|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-460 |
0e+00 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 930.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 1 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 79
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 80 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVL 159
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 160 LPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRI 239
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 240 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 319
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 320 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINK 399
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5D6B_A 400 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 460
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-462 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 929.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 1 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 79
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 80 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVL 159
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 160 LPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRI 239
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 240 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 319
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 320 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINK 399
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
5D6B_A 400 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 462
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
3-458 |
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: 914.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLP 161
Cdd:cd01362 79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 162 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 241
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 242 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 321
Cdd:cd01362 239 AEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 322 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 401
Cdd:cd01362 319 GKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
5D6B_A 402 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 458
Cdd:cd01362 399 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
9-461 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 853.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 9 FGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDH 87
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 88 FPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLH 167
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 168 DALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAA 247
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 248 KVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPT 327
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 328 QCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLML 407
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
5D6B_A 408 VTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 461
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
3-454 |
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: 836.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGsKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLP 161
Cdd:cd01596 79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 162 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 241
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 242 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 321
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 322 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 401
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
5D6B_A 402 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVK 454
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
2-460 |
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: 821.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 2 FRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGgvTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVA 80
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 81 EGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLL 160
Cdd:TIGR00979 79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 161 PGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIG 240
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 241 FAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIM 320
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 321 PGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKL 400
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 401 MNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 460
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
3-461 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 619.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLP 161
Cdd:PRK12425 81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 162 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 241
Cdd:PRK12425 161 AIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 242 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 321
Cdd:PRK12425 241 AEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 322 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 401
Cdd:PRK12425 321 GKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 402 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 461
Cdd:PRK12425 401 ERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
3-462 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 605.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLP 161
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 162 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 241
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 242 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 321
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 322 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 401
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5D6B_A 402 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 462
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-462 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 1 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 79
Cdd:PRK12273 4 NTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 80 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVL 159
Cdd:PRK12273 84 LAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSLRKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 160 LPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRI 239
Cdd:PRK12273 163 LDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 240 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 319
Cdd:PRK12273 243 GYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 320 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINK 399
Cdd:PRK12273 323 MPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCRE 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
5D6B_A 400 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 462
Cdd:PRK12273 403 YVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
3-451 |
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: 575.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLP 161
Cdd:cd01357 79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLAL-ILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 162 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 241
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 242 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 321
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 322 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 401
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
5D6B_A 402 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDE 451
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
1-462 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 561.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 1 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 79
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 80 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEvL 159
Cdd:PRK13353 82 LAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG-L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 160 LPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRI 239
Cdd:PRK13353 161 LAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 240 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 319
Cdd:PRK13353 241 EYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 320 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINK 399
Cdd:PRK13353 321 MPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
5D6B_A 400 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 462
Cdd:PRK13353 401 YVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
3-461 |
4.32e-151 |
|
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: 438.11 E-value: 4.32e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 -GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLL 160
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAV-YSSLIKLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 161 PGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIG 240
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 241 FAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIM 320
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 321 PGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKL 400
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5D6B_A 401 MNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 461
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
10-341 |
1.70e-147 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 422.93 E-value: 1.70e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 10 GELKVPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANAIMKAADEVAE-GKLNDHF 88
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 89 PLVVWQTGSGTQTNMNVNEVISnraiEMLGgelgskIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHD 168
Cdd:pfam00206 71 PLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLID 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 169 ALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPR-IYELAAGGTAVGTGLNTRIGFAEKVAA 247
Cdd:pfam00206 141 ALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 248 KVAALTGLPfVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrSGLGELILPENEPGSSIMPGKVNPT 327
Cdd:pfam00206 221 ELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPD 298
|
330
....*....|....
5D6B_A 328 QCEAMTMVAAQVMG 341
Cdd:pfam00206 299 QLELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-461 |
2.56e-145 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 423.64 E-value: 2.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 3 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 81
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGY--KIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 82 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLP 161
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALEGLLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 162 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 241
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 242 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 321
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 322 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 401
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 402 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 461
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-393 |
7.03e-124 |
|
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: 363.36 E-value: 7.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 45 IKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFplvvWQTGSGTQTNMNVNEVISNRAIEMlggelgs 123
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 124 kipvhpNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGY 203
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 204 VQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAkvaaLTGLpFVTAPNKFEALAAHDALVELSGAMNTT 283
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAE----LLGF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 284 ACSLMKIANDIRFLGSGprsGLGELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKP 362
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
5D6B_A 363 MMIKNVLHSARLLGDASVSFTENCvVGIQAN 393
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 ... |
103-383 |
1.06e-65 |
|
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: 210.93 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 103 MNVNEVISNRAIEMLGGELGSKipvhpndHVNKSQSSNDtFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIK 182
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 183 IGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyelaaggtavgtglntrigfaekvaakvaaltglpfvtapn 262
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 263 kfealaahdALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPeNEPGSSIMPGKVNPTQCEAMTMVAAQVMGN 342
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
5D6B_A 343 HVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFT 383
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
407-458 |
5.87e-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: 105.09 E-value: 5.87e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
5D6B_A 407 LVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 458
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
154-460 |
2.48e-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: 110.56 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 154 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 233
Cdd:COG0015 113 EALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 234 GLNtrigfaekvaakvaaltglpFVTAPNKFEALAA----------------HDALVELSGAMNTTACSLMKIANDIRFL 297
Cdd:COG0015 192 YAA--------------------HGEAWPEVEERVAeklglkpnpvttqiepRDRHAELFSALALIAGSLEKIARDIRLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 298 GsgpRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGN--HVAVTV------GGSNGHFELNVFkPMMIkn 367
Cdd:COG0015 252 Q---RTEVGEVeePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaaALLEALaswherDLSDSSVERNIL-PDAF-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 368 vlhsarLLGDASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IG----YDKAAKIAKTAHKNGSTLKE 436
Cdd:COG0015 326 ------LLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRE 399
|
330 340
....*....|....*....|....*....
5D6B_A 437 tAIE-----LGYLTAEQFDEWVKPKDMLG 460
Cdd:COG0015 400 -LLAadpeiPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
154-428 |
4.99e-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: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 154 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 233
Cdd:cd01595 103 DALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 234 GLNtrigFAEKVAAKVAALT---GLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLGELIL 310
Cdd:cd01595 182 HAS----LGPKGPEVEERVAeklGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 311 P--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvavtvggsnghfelnvFKPMMIKNVL-------HSA--RLLG--- 376
Cdd:cd01595 252 PfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL-----------------AAPALENLVQwherdlsDSSveRNILpda 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
5D6B_A 377 ----DASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IGYDKAAKIAKTAH 428
Cdd:cd01595 315 flllDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
154-460 |
1.06e-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: 100.01 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 154 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 233
Cdd:cd01597 113 DALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 234 -------GLNTRIGFaekvaakvAALTGLPFVTAPnkfeALAAHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLG 306
Cdd:cd01597 192 laslgdqGLAVQEAL--------AAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 307 ELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGnHVAVTV---------GGSNGHFELNVFKPMMIknvlhsarlL 375
Cdd:cd01597 257 EVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLdamvqeherDAGAWHAEWIALPEIFL---------L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 376 GDASVSFTENCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKA----AKIAKTAHKNGSTLKETAIE--- 440
Cdd:cd01597 327 ASGALEQAEFLLSGLEVNEDRMRAnldltgglILSEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpe 404
|
330 340
....*....|....*....|.
5D6B_A 441 -LGYLTAEQFDEWVKPKDMLG 460
Cdd:cd01597 405 vAAYLSDEELDALLDPANYLG 425
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
132-460 |
6.50e-22 |
|
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: 97.80 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 132 HVNKSQSSNDTFPTAMHIAAAiEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAM 211
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLLR-DALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 212 TRIKAAMPRIYELAAGGtAVGTGLNTRIGFAEKVAAKVAALtGLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIA 291
Cdd:TIGR00928 169 ERLLQAKERIKVGGISG-AVGTHAAAYPLVEEVEERVTEFL-GLKPVPISTQIEP---RDRHAELLDALALLATTLEKFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 292 NDIRFLgsgPRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAaqVMGNHVAVTVGGSNGH-FELNVFKPMMIKNV 368
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVeePFGKGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLwHERDLTDSSVERVI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 369 LHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHI-------GYDKAAKIAK-----TAHKNGSTLKE 436
Cdd:TIGR00928 319 LPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRelamgAAEVDEPDLLE 398
|
330 340
....*....|....*....|....*...
5D6B_A 437 TAIELG----YLTAEQFDEWVKPKDMLG 460
Cdd:TIGR00928 399 FLLEDEritkYLKEEELAELLDPETYIG 426
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
139-336 |
3.70e-15 |
|
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: 76.82 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 139 SNDTFPTA--MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKA 216
Cdd:cd01360 91 SSDVVDTAlaLQLREALDI---ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 217 AMPRIYELAAGGtAVGTGLNtrIGFAEKVAAKVAAltGLPFVTAPNKfeaLAAHDALVELSGAMNTTACSLMKIANDIRF 296
Cdd:cd01360 168 ARERILVGKISG-AVGTYAN--LGPEVEERVAEKL--GLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRH 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
5D6B_A 297 LgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVA 336
Cdd:cd01360 240 L---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
67-455 |
2.38e-14 |
|
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: 74.70 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 67 KIANAIMKAADEVAEGKLNDHFPLvvwqtgsgtqtnMNVNEVISNRAIEMLGGELGSKIpvhpndHVNKSQssNDTFPTA 146
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGKL------HTGRSR--NDQVATD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 147 MHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 226
Cdd:TIGR00838 115 LRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 227 GGTAV-GTGLntrigfaEKVAAKVAALTGLPFVTApNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 305
Cdd:TIGR00838 194 GSGALaGTGF-------PIDREYLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---F 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 306 GELILP-ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVtvggsnghfelnvfkpMMIKNVLHSA---------RLL 375
Cdd:TIGR00838 263 GFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM----------------LMTLKALPLAynrdlqedkEPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 376 GDaSVSFTENCV-------VGIQANTERINKLMNESLMLVTALNPHI---------GYDKAAKIAKTAHKNGSTLKETAI 439
Cdd:TIGR00838 327 FD-ALKTVELSLematgmlDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHHIVGELVATAIERGKGLEELTL 405
|
410
....*....|....*.
5D6B_A 440 ELGYLTAEQFDEWVKP 455
Cdd:TIGR00838 406 EELQKFSPEFDEDVYE 421
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
157-460 |
2.10e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 65.81 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 157 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT--G 234
Cdd:PRK09053 125 DLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGTlaS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 235 LNTRigfaekvaakvaaltglpfvtAPNKFEALAA-----------H---DALVELSGAMNTTACSLMKIANDIRFLgsg 300
Cdd:PRK09053 204 LGEQ---------------------ALPVAQALAAelqlalpalpwHtqrDRIAEFASALGLLAGTLGKIARDVSLL--- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 301 PRSGLGELILP--ENEPGSSIMPGKVNPTQCEAM------------TMVAAQVMGNHVAvtVGGsnGHFELNVFKPMmik 366
Cdd:PRK09053 260 MQTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERA--LGG--WHAEWDTLPEL--- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 367 nvlhsARLLGDAsVSFTENCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKAAKI----AKTAHKNGSTL 434
Cdd:PRK09053 333 -----ACLAAGA-LAQMAQIVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEGRHL 404
|
330 340 350
....*....|....*....|....*....|
5D6B_A 435 K----ETAIELGYLTAEQFDEWVKPKDMLG 460
Cdd:PRK09053 405 RdvlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
146-326 |
1.99e-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: 62.64 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 146 AMHIAAAIevHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKaampRIYELA 225
Cdd:cd01598 110 ALMIKEAR--NEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK----QIEILG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 226 AGGTAVGT------------------GLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAM---NTTa 284
Cdd:cd01598 184 KFNGAVGNfnahlvaypdvdwrkfseFFVTSLG-----------LTWNPYTT------QIEPHDYIAELFDALariNTI- 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
5D6B_A 285 csLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 326
Cdd:cd01598 246 --LIDLCRDIwgyislGYFKQKVKKG---------EVGSSTMPHKVNP 282
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
157-341 |
2.85e-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: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 157 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTaVGTG-- 234
Cdd:cd03302 113 DLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQas 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 235 --------------LNTRI----GFaekvaAKVAALTGLpfvTAPNKFEALAAhDALVELsGAmnttacSLMKIANDIRF 296
Cdd:cd03302 192 fldlfegdhdkveaLDELVtkkaGF-----KKVYPVTGQ---TYSRKVDIDVL-NALSSL-GA------TAHKIATDIRL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
5D6B_A 297 LgsgprSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMG 341
Cdd:cd03302 256 L-----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
146-326 |
2.96e-09 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 58.99 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 146 AMHIAAAIEvhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyELA 225
Cdd:PRK09285 132 ALMLKEARE--EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EIL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 226 A--GGtAVGTgLN-------------------TRIGfaekvaakvaaLTGLPFVTA--PnkfealaaHDALVELSGAM-- 280
Cdd:PRK09285 205 GkiNG-AVGN-YNahlaaypevdwhafsrefvESLG-----------LTWNPYTTQieP--------HDYIAELFDAVar 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
5D6B_A 281 -NTtacSLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 326
Cdd:PRK09285 264 fNT---ILIDLDRDVwgyislGYFKQKTKAG---------EIGSSTMPHKVNP 304
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
69-348 |
5.51e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 69 ANAIMKAADEVAEGKLNDHFplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvhpndHVNKSQssNDTFPT--A 146
Cdd:PLN02646 70 RDSILDGLDEIEKEIEAGKF---EWRPD-----REDVHMNNEARLTELIG-EPAKKL------HTARSR--NDQVATdtR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 147 MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 226
Cdd:PLN02646 133 LWCRDAIDV---IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 227 GGTAV-GTGLntriGFAEKVAAKVAALTGLpfvtAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 305
Cdd:PLN02646 210 GSCALaGTGL----PIDRFMTAKDLGFTAP----MRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---F 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....
5D6B_A 306 GELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 348
Cdd:PLN02646 279 GFVTPSDAvSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLA 322
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
49-411 |
3.03e-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: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 49 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGSGtqtnmNVNEVISNRAIEMLGgELGSKIpvh 128
Cdd:cd01359 27 GILTEEEAA---------KILAGLAKIRAEIEAGAF-------ELDPEDE-----DIHMAIERRLIERIG-DVGGKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 129 pndHVNKSqsSNDTFPTAMHIAAAIEVhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVK 208
Cdd:cd01359 82 ---HTGRS--RNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 209 YAMTRIKAAMPRIYELAAGGTA-VGTGLN-------TRIGFAEKvaakvaaltglpfvtAPNKFEALAAHDALVELSGAM 280
Cdd:cd01359 156 RDLERLADAYKRVNVSPLGAGAlAGTTFPidrertaELLGFDGP---------------TENSLDAVSDRDFVLEFLSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 281 NTTACSLMKIANDIRFLGSGPRsGLGELilpeneP-----GSSIMPGKVNPTQCEAMTMVAAQVMGNHVAV--TVGG--S 351
Cdd:cd01359 221 ALLMVHLSRLAEDLILWSTQEF-GFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLltTLKGlpL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
5D6B_A 352 NGHFELNVFKPMM---IKNVLHSARLLGDasvsftenCVVGIQANTERINKLMNESLMLVTAL 411
Cdd:cd01359 294 AYNKDLQEDKEPLfdaVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
119-330 |
1.22e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 50.94 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 119 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 198
Cdd:PRK12308 97 GDLGKKL------HTGRSR--NDQVATDLKLWCRQQGQQLLL-ALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 199 EFSGYVQQVKYAMTRIKAAMPRIYELAAG-GTAVGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAAH 270
Cdd:PRK12308 168 WCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTAypidreaLAHNLGFRRATR---------------NSLDSVSDR 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
5D6B_A 271 DALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGEliLPEN-EPGSSIMPGKVNPTQCE 330
Cdd:PRK12308 233 DHVMELMSVASISMLHLSRLAEDLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALE 290
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
286-460 |
3.54e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 47.72 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 286 SLMKIANDIRFLgSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvAVTVGGSNGH-FELNVFKPMM 364
Cdd:PRK08937 29 SLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY--LVTALENVPLwHERDLSHSSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 365 IKNVLHSARLLGDASVSFTENCVVGIQANTERINK--------LMNESLMLvTALNPHIG----YDKAAKIAKTAHKNGS 432
Cdd:PRK08937 106 ERIALPDAFLALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|..
5D6B_A 433 TLKETAIE----LGYLTAEQFDEWVKPKDMLG 460
Cdd:PRK08937 185 DLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
155-330 |
9.35e-06 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 47.81 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 155 VHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSgyvqQVKYAMTRIKAAMP--RIYELAAGGT--- 229
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMA----NFAYRLSRQRKQLSevKIKGKFAGAVgny 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 230 -------------AVGTGLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAMNTTACSLMKIANDIRF 296
Cdd:PLN02848 218 nahmsaypevdwpAVAEEFVTSLG-----------LTFNPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRDIWS 280
|
170 180 190
....*....|....*....|....*....|....
5D6B_A 297 LGSgprSGLGELILPENEPGSSIMPGKVNPTQCE 330
Cdd:PLN02848 281 YIS---LGYFKQITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
49-326 |
2.85e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 46.30 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 49 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvH 128
Cdd:PRK00855 51 GILSEEEAE---------KILAGLDEILEEIEAGKF-------EFSPE-----LEDIHMAIEARLTERIG-DVGGKL--H 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 129 P----NDHVnksqssndtfPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYV 204
Cdd:PRK00855 107 TgrsrNDQV----------ATDLRLYLRDEIDEIAE-LLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 205 QQVKYAMTRIKAAMPRIYELAAGGTA-VGTGLNT-------RIGFAEkvaakvaaltglpfVTApNKFEALAAHDALVEL 276
Cdd:PRK00855 176 EMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIdrertaeLLGFDG--------------VTE-NSLDAVSDRDFALEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
5D6B_A 277 SGAMNTTACSLMKIANDIrFLGSGPRSGLGELilpeneP-----GSSIMPGKVNP 326
Cdd:PRK00855 241 LSAASLLMVHLSRLAEEL-ILWSSQEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
119-348 |
1.66e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 43.82 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 119 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 198
Cdd:PRK04833 97 GDLGKKL------HTGRSR--NDQVATDLKLWCKDQVAE-LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 199 EFSGYVQQVKYAMTRIKAAMPR--IYELAAGGTAvGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAA 269
Cdd:PRK04833 168 WCLAYVEMLARDESRLQDALKRldVSPLGSGALA-GTAyeidreqLAGWLGFASATR---------------NSLDSVSD 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5D6B_A 270 HDALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGELIlPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 348
Cdd:PRK04833 232 RDHVLELLSDASISMVHLSRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLM 308
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
131-345 |
3.22e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 42.73 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 131 DHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYA 210
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRL-KAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 211 MTRIKAAMPRIYELAAGGtAVGTgLNTRIGFAEKVAAKVAALTGLPfvTAPnkfEALAAHDALVELSGAMNTTACSLMKI 290
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLGKF 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
5D6B_A 291 ANDIRFLgsgprSGLGELILPENEPGSSIMPGKVNPTQCEAMTMV----AAQVMGNHVA 345
Cdd:PRK05975 252 GQDIALM-----AQAGDEISLSGGGGSSAMPHKQNPVAAETLVTLarfnATQVSGLHQA 305
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
189-341 |
4.99e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 39.45 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 189 QDAVPLTLGQefsgYVQQVKYAMTRIKAAMPRIYE------LAAGGTAvGTGLNTRIGFAEKVaakvaaltgLPFVT-AP 261
Cdd:PRK02186 565 QPALPGSLGH----YLLAVDGALARETHALFALFEhidvcpLGAGAGG-GTTFPIDPEFVARL---------LGFEQpAP 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5D6B_A 262 NKFEALAAHDALVELSGAMNTTACSLMKIANDIRfLGSGPRSGLgeLILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVM 340
Cdd:PRK02186 631 NSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQ-LWTTREFAL--VSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVA 707
|
.
5D6B_A 341 G 341
Cdd:PRK02186 708 G 708
|
|
| |
