|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-463 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 922.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 1 MTATRTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 81 IDGKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 161 LPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPV 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 241 GFAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 321 MPGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKA 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586791851 401 GLERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGPK 463
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-461 |
0e+00 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 905.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 1 MTATRTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 81 IDGKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 161 LPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPV 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 241 GFAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 321 MPGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKA 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586791851 401 GLERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIG 461
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
5-459 |
0e+00 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 850.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 5 RTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDGK 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 85 LNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHLLPAL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 165 KHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAE 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 245 KVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 325 VNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLER 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1586791851 405 SLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETM 459
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
5-455 |
0e+00 |
|
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 780.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 5 RTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDGK 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 85 LNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGsKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHLLPAL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 165 KHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAE 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 245 KVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 325 VNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLER 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1586791851 405 SLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVR 455
Cdd:cd01596 400 SLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
5-461 |
0e+00 |
|
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]
Pssm-ID: 130052 [Multi-domain] Cd Length: 458 Bit Score: 775.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 5 RTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDGK 84
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 85 LNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHLLPAL 164
Cdd:TIGR00979 82 LDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 165 KHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAE 244
Cdd:TIGR00979 162 ENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 245 KVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIMPGK 324
Cdd:TIGR00979 242 KVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 325 VNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLER 404
Cdd:TIGR00979 322 VNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586791851 405 SLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIG 461
Cdd:TIGR00979 402 SLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
11-462 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 749.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 11 FGPIDVAADRYWGAQAERSLGNFKIG--WEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDGKLNDH 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 89 FPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHLLPALKHLH 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 169 AALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAEKVAQ 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 249 EIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 329 QCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLERSLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1586791851 409 VTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGP 462
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
4-462 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 594.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 4 TRTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDG 83
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 84 KLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHLLPA 163
Cdd:PRK12425 82 QHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 164 LKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFA 243
Cdd:PRK12425 162 IAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 244 EKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIMPG 323
Cdd:PRK12425 242 EAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 324 KVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLE 403
Cdd:PRK12425 322 KVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586791851 404 RSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGP 462
Cdd:PRK12425 402 RGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
5-463 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 587.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 5 RTETDTFGPIDVAADRYWGAQAERSLGNFKIGweKQPLS----IVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEV 80
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPIS--GRPISdhpeLIRALAMVKKAAALANRELGLLDKEKADAIVAACDEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 81 IDGKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHhL 160
Cdd:COG1027 79 IAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 161 LPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPV 240
Cdd:COG1027 158 LEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 241 GFAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSI 320
Cdd:COG1027 238 GYIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 321 MPGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKA 400
Cdd:COG1027 318 MPGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCRE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586791851 401 GLERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGPK 463
Cdd:COG1027 398 YVENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-463 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 576.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 1 MTATRTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEK--QPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQ 78
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKisDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 79 EVIDGKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIaH 158
Cdd:PRK12273 82 EILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSL-R 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 159 HLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNA 238
Cdd:PRK12273 161 KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 239 PVGFAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGS 318
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 319 SIMPGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNI 398
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586791851 399 KAGLERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGPK 463
Cdd:PRK12273 401 REYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-453 |
0e+00 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 556.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 5 RTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDGK 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 85 LNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHhLLPAL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRK-LLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 165 KHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAE 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 245 KVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 325 VNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLER 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1586791851 405 SLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAI 453
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEI 448
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
2-463 |
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 1586791851 2 TATRTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEKQPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVI 81
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 82 DGKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIaHHLL 161
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL-EGLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 162 PALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVG 241
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 242 FAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIM 321
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 322 PGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAG 401
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586791851 402 LERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGPK 463
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-462 |
4.48e-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: 4.48e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 5 RTETDTFGPIDVAADRYWGAQAERSLGNFKIGWEK--QPLSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVID 82
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKisDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 83 -GKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHhLL 161
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIK-LV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 162 PALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVG 241
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 242 FAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIM 321
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 322 PGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAG 401
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586791851 402 LERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGP 462
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-462 |
1.06e-147 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 429.80 E-value: 1.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 3 ATRTETDTFGPIDVAADRYWGAQAERSLGNFKI-GWEKQPlSIVRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVI 81
Cdd:PRK14515 10 GVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPItGYKIHE-GLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 82 DGKLNDHFPLVVWQTGSGTQSNMNANEVISNRAIEMLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIaHHLL 161
Cdd:PRK14515 89 DGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNAL-EGLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 162 PALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVG 241
Cdd:PRK14515 168 QTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 242 FAEKVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPENEPGSSIM 321
Cdd:PRK14515 248 YIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 322 PGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAG 401
Cdd:PRK14515 328 PGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEY 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586791851 402 LERSLMLVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETMIGP 462
Cdd:PRK14515 408 VEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
6.83e-126 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 368.23 E-value: 6.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 12 GPIDVAADRYWGAQAERSLGNFKIGWEKqplsiVRALGIVKQAAARANVSLgqlePALGKGIVDAAQEVI-DGKLNDHFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-----IKGLAALKKAAAKANVIL----KEEAAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 91 LVVWQTGSGTQSNMNANEVISnraiEMLGgvmgskKPVHPNDHVNMSQSSNDTYPTAMHIACAERIAHHLLPALKHLHAA 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 171 LDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPG-LCELAQGGTAVGTGLNAPVGFAEKVAQE 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 250 IANITGMPfVTAPNKFEALASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPrAGLGELALPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 1586791851 330 CEAMTQVCIHIFG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-393 |
8.52e-112 |
|
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: 332.54 E-value: 8.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 45 VRALGIVKQAAARANVSLGQLEPALGKGIVDAAQEVIDGKLNDHFplvvWQTGSGTQSNMNANEVISNRAIEMLGGvmgs 124
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 125 kkpvhpndHVNMSQSSNDTYPTAMHIACAERIaHHLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGY 204
Cdd:cd01334 73 --------YVHTGRSSNDIVDTALRLALRDAL-DILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 205 AAQVGSAIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAEKVAQEIanitGMpFVTAPNKFEALASHDSMVFSHGAINAA 284
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELL----GF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 285 AAALFKIANDIRLLGSGpraGLGELALPEN-EPGSSIMPGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHFELNVYNP 363
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|
gi 1586791851 364 MMAYNFLQSVQLLADAAVSFTDNCvVGIEA 393
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVL-EGLEV 324
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
104-384 |
2.80e-54 |
|
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: 181.27 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 104 MNANEVISNRAIEMLGGVmgskkpvHPNDHVNMSQSSNDTYPTAMHIACAERIaHHLLPALKHLHAALDMKVTEFSHIIK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDIGTTALRLALRDAL-DDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 184 IGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEmtlpglcelaqggtavgtglNAPVgfaekvaqeianitgmpfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLE--------------------EAAV----------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 264 kfealashdsmVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPeNEPGSSIMPGKVNPTQCEAMTQVCIHIFGN 343
Cdd:cd01594 123 -----------AEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1586791851 344 NAALTFADSQGHFELNVYNPMMAYNFLQSVQLLADAAVSFT 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
3.39e-24 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 94.69 E-value: 3.39e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1586791851 408 LVTALAPKIGYDAAAKIAKTAHKNGTTLKEEALASGLVTSEEYDAIVRPETM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
160-461 |
5.35e-23 |
|
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: 100.93 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 160 LLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGtAVGTgLNAP 239
Cdd:COG0015 118 LLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT-YAAH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 240 VGFAEKVAQEIANITGMpfvtapnKFEALA----SHDSM--VFShgAINAAAAALFKIANDIRLLGsgpRAGLGELALP- 312
Cdd:COG0015 196 GEAWPEVEERVAEKLGL-------KPNPVTtqiePRDRHaeLFS--ALALIAGSLEKIARDIRLLQ---RTEVGEVEEPf 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 313 -ENEPGSSIMPGKVNPTQCEAMT-------QVCIHIFGNNA-----ALTfaDSqgHFELNVynpmmaynfLQSVQLLADA 379
Cdd:COG0015 264 aKGQVGSSAMPHKRNPIDSENIEglarlarALAAALLEALAswherDLS--DS--SVERNI---------LPDAFLLLDG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 380 AVSFTDNCVVGIEAREDNIKAGLERSLMLV------TALAPK-IG----YDAAAKIAKTAHKNGTTLKEEALA----SGL 444
Cdd:COG0015 331 ALERLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRELLAAdpeiPAE 410
|
330
....*....|....*..
gi 1586791851 445 VTSEEYDAIVRPETMIG 461
Cdd:COG0015 411 LSKEELEALFDPANYLG 427
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
133-461 |
1.12e-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: 97.03 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 133 HVNMSQSSNDTYPTAMHIACAERIaHHLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAI 212
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLLRDAL-EIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 213 KRIEMTLPGLCeLAQGGTAVGTGLNAPVGFAEkVAQEIANITGMPFVTAPNKFEALASHDSMVFSHGAINAAaaaLFKIA 292
Cdd:TIGR00928 169 ERLLQAKERIK-VGGISGAVGTHAAAYPLVEE-VEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATT---LEKFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 293 NDIRLLgsgPRAGLGELALP--ENEPGSSIMPGKVNPTQCEAMTQVCIHIFGN------NAALtfadsqgHFELNVYNPM 364
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLARVIRGYaspaleNAPL-------WHERDLTDSS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 365 MAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIKAGLERSLMLVtaLAPKI---------GYDAAAKIAK-----TAHK 430
Cdd:TIGR00928 314 VERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLI--ASERVlialvergmGREEAYEIVRelamgAAEV 391
|
330 340 350
....*....|....*....|....*....|....*
gi 1586791851 431 NGTTLKEEALASGLVTS----EEYDAIVRPETMIG 461
Cdd:TIGR00928 392 DEPDLLEFLLEDERITKylkeEELAELLDPETYIG 426
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
158-429 |
1.08e-20 |
|
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176467 [Multi-domain] Cd Length: 381 Bit Score: 93.34 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 158 HHLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGtAVGTGLN 237
Cdd:cd01595 106 DIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHAS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 238 APVGfAEKVAQEIANITGMPFVTAPNKFEalaSHDSMVFSHGAINAAAAALFKIANDIRLLGsgpRAGLGELALP--ENE 315
Cdd:cd01595 185 LGPK-GPEVEERVAEKLGLKVPPITTQIE---PRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 316 PGSSIMPGKVNPTQCEAMT----QVC--IHIFGNNAALTF--ADSQGHFELNVYnPMMAYnflqsvqlLADAAVSFTDNC 387
Cdd:cd01595 258 VGSSTMPHKRNPIDSENIEglarLVRalAAPALENLVQWHerDLSDSSVERNIL-PDAFL--------LLDAALSRLQGL 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1586791851 388 VVGIEAREDNIKAGLERSLMLV------TALAPK-IGYDAAAKIAKTAH 429
Cdd:cd01595 329 LEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
160-334 |
1.33e-12 |
|
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: 69.12 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 160 LLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGtAVGTGlnAP 239
Cdd:cd01360 110 ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKISG-AVGTY--AN 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 240 VGFaeKVAQEIANITGMPFVTAPNKfeaLASHDSMVFSHGAINAAAAALFKIANDIRLLgsgPRAGLGELALP--ENEPG 317
Cdd:cd01360 187 LGP--EVEERVAEKLGLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRHL---QRTEVLEVEEPfsKGQKG 258
|
170
....*....|....*..
gi 1586791851 318 SSIMPGKVNPTQCEAMT 334
Cdd:cd01360 259 SSAMPHKRNPILSENIC 275
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
159-461 |
5.77e-10 |
|
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: 61.18 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 159 HLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELAQGGTaVGTG--- 235
Cdd:cd03302 114 LILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQasf 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 236 LNAPVGFAEKVAQ------------EIANITGMpfvTAPNKfealasHDSMVFShgAINAAAAALFKIANDIRLLgsgpr 303
Cdd:cd03302 193 LDLFEGDHDKVEAldelvtkkagfkKVYPVTGQ---TYSRK------VDIDVLN--ALSSLGATAHKIATDIRLL----- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 304 AGLGELALP--ENEPGSSIMPGKVNPTQCEAMTQVCIHIFG--NNAALTFADsQGhFELNVYNPMMAYNFLQSVQLLADA 379
Cdd:cd03302 257 ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMNlaSNAAQTAST-QW-FERTLDDSANRRIAIPEAFLAADA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 380 AVSFTDNCVVGIEAREDNIKAGLERSL--MLVTAL---APKIG---YDAAAKIAKTAHKNGTTLKEEALASGLV------ 445
Cdd:cd03302 335 ILITLQNISEGLVVYPKVIERHIRQELpfMATENIimaAVKAGgdrQDAHERIRVLSHQAAAVVKQEGGDNDLIeriknd 414
|
330 340
....*....|....*....|.
gi 1586791851 446 -----TSEEYDAIVRPETMIG 461
Cdd:cd03302 415 ayfkpIWDELDALLDPKTFIG 435
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
54-343 |
2.33e-09 |
|
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: 59.29 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 54 AAARANVSLGQLEPALGKGIVDA----AQEVIDGKLNDHFPLvvwqtgsgtqsnMNANEVISNRAIEMLGGVMGSKkpvh 129
Cdd:TIGR00838 37 AHTKMLKKAGILTEEEAAKIIEGlnelKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGK---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 130 pndhVNMSQSSNDTYPTAMHIACAERIAHhLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVG 209
Cdd:TIGR00838 101 ----LHTGRSRNDQVATDLRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 210 SAIKRIEMTLPGLCELAQGGTAV-GTGLnapvgfaeKVAQE-IANITGMPFVTApNKFEALASHDSMVFSHGAINAAAAA 287
Cdd:TIGR00838 176 RDYERLQDALKRVNVSPLGSGALaGTGF--------PIDREyLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586791851 288 LFKIANDIRLLGSGpRAGLGELAlPENEPGSSIMPGKVNPTQCEAMTQVCIHIFGN 343
Cdd:TIGR00838 247 LSRFAEDLILWSTG-EFGFVELP-DEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
156-327 |
5.62e-09 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 58.02 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 156 IAHHLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPglceLAQGGTAVGTg 235
Cdd:cd01598 117 RNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQIEI----LGKFNGAVGN- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 236 LNA-----P----VGFAEKVAQEIaNITGMPFVTapnkfeALASHDSMVFSHGAINAAAAALFKIANDI------RLLGS 300
Cdd:cd01598 192 FNAhlvayPdvdwRKFSEFFVTSL-GLTWNPYTT------QIEPHDYIAELFDALARINTILIDLCRDIwgyislGYFKQ 264
|
170 180
....*....|....*....|....*..
gi 1586791851 301 GPRAGlgelalpenEPGSSIMPGKVNP 327
Cdd:cd01598 265 KVKKG---------EVGSSTMPHKVNP 282
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
154-331 |
8.49e-09 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 57.44 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 154 ERIAHHLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEmTLPGLCELAqggTAVG 233
Cdd:PLN02848 140 EGVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLS-EVKIKGKFA---GAVG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 234 TgLNAPVgFA------EKVAQEIANITGM---PFVTapnkfeALASHDSMVFSHGAINAAAAALFKIANDIR---LLG-- 299
Cdd:PLN02848 216 N-YNAHM-SAypevdwPAVAEEFVTSLGLtfnPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRDIWsyiSLGyf 287
|
170 180 190
....*....|....*....|....*....|...
gi 1586791851 300 -SGPRAGlgelalpenEPGSSIMPGKVNPTQCE 331
Cdd:PLN02848 288 kQITKAG---------EVGSSTMPHKVNPIDFE 311
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
290-461 |
1.57e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 54.65 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 290 KIANDIRLLgSGPRAGLGELALPENEPGSSIMPGKVNPTQCEAMTQVCIHIFGnNAALTFADSQGHFELNV-YNPM---- 364
Cdd:PRK08937 32 KFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRS-YLVTALENVPLWHERDLsHSSAeria 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 365 MAYNFlqsvqLLADAAVSFTDNCVVGIEAREDNIKAGLERSL-------MLVTALAPKIG----YDAAAKIAKTAHKNGT 433
Cdd:PRK08937 110 LPDAF-----LALDYILNRFVNILENLVVFPENIERNLDKTLgfiaterVLLELVEKGMGreeaHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|..
gi 1586791851 434 TLKEEALA----SGLVTSEEYDAIVRPETMIG 461
Cdd:PRK08937 185 DLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
160-461 |
1.14e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 53.87 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 160 LLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGLCELaQGGTAVGTgLNAP 239
Cdd:PRK09053 127 LEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVL-QFGGAAGT-LASL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 240 VGFAEKVAQEIANITGMPFVTAPNKfealASHDSMVFSHGAINAAAAALFKIANDIRLLGSGPRAGLGELALPeNEPGSS 319
Cdd:PRK09053 205 GEQALPVAQALAAELQLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPAAA-GKGGSS 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 320 IMPGKVNPTQCEAMTQVCIHIFGNNAALTFADSQGHfELNVYNPMMAYNFLQSVQLLADAAVSFTDNCVVGIEAREDNIK 399
Cdd:PRK09053 280 TMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEH-ERALGGWHAEWDTLPELACLAAGALAQMAQIVEGLEVDAARMR 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586791851 400 AGLE--RSLML----VTALAPKIGYDAAAKI----AKTAHKNGTTLK----EEALASGLVTSEEYDAIVRPETMIG 461
Cdd:PRK09053 359 ANLDltHGLILaeavMLALADRIGRLDAHHLveqaSKRAVAEGRHLRdvlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
160-327 |
1.39e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 53.60 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 160 LLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEmTLPGLCELaqGGtAVGTgLNAP 239
Cdd:PRK09285 143 LLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLE-AVEILGKI--NG-AVGN-YNAH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 240 VgFA------EKVAQEianitgmpFVTA----PNKF----EalaSHDSMVFSHGAINAAAAALFKIANDI------RLLG 299
Cdd:PRK09285 218 L-AAypevdwHAFSRE--------FVESlgltWNPYttqiE---PHDYIAELFDAVARFNTILIDLDRDVwgyislGYFK 285
|
170 180
....*....|....*....|....*...
gi 1586791851 300 SGPRAGlgelalpenEPGSSIMPGKVNP 327
Cdd:PRK09285 286 QKTKAG---------EIGSSTMPHKVNP 304
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
138-425 |
2.24e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 50.17 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 138 QSSNDTYPTAMHIACAERiAHHLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQVGSAIKRIEM 217
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQ-GQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLED 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 218 TLPGL--CELAQGGTAvGTGLnaPVGfAEKVAQEIAnitgmpFVTAP-NKFEALASHDSMVFSHGAINAAAAALFKIAND 294
Cdd:PRK12308 186 ALTRLdtCPLGSGALA-GTAY--PID-REALAHNLG------FRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAED 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 295 IRLLGSGpRAGLGELAlPENEPGSSIMPGKVNPTQCEAMTQVCIHIFGNNAALTfadsqghfeLNVYNPMMAYN--FLQS 372
Cdd:PRK12308 256 LIFYNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMM---------MTVKALPLAYNkdMQED 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1586791851 373 VQLLADAAVSFTDnCVVGIEAREDNIKAGLERSLMlvtalAPKIGYDAAAKIA 425
Cdd:PRK12308 325 KEGLFDALDTWND-CMEMAALCFDGIKVNGERTLE-----AAKQGYANATELA 371
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
190-413 |
5.97e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 48.69 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 190 QDATPLTLGQEFSGYAAQVGSAIKRIEMTLPGL--CELaqgGTAVGTGLNAPVGfAEKVAQEIANITGmpfvtAPNKFEA 267
Cdd:PRK02186 565 QPALPGSLGHYLLAVDGALARETHALFALFEHIdvCPL---GAGAGGGTTFPID-PEFVARLLGFEQP-----APNSLDA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 268 LASHDSMVFSHGAINAAAAALFKIANDIRLLGSgprAGLGELALPEN-EPGSSIMPGKVNPTQCEAMTQVCIHIFGNNAA 346
Cdd:PRK02186 636 VASRDGVLHFLSAMAAISTVLSRLAQDLQLWTT---REFALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAGALAS 712
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586791851 347 LTFADSQGHF--ELNVYNPMmaynflqsVQLLADAAVSFTDNCVV------GIEAREDNIKAGLERSLMLVTALA 413
Cdd:PRK02186 713 ASAALGKTPFsnSFEAGSPM--------NGPIAQACAAIEDAAAVlvllidGLEADQARMRAHLEDGGVSATAVA 779
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
53-327 |
7.92e-05 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 45.10 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 53 QAAARANVSLGQLEP----ALGKGIVDAAQEVIDGKLndhfplvVWQTGSgTQSNMNanevISNRAIEMLGGVMGSkkpv 128
Cdd:PLN02646 53 KAHASMLAKQGIITDedrdSILDGLDEIEKEIEAGKF-------EWRPDR-EDVHMN----NEARLTELIGEPAKK---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 129 hpndhVNMSQSSNDTYPTAMHIACAERIAHhLLPALKHLHAALDMKVTEFSHIIKIGRTHTQDATPLTLGQEFSGYAAQ- 207
Cdd:PLN02646 117 -----LHTARSRNDQVATDTRLWCRDAIDV-IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791851 208 ------VGSAIKRIEMTLPGLCELAqggtavGTGLnaPVGfaekvAQEIANITGMPFVTaPNKFEALASHDSMVFSHGAI 281
Cdd:PLN02646 191 erdagrLVDCRPRVNFCPLGSCALA------GTGL--PID-----RFMTAKDLGFTAPM-RNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1586791851 282 NAAAAALFKIANDIRLLGSGPragLGELALPEN-EPGSSIMPGKVNP 327
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEE---FGFVTPSDAvSTGSSIMPQKKNP 300
|
|
| |
