMPMTV-NTYINYIKSILYhHINNLDSFLMDLREMPYG---YGSGYGSPSSVKFN---QMSELLGMEKNIKNP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442792 319 KFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGprcglGELILPAN-EPGSSIMPGKVNPTQCEALTMVCAQvmg 397
Cdd:PRK06389 220 VYSSSLYIKTIENISYLISSLAVDLSRICQDIIIYYEN-----GIITIPDEfTTGSSLMPNKRNPDYLELFQGIAAE--- 291
|
170
....*....|....*..
gi 295442792 398 nhaTITVAGASGHCELN 414
Cdd:PRK06389 292 ---SISVLSFIAQSELN 305
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
327-398 |
1.20e-03 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 40.40 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295442792 327 DAIVEMsgALNVIACSLMKIANDIRqLGSGPRCGLGELILPANEPGSSIMPGKVNPTQCEALTMVCAQVMGN 398
Cdd:PRK08937 16 EDIAEI--VLALIATSLEKFANEIR-LLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY 84
|
|
| PRK02395 |
PRK02395 |
hypothetical protein; Provisional |
116-165 |
5.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235034 [Multi-domain] Cd Length: 279 Bit Score: 38.91 E-value: 5.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 295442792 116 REFGLDPKLADAIEQAAQEVI-DGRLDDNFPLVVFqtGSGTQSNMNSNEVI 165
Cdd:PRK02395 107 GPVGTHPAMADVIAARARSVTgDPDVGEDTALAVV--GHGTERNENSAKAI 155
|
|
| |
