|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
46-505 |
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 226823367 46 SFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGatERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEV 124
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 125 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVL 204
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 205 LPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRI 284
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 285 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 364
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 365 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINK 444
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226823367 445 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 505
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
46-507 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 921.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 46 SFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGatERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEV 124
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 125 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVL 204
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 205 LPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRI 284
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 285 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 364
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 365 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINK 444
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823367 445 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 507
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
48-503 |
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: 903.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 48 RVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGatERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAE 126
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 127 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLP 206
Cdd:cd01362 79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 207 GLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGF 286
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 287 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 366
Cdd:cd01362 239 AEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 367 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLM 446
Cdd:cd01362 319 GKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 226823367 447 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 503
Cdd:cd01362 399 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
54-506 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 840.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 54 FGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAEGKLNDH 132
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 133 FPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLH 212
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 213 DALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAA 292
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 293 KVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPT 372
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 373 QCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLMNESLML 452
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 226823367 453 VTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 506
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
48-499 |
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: 824.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 48 RVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGatERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAE 126
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 127 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGsKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLP 206
Cdd:cd01596 79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 207 GLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGF 286
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 287 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 366
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 367 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLM 446
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 226823367 447 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVK 499
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
47-505 |
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: 812.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 47 FRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGgaTERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVA 125
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 126 EGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLL 205
Cdd:TIGR00979 79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 206 PGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIG 285
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 286 FAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIM 365
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 366 PGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKL 445
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 446 MNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 505
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
48-506 |
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 226823367 48 RVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGatERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAE 126
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 127 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLP 206
Cdd:PRK12425 81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 207 GLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGF 286
Cdd:PRK12425 161 AIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 287 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 366
Cdd:PRK12425 241 AEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 367 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLM 446
Cdd:PRK12425 321 GKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 447 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 506
Cdd:PRK12425 401 ERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
48-507 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 595.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 48 RVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAE 126
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 127 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAaVEVHKVLLP 206
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 207 GLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGF 286
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 287 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 366
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 367 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLM 446
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226823367 447 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 507
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
45-507 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 568.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 45 NSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADE 123
Cdd:PRK12273 3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 124 VAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAaVEVHKV 203
Cdd:PRK12273 83 ILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSLRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 204 LLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTR 283
Cdd:PRK12273 162 LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 284 IGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSS 363
Cdd:PRK12273 242 PGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 364 IMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERIN 443
Cdd:PRK12273 322 IMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226823367 444 KLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 507
Cdd:PRK12273 402 EYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
48-496 |
0e+00 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 562.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 48 RVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGatERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAE 126
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 127 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAaVEVHKVLLP 206
Cdd:cd01357 79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLAL-ILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 207 GLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGF 286
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 287 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 366
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 367 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLM 446
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 226823367 447 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDE 496
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
44-507 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 553.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 44 QNSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGAteRMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAAD 122
Cdd:PRK13353 2 NKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 123 EVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHK 202
Cdd:PRK13353 80 EILAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 203 vLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNT 282
Cdd:PRK13353 160 -LLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 283 RIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGS 362
Cdd:PRK13353 239 DPEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 363 SIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERI 442
Cdd:PRK13353 319 SIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERC 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226823367 443 NKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 507
Cdd:PRK13353 399 KEYVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
48-506 |
4.95e-147 |
|
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: 429.64 E-value: 4.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 48 RVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAE 126
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 127 -GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLL 205
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 206 PgLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIG 285
Cdd:TIGR00839 161 A-INQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 286 FAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIM 365
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 366 PGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKL 445
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226823367 446 MNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 506
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
55-386 |
1.13e-143 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 414.84 E-value: 1.13e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 55 GELKVPTDKYYGAQTVRSTMNFKIGGATERmpipviqAFGILKRAAAEVNQEYgldPKIASAIMKAADEVAE-GKLNDHF 133
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIK-------GLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 134 PLVVWQTGSGTQTNMNVNEVISnraiEMLGgelgskKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLHD 213
Cdd:pfam00206 71 PLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLID 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 214 ALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPR-IYELAAGGTAVGTGLNTRIGFAEKVAA 292
Cdd:pfam00206 141 ALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 293 KVAALTGLPfVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPrSGLGELILPENEPGSSIMPGKVNPT 372
Cdd:pfam00206 221 ELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPD 298
|
330
....*....|....
gi 226823367 373 QCEAMTMVAAQVMG 386
Cdd:pfam00206 299 QLELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
44-506 |
4.02e-143 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 419.79 E-value: 4.02e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 44 QNSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGAteRMPIPVIQAFGILKRAAAEVNQEYG-LDPKIASAIMKAAD 122
Cdd:PRK14515 8 KNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGY--KIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 123 EVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHK 202
Cdd:PRK14515 86 EILDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 203 vLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNT 282
Cdd:PRK14515 166 -LLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 283 RIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGS 362
Cdd:PRK14515 245 DPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 363 SIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERI 442
Cdd:PRK14515 325 SIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRL 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226823367 443 NKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 506
Cdd:PRK14515 405 KEYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
90-438 |
4.40e-122 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 360.28 E-value: 4.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 90 IQAFGILKRAAAEVNQEYG-LDPKIASAIMKAADEVAEGKLNDHFplvvWQTGSGTQTNMNVNEVISNRAIEMlggelgs 168
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 169 kkpvhpNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGY 248
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 249 VQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAkvaaLTGLpFVTAPNKFEALAAHDALVELSGAMNTA 328
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAE----LLGF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 329 ACSLMKIANDIRFLGSGprsGLGELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKP 407
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 226823367 408 MMIKNVLHSARLLGDASVSFTDNCvVGIQAN 438
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 ... |
148-428 |
3.86e-64 |
|
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: 207.85 E-value: 3.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 148 MNVNEVISNRAIEMLGGELGSKkpvhpndHVNKSQSSNDtFPTAMHIAAAVEVHKVLLPGLQKLHDALSAKSKEFAQVIK 227
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 228 IGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAmpriyelaaggtavgtglntrigfaekvaakvaaltglpfvtapn 307
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 308 kfealaahdALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPeNEPGSSIMPGKVNPTQCEAMTMVAAQVMGN 387
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 226823367 388 HVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFT 428
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
452-503 |
6.47e-28 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 105.48 E-value: 6.47e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226823367 452 LVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 503
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
199-505 |
2.84e-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: 110.94 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 199 EVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGtAVGT 278
Cdd:COG0015 113 EALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 279 GLNtrigfaekvaakvaaltglpFVTAPNKFEALAA----------------HDALVELSGAMNTAACSLMKIANDIRFL 342
Cdd:COG0015 192 YAA--------------------HGEAWPEVEERVAeklglkpnpvttqiepRDRHAELFSALALIAGSLEKIARDIRLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 343 GsgpRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGN--HVAVTV------GGSNGHFELNVFkPmmikn 412
Cdd:COG0015 252 Q---RTEVGEVeePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaaALLEALaswherDLSDSSVERNIL-P----- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 413 vlHSARLLGDASVSFTdNCVVGIQANTERINKLMNESLMLV------TALNPH-IG----YDKAAKIAKTAHKNGSTLKE 481
Cdd:COG0015 323 --DAFLLLDGALERLL-KLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRE 399
|
330 340
....*....|....*....|....*....
gi 226823367 482 tAIE-----LGYLTAEQFDEWVKPKDMLG 505
Cdd:COG0015 400 -LLAadpeiPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
198-473 |
6.61e-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: 106.05 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 198 VEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGtAVG 277
Cdd:cd01595 102 RDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 278 TGLNtrigFAEKVAAKVAALT---GLPFVTAPNKFEAlaaHDALVELSGAMNTAACSLMKIANDIRFLGsgpRSGLGELI 354
Cdd:cd01595 181 THAS----LGPKGPEVEERVAeklGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 355 LP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvavtvggsnghfelnvFKPMMIKNVL-------HSA--RLLG-- 421
Cdd:cd01595 251 EPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL-----------------AAPALENLVQwherdlsDSSveRNILpd 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226823367 422 -----DASVSFTDNCVVGIQANTERINKLMNESLMLV------TALNPH-IGYDKAAKIAKTAH 473
Cdd:cd01595 314 aflllDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
199-505 |
5.30e-22 |
|
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: 98.47 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 199 EVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGtAVGT 278
Cdd:cd01597 113 DALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 279 -------GLNTRIGFaekvaakvAALTGLPFVTAPnkfeALAAHDALVELSGAMNTAACSLMKIANDIRFLGsgpRSGLG 351
Cdd:cd01597 192 laslgdqGLAVQEAL--------AAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 352 ELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGnHVAVTV---------GGSNGHFELNVFKPMMIknvlhsarlL 420
Cdd:cd01597 257 EVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLdamvqeherDAGAWHAEWIALPEIFL---------L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 421 GDASVSFTDNCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKA----AKIAKTAHKNGSTLKETAIE--- 485
Cdd:cd01597 327 ASGALEQAEFLLSGLEVNEDRMRAnldltgglILSEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpe 404
|
330 340
....*....|....*....|.
gi 226823367 486 -LGYLTAEQFDEWVKPKDMLG 505
Cdd:cd01597 405 vAAYLSDEELDALLDPANYLG 425
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
177-505 |
6.07e-21 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 95.11 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 177 HVNKSQSSNDTFPTAMHIAAaVEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAM 256
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLL-RDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 257 VRIKAAMPRIYELAAGGtAVGTGLNTRIGFAEKVAAKVAALtGLPFVTAPNKFEAlaaHDALVELSGAMNTAACSLMKIA 336
Cdd:TIGR00928 169 ERLLQAKERIKVGGISG-AVGTHAAAYPLVEEVEERVTEFL-GLKPVPISTQIEP---RDRHAELLDALALLATTLEKFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 337 NDIRFLgsgPRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAaqVMGNHVAVTVGGSNGH-FELNVFKPMMIKNV 413
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVeePFGKGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLwHERDLTDSSVERVI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 414 LHSARLLGDASVSFTDNCVVGIQANTERINKLMNESLMLVTALNPHI-------GYDKAAKIAK-----TAHKNGSTLKE 481
Cdd:TIGR00928 319 LPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRelamgAAEVDEPDLLE 398
|
330 340
....*....|....*....|....*...
gi 226823367 482 TAIELG----YLTAEQFDEWVKPKDMLG 505
Cdd:TIGR00928 399 FLLEDEritkYLKEEELAELLDPETYIG 426
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
112-387 |
6.84e-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: 76.62 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 112 KIASAIMKAADEVAEGKLNDHFPLvvwqtgsgtqtnMNVNEVISNRAIEMLGGELGSKkpvhpndhVNKSQSSNDTFPTA 191
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGK--------LHTGRSRNDQVATD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 192 MHIAAAVEVhKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAA 271
Cdd:TIGR00838 115 LRLYLRDHV-LELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 272 GGTAV-GTGLntrigfaEKVAAKVAALTGLPFVTApNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPrsgL 350
Cdd:TIGR00838 194 GSGALaGTGF-------PIDREYLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---F 262
|
250 260 270
....*....|....*....|....*....|....*...
gi 226823367 351 GELILP-ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGN 387
Cdd:TIGR00838 263 GFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
184-381 |
4.01e-14 |
|
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: 74.13 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 184 SNDTFPTA--MHIAAAVevhKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKA 261
Cdd:cd01360 91 SSDVVDTAlaLQLREAL---DIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 262 AMPRIYELAAGGtAVGTGLNtrIGFAEKVAAKVAAltGLPFVTAPNKfeaLAAHDALVELSGAMNTAACSLMKIANDIRF 341
Cdd:cd01360 168 ARERILVGKISG-AVGTYAN--LGPEVEERVAEKL--GLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRH 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 226823367 342 LgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVA 381
Cdd:cd01360 240 L---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
203-386 |
4.78e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 64.65 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 203 VLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGtAVGTGLNT 282
Cdd:PRK09053 126 LLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGTLASL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 283 RIGFAEKVAAKVAALtGLPFVTAPNKfealAAHDALVELSGAMNTAACSLMKIANDIRFLgsgPRSGLGELILP--ENEP 360
Cdd:PRK09053 205 GEQALPVAQALAAEL-QLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDVSLL---MQTEVGEVFEPaaAGKG 276
|
170 180
....*....|....*....|....*.
gi 226823367 361 GSSIMPGKVNPTQCEAMTMVAAQVMG 386
Cdd:PRK09053 277 GSSTMPHKRNPVGCAAVLTAATRAPG 302
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
191-371 |
4.89e-10 |
|
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: 61.48 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 191 AMHIAAAVevHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVqqvqYAMVRIKAAMPRIYELA 270
Cdd:cd01598 110 ALMIKEAR--NEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFV----YRLERQYKQLKQIEILG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 271 AGGTAVGT------------------GLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAMNTAACSL 332
Cdd:cd01598 184 KFNGAVGNfnahlvaypdvdwrkfseFFVTSLG-----------LTWNPYTT------QIEPHDYIAELFDALARINTIL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 226823367 333 MKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 371
Cdd:cd01598 247 IDLCRDIwgyislGYFKQKVKKG---------EVGSSTMPHKVNP 282
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
191-371 |
2.36e-09 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 59.38 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 191 AMHIAAAVEvhKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAmpriyELA 270
Cdd:PRK09285 132 ALMLKEARE--EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EIL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 271 A--GGtAVGTgLN-------------------TRIGfaekvaakvaaLTGLPFVTA--PnkfealaaHDALVELSGAMNT 327
Cdd:PRK09285 205 GkiNG-AVGN-YNahlaaypevdwhafsrefvESLG-----------LTWNPYTTQieP--------HDYIAELFDAVAR 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 226823367 328 AACSLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 371
Cdd:PRK09285 264 FNTILIDLDRDVwgyislGYFKQKTKAG---------EIGSSTMPHKVNP 304
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
203-386 |
3.03e-09 |
|
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: 58.87 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 203 VLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTaVGTG--- 279
Cdd:cd03302 114 LILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQasf 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 280 -------------LNTRI----GFaekvaAKVAALTGLpfvTAPNKFEALAAhDALVELsGAmntaacSLMKIANDIRFL 342
Cdd:cd03302 193 ldlfegdhdkveaLDELVtkkaGF-----KKVYPVTGQ---TYSRKVDIDVL-NALSSL-GA------TAHKIATDIRLL 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 226823367 343 gsgprSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMG 386
Cdd:cd03302 257 -----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
114-393 |
6.65e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 114 ASAIMKAADEVAEGKLNDHFplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKkpvhpndhVNKSQSSNDTFPT--A 191
Cdd:PLN02646 70 RDSILDGLDEIEKEIEAGKF---EWRPD-----REDVHMNNEARLTELIG-EPAKK--------LHTARSRNDQVATdtR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 192 MHIAAAVevhKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAA 271
Cdd:PLN02646 133 LWCRDAI---DVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 272 GGTAV-GTGLntriGFAEKVAAKVAALTGLpfvtAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPrsgL 350
Cdd:PLN02646 210 GSCALaGTGL----PIDRFMTAKDLGFTAP----MRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---F 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 226823367 351 GELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 393
Cdd:PLN02646 279 GFVTPSDAvSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLA 322
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
94-456 |
4.13e-08 |
|
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: 55.63 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 94 GILKRAAAEvnqeygldpKIASAIMKAADEVAEGKLndhfplvVWQTGSGtqtnmNVNEVISNRAIEMLGgELGSKkpVH 173
Cdd:cd01359 27 GILTEEEAA---------KILAGLAKIRAEIEAGAF-------ELDPEDE-----DIHMAIERRLIERIG-DVGGK--LH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 174 pndhvnKSQSSNDTFPTAMHIAAAVEVhKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQ 253
Cdd:cd01359 83 ------TGRSRNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 254 YAMVRIKAAMPRIYELAAGGTA-VGTGLN-------TRIGFAEKvaakvaaltglpfvtAPNKFEALAAHDALVELSGAM 325
Cdd:cd01359 156 RDLERLADAYKRVNVSPLGAGAlAGTTFPidrertaELLGFDGP---------------TENSLDAVSDRDFVLEFLSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 326 NTAACSLMKIANDIRFLGSGPRsGLGELilpeneP-----GSSIMPGKVNPTQCEAMTMVAAQVMGNHVAV--TVGG--S 396
Cdd:cd01359 221 ALLMVHLSRLAEDLILWSTQEF-GFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLltTLKGlpL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823367 397 NGHFELNVFKPMM---IKNVLHSARLLGDasvsftdnCVVGIQANTERINKLMNESLMLVTAL 456
Cdd:cd01359 294 AYNKDLQEDKEPLfdaVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
200-375 |
3.18e-07 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 52.82 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 200 VHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGY-----VQQVQYAMVRIKAAMpriyelaAGGT 274
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFayrlsRQRKQLSEVKIKGKF-------AGAV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 275 ----------------AVGTGLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAMNTAACSLMKIAND 338
Cdd:PLN02848 215 gnynahmsaypevdwpAVAEEFVTSLG-----------LTFNPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRD 277
|
170 180 190
....*....|....*....|....*....|....*..
gi 226823367 339 IRFLGSgprSGLGELILPENEPGSSIMPGKVNPTQCE 375
Cdd:PLN02848 278 IWSYIS---LGYFKQITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
164-375 |
5.11e-07 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 52.48 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 164 GELGSKkpvhpndhVNKSQSSNDTFPTAMHIAAAVEVHKVLLpGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQ 243
Cdd:PRK12308 97 GDLGKK--------LHTGRSRNDQVATDLKLWCRQQGQQLLL-ALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 244 EFSGYVQQVQYAMVRIKAAMPRIYELAAG-GTAVGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAAH 315
Cdd:PRK12308 168 WCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTAypidreaLAHNLGFRRATR---------------NSLDSVSDR 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226823367 316 DALVELsgaMNTAACSLM---KIANDIRFLGSGpRSGLGEliLPEN-EPGSSIMPGKVNPTQCE 375
Cdd:PRK12308 233 DHVMEL---MSVASISMLhlsRLAEDLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALE 290
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
331-505 |
5.29e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 47.33 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 331 SLMKIANDIRFLgSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvAVTVGGSNGH-FELNVFKPMM 409
Cdd:PRK08937 29 SLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY--LVTALENVPLwHERDLSHSSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 410 IKNVLHSARLLGDASVSFTDNCVVGIQANTERINK--------LMNESLMLvTALNPHIG----YDKAAKIAKTAHKNGS 477
Cdd:PRK08937 106 ERIALPDAFLALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|..
gi 226823367 478 TLKETAIE----LGYLTAEQFDEWVKPKDMLG 505
Cdd:PRK08937 185 DLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
94-371 |
8.57e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 45.14 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 94 GILKRAAAEvnqeygldpKIASAIMKAADEVAEGKLndhfplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKkpVH 173
Cdd:PRK00855 51 GILSEEEAE---------KILAGLDEILEEIEAGKF-------EFSPE-----LEDIHMAIEARLTERIG-DVGGK--LH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 174 P----NDHVnksqssndtfPTAMHIAAAVEVhKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYV 249
Cdd:PRK00855 107 TgrsrNDQV----------ATDLRLYLRDEI-DEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 250 QQVQYAMVRIKAAMPRIYELAAGGTA-VGTGLNT-------RIGFAEkvaakvaaltglpfVTApNKFEALAAHDALVEL 321
Cdd:PRK00855 176 EMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIdrertaeLLGFDG--------------VTE-NSLDAVSDRDFALEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 226823367 322 SGAMNTAACSLMKIANDIrFLGSGPRSGLGELilpeneP-----GSSIMPGKVNP 371
Cdd:PRK00855 241 LSAASLLMVHLSRLAEEL-ILWSSQEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
164-393 |
6.45e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 42.28 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 164 GELGSKKpvhpndHVNKSQssNDTFPTAMHIAAAVEVHkVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQ 243
Cdd:PRK04833 97 GDLGKKL------HTGRSR--NDQVATDLKLWCKDQVA-ELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 244 EFSGYVQQVQYAMVRIKAAMPR--IYELAAGGTAvGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAA 314
Cdd:PRK04833 168 WCLAYVEMLARDESRLQDALKRldVSPLGSGALA-GTAyeidreqLAGWLGFASATR---------------NSLDSVSD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 315 HDALVELsgaMNTAACSLM---KIANDIRFLGSGpRSGLGELIlPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAV 391
Cdd:PRK04833 232 RDHVLEL---LSDASISMVhlsRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGM 306
|
..
gi 226823367 392 TV 393
Cdd:PRK04833 307 LM 308
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
176-390 |
2.13e-03 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 40.42 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 176 DHVNKSQSSNDTFPT--AMHIAAAVEVhkvLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQ 253
Cdd:PRK05975 100 AHVHFGATSQDVIDTslMLRLKAASEI---LAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 254 YAMVRIKAAMPRIYELAAGGtAVGTgLNTRIGFAEKVAAKVAALTGLPfvTAPnkfEALAAHDALVELSGAMNTAACSLM 333
Cdd:PRK05975 177 RHRDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLG 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226823367 334 KIANDIRFLgsgprSGLGELILPENEPGSSIMPGKVNPTQCEAMTMV----AAQVMGNHVA 390
Cdd:PRK05975 250 KFGQDIALM-----AQAGDEISLSGGGGSSAMPHKQNPVAAETLVTLarfnATQVSGLHQA 305
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
234-386 |
8.17e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 39.06 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 234 QDAVPLTLGQefsgYVQQVQYAMVRIKAAMPRIYE------LAAGGTAvGTGLNTRIGFAEKVaakvaaltgLPFVT-AP 306
Cdd:PRK02186 565 QPALPGSLGH----YLLAVDGALARETHALFALFEhidvcpLGAGAGG-GTTFPIDPEFVARL---------LGFEQpAP 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823367 307 NKFEALAAHDALVELSGAMNTAACSLMKIANDIRfLGSGPRSGLgeLILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVM 385
Cdd:PRK02186 631 NSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQ-LWTTREFAL--VSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVA 707
|
.
gi 226823367 386 G 386
Cdd:PRK02186 708 G 708
|
|
| |
