|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-464 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 926.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 1 MAATRIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEV 80
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 81 LAGKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDL 160
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 161 LPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHP 240
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 241 EYAVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 321 MPGKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINK 400
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363274 401 LLHESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVGSMK 464
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| 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: 916.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 1 MAATRIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEV 80
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 81 LAGKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDL 160
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 161 LPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHP 240
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 241 EYAVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 321 MPGKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINK 400
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490363274 401 LLHESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVG 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: 862.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 5 RIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLAGK 84
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 85 HPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDLLPEL 164
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 165 KSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 245 RVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 325 VNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLLHE 404
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 490363274 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDM 459
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| 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: 849.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 5 RIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLAGK 84
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 85 HPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDLLPEL 164
Cdd:TIGR00979 82 LDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 165 KSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEYAV 244
Cdd:TIGR00979 162 ENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 245 RVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:TIGR00979 242 KVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 325 VNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLLHE 404
Cdd:TIGR00979 322 VNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363274 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVG 461
Cdd:TIGR00979 402 SLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| 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: 787.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 5 RIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLAGK 84
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 85 HPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGmERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDLLPEL 164
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 165 KSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 245 RVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 325 VNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLLHE 404
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 490363274 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVR 455
Cdd:cd01596 400 SLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
11-461 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 709.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 11 MGQIEVPADQLWGAQTQRSLEHFRISV--EKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLAGKHPTE 88
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGerERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 89 FPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDLLPELKSLL 168
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 169 KVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEYAVRVAK 248
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 249 RIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPT 328
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 329 QCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLLHESLML 408
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 490363274 409 VTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVG 461
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTG 453
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
4-465 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 603.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 4 TRIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLAG 83
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 84 KHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDLLPE 163
Cdd:PRK12425 82 QHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 164 LKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEYA 243
Cdd:PRK12425 162 IAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 244 VRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG 323
Cdd:PRK12425 242 EAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 324 KVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLLH 403
Cdd:PRK12425 322 KVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490363274 404 ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVGSMKK 465
Cdd:PRK12425 402 RGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAGGH 463
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
5-461 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 572.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 5 RIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPV--ALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLA 82
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDhpELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 83 GKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQdLLP 162
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRE-LLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 163 ELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEY 242
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 243 AVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMP 322
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 323 GKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLL 402
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363274 403 HESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVG 461
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTG 458
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-461 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 561.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 1 MAATRIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKM---PvALIHALALTKKAAAGVNMDLGLLPKERADAIIAAA 77
Cdd:PRK12273 2 MMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKIsdyP-ELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 78 DEVLAGKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALR 157
Cdd:PRK12273 81 DEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 158 QdLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLN 237
Cdd:PRK12273 161 K-LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 238 THPEYAVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPG 317
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 318 SSIMPGKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRER 397
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490363274 398 INKLLHESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMVG 461
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTH 463
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
5-451 |
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: 554.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 5 RIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLAGK 84
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 85 HPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRqDLLPEL 164
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLR-KLLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 165 KSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEYAV 244
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 245 RVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGK 324
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 325 VNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLLHE 404
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 490363274 405 SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFD 451
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELD 446
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
2-460 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 524.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 2 AATRIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVL 81
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 82 AGKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRqDLL 161
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLE-GLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 162 PELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPE 241
Cdd:PRK13353 162 AAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 242 YAVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIM 321
Cdd:PRK13353 242 YIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 322 PGKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKL 401
Cdd:PRK13353 322 PGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEY 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490363274 402 LHESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMV 460
Cdd:PRK13353 402 VEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
5-460 |
2.18e-144 |
|
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]
Pssm-ID: 213564 [Multi-domain] Cd Length: 468 Bit Score: 421.16 E-value: 2.18e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 5 RIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKM---PVaLIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVL 81
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKIsdiPE-FVRGMVMVKKAAALANKELGTIPESIANAIVAACDEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 82 -AGKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAaVIALRQDL 160
Cdd:TIGR00839 80 nNGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIA-VYSSLIKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 161 LPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHP 240
Cdd:TIGR00839 159 VDAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 241 EYAVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI 320
Cdd:TIGR00839 239 EYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 321 MPGKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINK 400
Cdd:TIGR00839 319 MPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 401 LLHESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDMV 460
Cdd:TIGR00839 399 YVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLM 458
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-459 |
4.24e-134 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 395.14 E-value: 4.24e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 3 ATRIEKDSMGQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKKAAAGVNMDLGLLPKERADAIIAAADEVLA 82
Cdd:PRK14515 10 GVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 83 GKHPTEFPLAIWQTGSGTQSNMNMNEVLANRGSEILGGIRGMERKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQdLLP 162
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG-LLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 163 ELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALGGTAVGTGLNTHPEY 242
Cdd:PRK14515 169 TMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 243 AVRVAKRIAELSGQPFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMP 322
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 323 GKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINKLL 402
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490363274 403 HESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDM 459
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEM 465
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-342 |
2.24e-131 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 382.10 E-value: 2.24e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 12 GQIEVPADQLWGAQTQRSLEHFRISVEKMPVALIHALALTKkaaagvnmdLGLLPKERADAIIAAADEVLA-GKHPTEFP 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAK---------ANVILKEEAAAIIKALDEVAEeGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 91 LAIWQTGSGTQSNMNMNEVLAnrgsEILGgirgmeRKIHPNDDVNKSQSSNDVFPTAMHVAAVIALRQDLLPELKSLLKV 170
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 171 FKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVP-HVCELALGGTAVGTGLNTHPEYAVRVAKR 249
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPrLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 250 IAELSGQPfVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRWLASGPrCGIGEISIPENEPGSSIMPGKVNPTQ 329
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 490363274 330 CEALTMLCAQVMG 342
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
58-394 |
8.92e-116 |
|
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: 342.95 E-value: 8.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 58 VNMDLGLLPKERADAIIAAADEVLAGKHPtefpLAIWQTGSGTQSNMNMNEVLANRGSEILGGIrgmerkihpnddVNKS 137
Cdd:cd01334 14 ALAELGLLPKEAAEAILAALDEILEGIAA----DQVEQEGSGTHDVMAVEEVLAERAGELNGGY------------VHTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 138 QSSNDVFPTaMHVAAVIALRQDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIED 217
Cdd:cd01334 78 RSSNDIVDT-ALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 218 SVPHVCELALGGTAVGTGLNTHPEYAVRVAKRIAElsgqpFVTAPNKFEALATCDALVHSHGALKGLAASLMKIANDVRW 297
Cdd:cd01334 157 ALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 298 LASGprcGIGEISIPEN-EPGSSIMPGKVNPTQCEALTMLCAQVMGNDVAINIGGASGNFELNVYRPMIIDNFLQSVRLL 376
Cdd:cd01334 232 LSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLL 308
|
330
....*....|....*...
gi 490363274 377 ADGMRSFNEHCAiGIEPN 394
Cdd:cd01334 309 DAALRLLTGVLE-GLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
104-384 |
3.09e-64 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 207.08 E-value: 3.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 104 MNMNEVLANRGSEILGGIrgmerkiHPNDDVNKSQSSNDVFPTAMHVAAVIALRqDLLPELKSLLKVFKEKAEAFHDIVK 183
Cdd:cd01594 14 ALVEEVLAGRAGELAGGL-------HGSALVHKGRSSNDIGTTALRLALRDALD-DLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 184 IGRTHLQDATPLTLGQEISGWAAMLEhnikhiedsvphvcelalggtavgtglnthpeyavRVAKRIAELsgqpfvtapn 263
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLG-----------------------------------RDLERLEEA---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 264 kfealatcdALVHSHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPeNEPGSSIMPGKVNPTQCEALTMLCAQVMGN 343
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490363274 344 DVAINIGGASGNFELNVYRPMIIDNFLQSVRLLADGMRSFN 384
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
140-461 |
2.24e-31 |
|
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: 125.20 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 140 SNDVFPTAMhvaaVIALRQ---DLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIE 216
Cdd:COG0015 99 SQDINDTAL----ALQLREaleLLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 217 DSVPHVCELALGGtAVGTgLNTHPEYAVRVAKRIAE---LSGQPFVT--APNKFEAlatcdALVHshgALKGLAASLMKI 291
Cdd:COG0015 175 EARERVLVGKIGG-AVGT-YAAHGEAWPEVEERVAEklgLKPNPVTTqiEPRDRHA-----ELFS---ALALIAGSLEKI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 292 ANDVRWLAsgpRCGIGEIS--IPENEPGSSIMPGKVNPTQCEALTMLCAQVMGndvaiNIGGASGNFELN---------V 360
Cdd:COG0015 245 ARDIRLLQ---RTEVGEVEepFAKGQVGSSAMPHKRNPIDSENIEGLARLARA-----LAAALLEALASWherdlsdssV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 361 YRPMIIDNFlqsvrLLADGM-RSFNEHCAiGIEPNRERINKLLHESLMLV------TALNTH-IG----YDKAAEIAKKA 428
Cdd:COG0015 317 ERNILPDAF-----LLLDGAlERLLKLLE-GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGA 390
|
330 340 350
....*....|....*....|....*....|....*...
gi 490363274 429 HKEGLTLKEsALKLN-----YLTAEEFDSWVRPEDMVG 461
Cdd:COG0015 391 WEEGNDLRE-LLAADpeipaELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
140-429 |
7.44e-28 |
|
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: 114.14 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 140 SNDVFPTAMhvaaVIALRQDL---LPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIE 216
Cdd:cd01595 89 SQDINDTAL----ALQLRDALdiiLPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 217 DSVPHVCELALGGtAVGTGLNTHPEyAVRVAKRIAELSGQPFVTAPNKFEAlatCDALVHSHGALKGLAASLMKIANDVR 296
Cdd:cd01595 165 EARERVLVGGISG-AVGTHASLGPK-GPEVEERVAEKLGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 297 WLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCAQVMGNdvaINIGGASGNFEL-------NVYRPMIID 367
Cdd:cd01595 240 LLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL---AAPALENLVQWHerdlsdsSVERNILPD 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490363274 368 NFlqsvrLLADGMRSFNEHCAIGIEPNRERINKLLHESLMLV------TAL-NTHIGYDKAAEIAKKAH 429
Cdd:cd01595 314 AF-----LLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALaKKGLGRQEAYELVKEEN 377
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
408-459 |
1.67e-26 |
|
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: 101.24 E-value: 1.67e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 490363274 408 LVTALNTHIGYDKAAEIAKKAHKEGLTLKESALKLNYLTAEEFDSWVRPEDM 459
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
151-462 |
2.94e-23 |
|
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: 101.55 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 151 AAVIALRQDL---LPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELAL 227
Cdd:cd01597 106 ALVLQLRDALdllERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 228 GGtAVGTgLNTHPEYAVRVAKRIAELSG-----QPFVTAPNKFEALATCDALVhshgalkglAASLMKIANDVRWLAsgp 302
Cdd:cd01597 186 GG-AAGT-LASLGDQGLAVQEALAAELGlgvpaIPWHTARDRIAELASFLALL---------TGTLGKIARDVYLLM--- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 303 RCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCAQVMGnDVAINIGGASGNFElnvyRP----MIIDNFLQSVRLL 376
Cdd:cd01597 252 QTEIGEVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLDAMVQEHE----RDagawHAEWIALPEIFLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 377 ADGMRSFNEHCAIGIEPNRERINKLLH--------ESLMLvtALNTHIGYDKA----AEIAKKAHKEGLTLKESALK--- 441
Cdd:cd01597 327 ASGALEQAEFLLSGLEVNEDRMRANLDltgglilsEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpe 404
|
330 340
....*....|....*....|..
gi 490363274 442 -LNYLTAEEFDSWVRPEDMVGS 462
Cdd:cd01597 405 vAAYLSDEELDALLDPANYLGS 426
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
140-462 |
3.76e-21 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 95.49 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 140 SNDVFPTAMhvaaVIALRQDL---LPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAA-MLEH--NIK 213
Cdd:TIGR00928 97 SNDIVDTAL----ALLLRDALeiiLPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEeMLRQleRLL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 214 HIEDSVPhvcelaLGGT--AVGTGLNTHPEYAvRVAKRIAELSGQPFVTAPNKFEA----LATCDALVHshgalkgLAAS 287
Cdd:TIGR00928 173 QAKERIK------VGGIsgAVGTHAAAYPLVE-EVEERVTEFLGLKPVPISTQIEPrdrhAELLDALAL-------LATT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 288 LMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCAQVMGNDVAiniggASGN----FELNVY 361
Cdd:TIGR00928 239 LEKFAVDIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASP-----ALENaplwHERDLT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 362 RPMIIDNFLQSVRLLADGMRSFNEHCAIGIEPNRERINK-------LLHESLMLVTALNTHIGYDKAAEIAKK-----AH 429
Cdd:TIGR00928 311 DSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRnldltlgLIASERVLIALVERGMGREEAYEIVRElamgaAE 390
|
330 340 350
....*....|....*....|....*....|....*..
gi 490363274 430 KEGLTLKESALKLN----YLTAEEFDSWVRPEDMVGS 462
Cdd:TIGR00928 391 VDEPDLLEFLLEDEritkYLKEEELAELLDPETYIGN 427
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
140-337 |
1.71e-20 |
|
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: 93.00 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 140 SNDVFPTAMHVAAVIALRQdLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSV 219
Cdd:cd01360 91 SSDVVDTALALQLREALDI-ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEAR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 220 PHVCELALGGtAVGTGLNTHPEYAVRVAK----RIAELSGQpfVTAPNKFEALATcdalvhshgALKGLAASLMKIANDV 295
Cdd:cd01360 170 ERILVGKISG-AVGTYANLGPEVEERVAEklglKPEPISTQ--VIQRDRHAEYLS---------TLALIASTLEKIATEI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490363274 296 RWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLC 337
Cdd:cd01360 238 RHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
139-343 |
2.97e-17 |
|
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: 83.94 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 139 SSNDVFPTAMHvaavIALRQ---DLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHI 215
Cdd:TIGR00838 106 SRNDQVATDLR----LYLRDhvlELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 216 EDSVPHVCELALGGTAV-GTGLNTHPEYavrvakrIAELSGQPFVTApNKFEALATCDALVHSHGALKGLAASLMKIAND 294
Cdd:TIGR00838 182 QDALKRVNVSPLGSGALaGTGFPIDREY-------LAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAED 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490363274 295 VRWLASGPrcgIGEISIP-ENEPGSSIMPGKVNPTQCEALTMLCAQVMGN 343
Cdd:TIGR00838 254 LILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
139-460 |
1.25e-16 |
|
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: 81.82 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 139 SSNDVFPTAMHVAAVIALRqDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDS 218
Cdd:cd01359 86 SRNDQVATDLRLYLRDALL-ELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 219 VPHVCELALGGTA-VGTGLNTHPEyavrvakRIAELSGQPFVTaPNKFEALATCDALVHSHGALKGLAASLMKIANDVRW 297
Cdd:cd01359 165 YKRVNVSPLGAGAlAGTTFPIDRE-------RTAELLGFDGPT-ENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 298 LASGPRcgiGEISIPEN-EPGSSIMPGKVNPTQCEALTMLCAQVMGNDVAI-----NIGGASGNFELNVYRPMI--IDNF 369
Cdd:cd01359 237 WSTQEF---GFVELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLlttlkGLPLAYNKDLQEDKEPLFdaVDTL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 370 LQSVRLLADGMRsfnehcaiGIEPNRERINKLLHESLMLVTAL------NTHI----GYDKAAEIAKKAHKEGLTLKESA 439
Cdd:cd01359 314 IASLRLLTGVIS--------TLTVNPERMREAAEAGFSTATDLadylvrEKGVpfreAHHIVGRAVRLAEEKGKDLSDLT 385
|
330 340
....*....|....*....|....*
gi 490363274 440 L----KLNYLTAEEFDSWVRPEDMV 460
Cdd:cd01359 386 LaelqAISPLFEEDVREALDPENSV 410
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-327 |
2.65e-14 |
|
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: 74.58 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 155 ALRQDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCelaLGGtAVGT 234
Cdd:cd01598 116 ARNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQIEILGK---FNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 235 gLNTH----PEYAVRV-AKRIAE---LSGQPFVT--APNKFEAlATCDALVHSHGALKGLaaslmkiANDVrWlasgprc 304
Cdd:cd01598 192 -FNAHlvayPDVDWRKfSEFFVTslgLTWNPYTTqiEPHDYIA-ELFDALARINTILIDL-------CRDI-W------- 254
|
170 180 190
....*....|....*....|....*....|
gi 490363274 305 giGEISI-------PENEPGSSIMPGKVNP 327
Cdd:cd01598 255 --GYISLgyfkqkvKKGEVGSSTMPHKVNP 282
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
147-437 |
3.62e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 74.28 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 147 AMHVAAVIALRQ--DLL-PELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVC 223
Cdd:PRK09053 111 IIDTGLVLQLRDalDLLePDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 224 ELALGGtAVGTgLNTHPEYAVRVAKRIAE-----LSGQPFVTAPNKFEALATCDALvhshgalkgLAASLMKIANDVRWL 298
Cdd:PRK09053 191 VLQFGG-AAGT-LASLGEQALPVAQALAAelqlaLPALPWHTQRDRIAEFASALGL---------LAGTLGKIARDVSLL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 299 AsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEAL------------TMLCAQVMGNDVAinIGGASGNFelnvyrpm 364
Cdd:PRK09053 260 M---QTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERA--LGGWHAEW-------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 365 iiDNFLQSVRLLADGMRSFNEhCAIGIEPNRERINK--------LLHESLMLvtALNTHIGYDKAAEI----AKKAHKEG 432
Cdd:PRK09053 327 --DTLPELACLAAGALAQMAQ-IVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEG 401
|
....*
gi 490363274 433 LTLKE 437
Cdd:PRK09053 402 RHLRD 406
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
155-327 |
7.19e-12 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 67.08 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 155 ALRQDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDsvphvCELA--LGGtAV 232
Cdd:PRK09285 138 AREEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEA-----VEILgkING-AV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 233 GTgLNTH----PEYA-VRVAKRiaelsgqpFVTAPN-KFEALAT----CDALVHSHGALKGLAASLMKIANDVrWlasgp 302
Cdd:PRK09285 212 GN-YNAHlaayPEVDwHAFSRE--------FVESLGlTWNPYTTqiepHDYIAELFDAVARFNTILIDLDRDV-W----- 276
|
170 180 190
....*....|....*....|....*....|..
gi 490363274 303 rcgiGEIS-------IPENEPGSSIMPGKVNP 327
Cdd:PRK09285 277 ----GYISlgyfkqkTKAGEIGSSTMPHKVNP 304
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
151-342 |
1.33e-11 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 66.19 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 151 AAVIALRQDLLPELKSLLKV---FKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELAL 227
Cdd:cd03302 103 TDLIQIRDALDLILPKLAAVidrLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 228 GGTaVGTG------LNTHPEYAVRVAKRIAELSGQPFV------TAPNKFealatcDALVHShgALKGLAASLMKIANDV 295
Cdd:cd03302 183 KGT-TGTQasfldlFEGDHDKVEALDELVTKKAGFKKVypvtgqTYSRKV------DIDVLN--ALSSLGATAHKIATDI 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490363274 296 RWLAsgprcGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCAQVMG 342
Cdd:cd03302 254 RLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
139-327 |
2.13e-10 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 62.48 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 139 SSNDvfptamHVAAVIALR-----QDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIK 213
Cdd:PRK00855 110 SRND------QVATDLRLYlrdeiDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 214 HIEDSVPHVCELALGGTA-VGTGLNTHPEYavrvakrIAELSGqpF--VTApNKFEALATCDALVHSHGALKGLAASLMK 290
Cdd:PRK00855 184 RLRDARKRVNRSPLGSAAlAGTTFPIDRER-------TAELLG--FdgVTE-NSLDAVSDRDFALEFLSAASLLMVHLSR 253
|
170 180 190
....*....|....*....|....*....|....*....
gi 490363274 291 IAND-VRWlaSGPRCGIgeISIPEN-EPGSSIMPGKVNP 327
Cdd:PRK00855 254 LAEElILW--SSQEFGF--VELPDAfSTGSSIMPQKKNP 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
280-461 |
2.35e-09 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 57.35 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 280 ALKGLAASLMKIANDVRWLAsgpRCGIGEISIP--ENEPGSSIMPGKVNPTQCEALTMLCAQVMGNdVAINIGGASGNFE 357
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIGSERITGLARVLRSY-LVTALENVPLWHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 358 LNVY-----RPMIIDNFlqsvrLLADGMRSFNEHCAIGIEPNRERINK--------LLHESLMLvTALNTHIG----YDK 420
Cdd:PRK08937 98 RDLShssaeRIALPDAF-----LALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHEL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490363274 421 AAEIAKKAHKEGLTLKESALK----LNYLTAEEFDSWVRPEDMVG 461
Cdd:PRK08937 172 IREKAMEAWKNQKDLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
134-336 |
1.07e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 53.52 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 134 VNKSQSSNDVFPTAMhVAAVIALRQDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIK 213
Cdd:PRK05975 102 VHFGATSQDVIDTSL-MLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 214 HIEDSVPHVCELALGGtAVGTGLNTHPEyAVRVAKRIAELSGqpFVTAPnkfEALATCDALVHSHGALKGLAASLMKIAN 293
Cdd:PRK05975 181 RLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--LEDAP---QWHSQRDFIADFAHLLSLVTGSLGKFGQ 253
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490363274 294 DVRWLASGPrcgiGEISIPENePGSSIMPGKVNPTQCEALTML 336
Cdd:PRK05975 254 DIALMAQAG----DEISLSGG-GGSSAMPHKQNPVAAETLVTL 291
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
155-331 |
1.75e-06 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 50.12 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 155 ALRQDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIeDSVPHVCELAlggTAVGT 234
Cdd:PLN02848 141 GVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQL-SEVKIKGKFA---GAVGN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 235 gLNTH----PEYA-VRVAKRIAE---LSGQPFVTAPNKFEALATCDALVHSHGALkglaasLMKIANDVRWLASgprcgI 306
Cdd:PLN02848 217 -YNAHmsayPEVDwPAVAEEFVTslgLTFNPYVTQIEPHDYMAELFNAVSRFNNI------LIDFDRDIWSYIS-----L 284
|
170 180
....*....|....*....|....*...
gi 490363274 307 G---EISIPeNEPGSSIMPGKVNPTQCE 331
Cdd:PLN02848 285 GyfkQITKA-GEVGSSTMPHKVNPIDFE 311
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
158-342 |
3.61e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 49.40 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 158 QDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPH--VCEL---ALGGTAv 232
Cdd:PRK12308 126 QQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRldTCPLgsgALAGTA- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 233 gtglnthpeYAVrvaKRIAELSGQPFVTAP-NKFEALATCDALVHshgaLKGLAASLM----KIANDVRWLASGPRcgiG 307
Cdd:PRK12308 205 ---------YPI---DREALAHNLGFRRATrNSLDSVSDRDHVME----LMSVASISMlhlsRLAEDLIFYNSGES---G 265
|
170 180 190
....*....|....*....|....*....|....*.
gi 490363274 308 EISIPEN-EPGSSIMPGKVNPTQCEALTMLCAQVMG 342
Cdd:PRK12308 266 FIELADTvTSGSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
158-347 |
1.07e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 47.67 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 158 QDLLPELKSLLKVFKEKAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVP--HVCEL---ALGGTAv 232
Cdd:PRK04833 126 AELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKrlDVSPLgsgALAGTA- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 233 gtglnthpeYAV-RVAkrIAELSGqpFVTAP-NKFEALATCDALVHshgALKGLAASLM---KIANDVRWLASGpRCGIG 307
Cdd:PRK04833 205 ---------YEIdREQ--LAGWLG--FASATrNSLDSVSDRDHVLE---LLSDASISMVhlsRFAEDLIFFNSG-EAGFV 267
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490363274 308 EISiPENEPGSSIMPGKVNPTQCEALTMLCAQVMGNDVAI 347
Cdd:PRK04833 268 ELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGM 306
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
185-347 |
5.23e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 45.27 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 185 GRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALG-GTAVGTGLNTHpeyavrvAKRIAELSGQPFVTAPN 263
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGyGSGYGSPSSVK-------FNQMSELLGMEKNIKNP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 264 KFEALATCDALVHSHGALKGLAASLMKIANDvrwLASGPRCGIGEISiPENEPGSSIMPGKVNPTQCEALTMLCAQVMGN 343
Cdd:PRK06389 220 VYSSSLYIKTIENISYLISSLAVDLSRICQD---IIIYYENGIITIP-DEFTTGSSLMPNKRNPDYLELFQGIAAESISV 295
|
....
gi 490363274 344 DVAI 347
Cdd:PRK06389 296 LSFI 299
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
174-342 |
4.37e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 42.91 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 174 KAEAFHDIVKIGRTHLQDATPLTLGQEISGWAAMLEHNIKHIEDSVPHVCELALG-GTAVGTGLNTHPEyavrvakRIAE 252
Cdd:PRK02186 549 KASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGaGAGGGTTFPIDPE-------FVAR 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490363274 253 LSG--QPFvtaPNKFEALATCDALVHSHGALKGLAASLMKIANDVR-WLASGprcgIGEISIPEN-EPGSSIMPGKVNPT 328
Cdd:PRK02186 622 LLGfeQPA---PNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQlWTTRE----FALVSLPDAlTGGSSMLPQKKNPF 694
|
170
....*....|....
gi 490363274 329 QCEALTMLCAQVMG 342
Cdd:PRK02186 695 LLEFVKGRAGVVAG 708
|
|
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