|
Name |
Accession |
Description |
Interval |
E-value |
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
2-434 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 875.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:PRK00485 32 NFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEVIAGKHDDHFPLDVWQTGSGTQSNMNVNEV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:PRK00485 110 IANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERLLPALEHLRDTLAAKAEEFADIVKIGRTHL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:PRK00485 190 QDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPGFAERVAEELAELTGLPFVTAPNKFEALA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PRK00485 270 AHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNDAAVTF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:PRK00485 350 AGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELLERSLMLVTALNPHIGYDKAAKIAKKAH 429
|
410 420 430
....*....|....*....|....*....|....
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 434
Cdd:PRK00485 430 KEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
2-432 |
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: 873.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:COG0114 32 NFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEVIAGKLDDHFPLDVWQTGSGTQTNMNVNEV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:COG0114 110 IANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERLLPALEHLRDTLEAKAEEFADIVKIGRTHL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:COG0114 190 QDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPGFAERVAAELAELTGLPFVSAPNKFEALA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:COG0114 270 AHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMPGKVNPTQCEALTMVCAQVMGNDAAITF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:COG0114 350 AGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELLERSLMLVTALNPHIGYDKAAKIAKKAH 429
|
410 420 430
....*....|....*....|....*....|..
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 432
Cdd:COG0114 430 KEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
1-430 |
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: 858.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 1 MNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNE 79
Cdd:cd01362 27 ENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIAGKLDDHFPLVVWQTGSGTQTNMNVNE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 80 VISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTH 159
Cdd:cd01362 105 VIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPALKHLIDALDAKADEFKDIVKIGRTH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 160 TQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEAL 239
Cdd:cd01362 185 LQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAEKVAAELAELTGLPFVTAPNKFEAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 240 AAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVT 319
Cdd:cd01362 265 AAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEALTMVAAQVMGNDAAIT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 320 VGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTA 399
Cdd:cd01362 345 IAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLERSLMLVTALNPHIGYDKAAKIAKKA 424
|
410 420 430
....*....|....*....|....*....|.
gi 119590499 400 HKNGSTLKETAIELGYLTAEQFDEWVKPKDM 430
Cdd:cd01362 425 HKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
2-433 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 817.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:PLN00134 22 NFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDHFPLVVWQTGSGTQTNMNANEV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:PLN00134 102 IANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELHESLRAKSFEFKDIVKIGRTHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:PLN00134 182 QDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAAAVAEETGLPFVTAPNKFEALA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PLN00134 262 AHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAITV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:PLN00134 342 GGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLMLVTALNPKIGYDKAAAVAKKAH 421
|
410 420 430
....*....|....*....|....*....|...
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 433
Cdd:PLN00134 422 KEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
1-426 |
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: 782.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 1 MNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNE 79
Cdd:cd01596 27 ENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIAGKLDDQFPLDVWQTGSGTSTNMNVNE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 80 VISNRAIEMLGGELGsKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTH 159
Cdd:cd01596 105 VIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 160 TQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEAL 239
Cdd:cd01596 184 LQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEKVAAELAELTGLPFVTAPNLFEAT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 240 AAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVT 319
Cdd:cd01596 264 AAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKVNPVIPEAVNMVAAQVIGNDTAIT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 320 VGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTA 399
Cdd:cd01596 344 MAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENSLMLVTALNPHIGYEKAAEIAKEA 423
|
410 420
....*....|....*....|....*..
gi 119590499 400 HKNGSTLKETAIELGYLTAEQFDEWVK 426
Cdd:cd01596 424 LKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
1-432 |
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: 770.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 1 MNFKIGgvTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNE 79
Cdd:TIGR00979 28 ENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEILAGKLDDHFPLVVWQTGSGTQSNMNVNE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 80 VISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTH 159
Cdd:TIGR00979 106 VIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPALENLKKTLDAKSKEFAHIVKIGRTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 160 TQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEAL 239
Cdd:TIGR00979 186 LQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDEKVAEEIAKETGLPFVTAPNKFEAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 240 AAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVT 319
Cdd:TIGR00979 266 AAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGKVNPTQCEALTMVCVQVMGNDATIG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 320 VGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTA 399
Cdd:TIGR00979 346 FAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNNSLMLVTALNPHIGYDNAAKIAKKA 425
|
410 420 430
....*....|....*....|....*....|...
gi 119590499 400 HKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 432
Cdd:TIGR00979 426 HKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
2-433 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 580.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:PRK12425 30 NFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLDGQHDDQFPLVVWQTGSGTQSNMNVNEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:PRK12425 108 IAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAIAELSGGLAEQSARHAKLVKTGRTHM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:PRK12425 188 MDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAEAIAAELAALSGLPFVTAPNKFAALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PRK12425 268 GHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGKVNPTQCEALSMLACQVMGNDATIGF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:PRK12425 348 AASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLERGLMLVTALNPHIGYDKAAEIAKKAY 427
|
410 420 430
....*....|....*....|....*....|...
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 433
Cdd:PRK12425 428 AEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
2-434 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 564.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:COG1027 28 NFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIAGKLHDQFVVDVIQGGAGTSTNMNANEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:COG1027 108 IANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:COG1027 187 QDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYIELVVEHLAEITGLPLVRAENLIEATQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:COG1027 267 DTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTVTM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:COG1027 347 AAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVENSIGLVTALNPYIGYEKAAEIAKEAL 426
|
410 420 430
....*....|....*....|....*....|....
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 434
Cdd:COG1027 427 ATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
2-434 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 537.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:PRK12273 33 NFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDEILAGKLHDQFVVDVIQGGAGTSTNMNANEV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:PRK12273 113 IANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:PRK12273 192 QDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPPGYIELVVEKLAEITGLPLVPAEDLIEATQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PRK12273 272 DTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:PRK12273 352 AAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREYVENSIGIVTALNPYIGYENAAEIAKEAL 431
|
410 420 430
....*....|....*....|....*....|....
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 434
Cdd:PRK12273 432 ETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
1-423 |
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: 534.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 1 MNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNE 79
Cdd:cd01357 27 ENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIAGKLHDQFVVDVIQGGAGTSTNMNANE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 80 VISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTH 159
Cdd:cd01357 105 VIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLAL-ILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 160 TQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEAL 239
Cdd:cd01357 184 LQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIELVVEKLSEITGLPLKRAENLIDAT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 240 AAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVT 319
Cdd:cd01357 264 QNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTIT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 320 VGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTA 399
Cdd:cd01357 344 MAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENSIGIVTALNPYIGYEAAAEIAKEA 423
|
410 420
....*....|....*....|....
gi 119590499 400 HKNGSTLKETAIELGYLTAEQFDE 423
Cdd:cd01357 424 LETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
2-434 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 520.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:PRK13353 33 NFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACDEILAGKLHDQFIVDPIQGGAGTSTNMNANEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:PRK13353 111 IANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG-LLAAMGALQDVFEEKAAEFDHVIKMGRTQL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:PRK13353 190 QDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYIERVVKHLAAITGLPLVGAEDLVDATQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PRK13353 270 NTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:PRK13353 350 AAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVEKSVGIATALNPHIGYEAAARIAKEAI 429
|
410 420 430
....*....|....*....|....*....|....
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 434
Cdd:PRK13353 430 ATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
2-433 |
3.61e-139 |
|
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: 406.52 E-value: 3.61e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE-GKLNDHFPLVVWQTGSGTQTNMNVNE 79
Cdd:TIGR00839 28 NFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILNnGKCHDQFPVDVYQGGAGTSVNMNTNE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 80 VISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTH 159
Cdd:TIGR00839 108 VIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAV-YSSLIKLVDAINQLRDGFEQKAKEFADILKMGRTQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 160 TQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEAL 239
Cdd:TIGR00839 187 LQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEYSPLVVKKLAEVTGLPCVPAENLIEAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 240 AAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVT 319
Cdd:TIGR00839 267 SDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 320 VGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTA 399
Cdd:TIGR00839 347 LAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYVFNSIGIVTYLNPFIGHHNGDIVGKIC 426
|
410 420 430
....*....|....*....|....*....|....
gi 119590499 400 HKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 433
Cdd:TIGR00839 427 AETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
1-313 |
1.04e-137 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 397.12 E-value: 1.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 1 MNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANAIMKAADEVAE-GKLNDHFPLVVWQTGSGTQTNMNVNE 79
Cdd:pfam00206 20 FNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQFPLKVWQEGSGTAVNMNLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 80 VISnraiEMLGgelgskIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTH 159
Cdd:pfam00206 90 VIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKEKAKEFADIVKPGRTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 160 TQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPR-IYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPfVTAPNKFEA 238
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAKELGFFTGLP-VKAPNSFEA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119590499 239 LAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMG 313
Cdd:pfam00206 239 TSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
2-433 |
3.00e-132 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 389.36 E-value: 3.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 2 NFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEV 80
Cdd:PRK14515 39 NFPITGY--KIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQEILDGKWHDHFIVDPIQGGAGTSMNMNANEV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 81 ISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHT 160
Cdd:PRK14515 117 IANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALA 240
Cdd:PRK14515 196 QDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIEAVVKHLAAISELPLVGAEDLVDATQ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 241 AHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PRK14515 276 NTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 321 GGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAH 400
Cdd:PRK14515 356 ASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEKSVGIITAVNPHIGYEAAARVAKEAI 435
|
410 420 430
....*....|....*....|....*....|...
gi 119590499 401 KNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 433
Cdd:PRK14515 436 ATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
17-365 |
5.16e-123 |
|
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: 359.89 E-value: 5.16e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 17 IKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFplvvWQTGSGTQTNMNVNEVISNRAIEMlggelgs 95
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 96 kipvhpNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGY 175
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 176 VQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAkvaaLTGLpFVTAPNKFEALAAHDALVELSGAMNTT 255
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAE----LLGF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 256 ACSLMKIANDIRFLGSGprsGLGELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKP 334
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 119590499 335 MMIKNVLHSARLLGDASVSFTENCvVGIQAN 365
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
75-355 |
7.29e-65 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 207.85 E-value: 7.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 75 MNVNEVISNRAIEMLGGELGSKipvhpndHVNKSQSSNDtFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIK 154
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 155 IGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyelaaggtavgtglntrigfaekvaakvaaltglpfvtapn 234
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 235 kfealaahdALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPeNEPGSSIMPGKVNPTQCEAMTMVAAQVMGN 314
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119590499 315 HVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFT 355
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
379-430 |
6.07e-28 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 104.71 E-value: 6.07e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119590499 379 LVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 430
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
126-432 |
3.94e-26 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 109.40 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 126 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 205
Cdd:COG0015 113 EALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 206 GLNtrigfaekvaakvaaltglpFVTAPNKFEALAA----------------HDALVELSGAMNTTACSLMKIANDIRFL 269
Cdd:COG0015 192 YAA--------------------HGEAWPEVEERVAeklglkpnpvttqiepRDRHAELFSALALIAGSLEKIARDIRLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 270 GsgpRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGN--HVAVTV------GGSNGHFELNVFkPMMIkn 339
Cdd:COG0015 252 Q---RTEVGEVeePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaaALLEALaswherDLSDSSVERNIL-PDAF-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 340 vlhsarLLGDASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IG----YDKAAKIAKTAHKNGSTLKE 408
Cdd:COG0015 326 ------LLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRE 399
|
330 340
....*....|....*....|....*....
gi 119590499 409 tAIE-----LGYLTAEQFDEWVKPKDMLG 432
Cdd:COG0015 400 -LLAadpeiPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
126-400 |
7.60e-25 |
|
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176467 [Multi-domain] Cd Length: 381 Bit Score: 105.28 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 126 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 205
Cdd:cd01595 103 DALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 206 GLNtrigFAEKVAAKVAALT---GLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLGELIL 282
Cdd:cd01595 182 HAS----LGPKGPEVEERVAeklGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 283 P--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvavtvggsnghfelnvFKPMMIKNVL-------HSA--RLLG--- 348
Cdd:cd01595 252 PfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL-----------------AAPALENLVQwherdlsDSSveRNILpda 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119590499 349 ----DASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IGYDKAAKIAKTAH 400
Cdd:cd01595 315 flllDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
126-432 |
2.78e-22 |
|
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.
Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 98.47 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 126 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 205
Cdd:cd01597 113 DALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 206 -------GLNTRIGFaekvaakvAALTGLPFVTAPnkfeALAAHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLG 278
Cdd:cd01597 192 laslgdqGLAVQEAL--------AAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 279 ELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGnHVAVTV---------GGSNGHFELNVFKPMMIknvlhsarlL 347
Cdd:cd01597 257 EVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLdamvqeherDAGAWHAEWIALPEIFL---------L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 348 GDASVSFTENCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKA----AKIAKTAHKNGSTLKETAIE--- 412
Cdd:cd01597 327 ASGALEQAEFLLSGLEVNEDRMRAnldltgglILSEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpe 404
|
330 340
....*....|....*....|.
gi 119590499 413 -LGYLTAEQFDEWVKPKDMLG 432
Cdd:cd01597 405 vAAYLSDEELDALLDPANYLG 425
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
104-432 |
5.83e-22 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 97.42 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 104 HVNKSQSSNDTFPTAMHIAAAiEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAM 183
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLLR-DALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 184 TRIKAAMPRIYELAAGGtAVGTGLNTRIGFAEKVAAKVAALtGLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIA 263
Cdd:TIGR00928 169 ERLLQAKERIKVGGISG-AVGTHAAAYPLVEEVEERVTEFL-GLKPVPISTQIEP---RDRHAELLDALALLATTLEKFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 264 NDIRFLgsgPRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAaqVMGNHVAVTVGGSNGH-FELNVFKPMMIKNV 340
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVeePFGKGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLwHERDLTDSSVERVI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 341 LHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHI-------GYDKAAKIAK-----TAHKNGSTLKE 408
Cdd:TIGR00928 319 LPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRelamgAAEVDEPDLLE 398
|
330 340
....*....|....*....|....*...
gi 119590499 409 TAIELG----YLTAEQFDEWVKPKDMLG 432
Cdd:TIGR00928 399 FLLEDEritkYLKEEELAELLDPETYIG 426
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
111-308 |
3.76e-15 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 76.44 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 111 SNDTFPTA--MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKA 188
Cdd:cd01360 91 SSDVVDTAlaLQLREALDI---ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 189 AMPRIYELAAGGtAVGTGLNtrIGFAEKVAAKVAAltGLPFVTAPNKfeaLAAHDALVELSGAMNTTACSLMKIANDIRF 268
Cdd:cd01360 168 ARERILVGKISG-AVGTYAN--LGPEVEERVAEKL--GLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRH 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119590499 269 LgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVA 308
Cdd:cd01360 240 L---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
39-427 |
2.60e-14 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 74.31 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 39 KIANAIMKAADEVAEGKLNDHFPLvvwqtgsgtqtnMNVNEVISNRAIEMLGGELGSKIpvhpndHVNKSQssNDTFPTA 118
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGKL------HTGRSR--NDQVATD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 119 MHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 198
Cdd:TIGR00838 115 LRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 199 GGTAV-GTGLntrigfaEKVAAKVAALTGLPFVTApNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 277
Cdd:TIGR00838 194 GSGALaGTGF-------PIDREYLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---F 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 278 GELILP-ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVtvggsnghfelnvfkpMMIKNVLHSA---------RLL 347
Cdd:TIGR00838 263 GFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM----------------LMTLKALPLAynrdlqedkEPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 348 GDAsVSFTENCV-------VGIQANTERINKLMNESLMLVTALNPHI---------GYDKAAKIAKTAHKNGSTLKETAI 411
Cdd:TIGR00838 327 FDA-LKTVELSLematgmlDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHHIVGELVATAIERGKGLEELTL 405
|
410
....*....|....*.
gi 119590499 412 ELGYLTAEQFDEWVKP 427
Cdd:TIGR00838 406 EELQKFSPEFDEDVYE 421
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
129-432 |
6.75e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 63.88 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 129 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT--G 206
Cdd:PRK09053 125 DLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGTlaS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 207 LNTRigfaekvaakvaaltglpfvtAPNKFEALAA-----------H---DALVELSGAMNTTACSLMKIANDIRFLgsg 272
Cdd:PRK09053 204 LGEQ---------------------ALPVAQALAAelqlalpalpwHtqrDRIAEFASALGLLAGTLGKIARDVSLL--- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 273 PRSGLGELILP--ENEPGSSIMPGKVNPTQCEAM------------TMVAAQVMGNHVAvtVGGsnGHFELNVFKPMmik 338
Cdd:PRK09053 260 MQTEVGEVFEPaaAGKGGSSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERA--LGG--WHAEWDTLPEL--- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 339 nvlhsARLLGDAsVSFTENCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKAAKI----AKTAHKNGSTL 406
Cdd:PRK09053 333 -----ACLAAGA-LAQMAQIVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAHHLveqaSKRAVAEGRHL 404
|
330 340 350
....*....|....*....|....*....|
gi 119590499 407 K----ETAIELGYLTAEQFDEWVKPKDMLG 432
Cdd:PRK09053 405 RdvlaEDPQVSAHLSPAALDRLLDPAHYLG 434
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
118-298 |
1.86e-10 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 62.25 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 118 AMHIAAAIevHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKaampRIYELA 197
Cdd:cd01598 110 ALMIKEAR--NEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK----QIEILG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 198 AGGTAVGT------------------GLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAM---NTTa 256
Cdd:cd01598 184 KFNGAVGNfnahlvaypdvdwrkfseFFVTSLG-----------LTWNPYTT------QIEPHDYIAELFDALariNTI- 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119590499 257 csLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 298
Cdd:cd01598 246 --LIDLCRDIwgyislGYFKQKVKKG---------EVGSSTMPHKVNP 282
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
129-313 |
2.93e-09 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 58.87 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 129 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTaVGTG-- 206
Cdd:cd03302 113 DLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQas 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 207 --------------LNTRI----GFaekvaAKVAALTGLpfvTAPNKFEALAAhDALVELsGAmnttacSLMKIANDIRF 268
Cdd:cd03302 192 fldlfegdhdkveaLDELVtkkaGF-----KKVYPVTGQ---TYSRKVDIDVL-NALSSL-GA------TAHKIATDIRL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 119590499 269 LgsgprSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMG 313
Cdd:cd03302 256 L-----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
118-298 |
2.98e-09 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 58.61 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 118 AMHIAAAIEvhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyELA 197
Cdd:PRK09285 132 ALMLKEARE--EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EIL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 198 A--GGtAVGTgLN-------------------TRIGfaekvaakvaaLTGLPFVTA--PnkfealaaHDALVELSGAM-- 252
Cdd:PRK09285 205 GkiNG-AVGN-YNahlaaypevdwhafsrefvESLG-----------LTWNPYTTQieP--------HDYIAELFDAVar 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 119590499 253 -NTtacSLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 298
Cdd:PRK09285 264 fNT---ILIDLDRDVwgyislGYFKQKTKAG---------EIGSSTMPHKVNP 304
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
41-320 |
4.84e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 41 ANAIMKAADEVAEGKLNDHFplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvhpndHVNKSQssNDTFPT--A 118
Cdd:PLN02646 70 RDSILDGLDEIEKEIEAGKF---EWRPD-----REDVHMNNEARLTELIG-EPAKKL------HTARSR--NDQVATdtR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 119 MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 198
Cdd:PLN02646 133 LWCRDAIDV---IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 199 GGTAV-GTGLntriGFAEKVAAKVAALTGLpfvtAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 277
Cdd:PLN02646 210 GSCALaGTGL----PIDRFMTAKDLGFTAP----MRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---F 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 119590499 278 GELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PLN02646 279 GFVTPSDAvSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLA 322
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
21-383 |
3.98e-08 |
|
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.
Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 55.25 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 21 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGSGtqtnmNVNEVISNRAIEMLGgELGSKIpvh 100
Cdd:cd01359 27 GILTEEEAA---------KILAGLAKIRAEIEAGAF-------ELDPEDE-----DIHMAIERRLIERIG-DVGGKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 101 pndHVNKSqsSNDTFPTAMHIAAAIEVhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVK 180
Cdd:cd01359 82 ---HTGRS--RNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 181 YAMTRIKAAMPRIYELAAGGTA-VGTGLN-------TRIGFAEKvaakvaaltglpfvtAPNKFEALAAHDALVELSGAM 252
Cdd:cd01359 156 RDLERLADAYKRVNVSPLGAGAlAGTTFPidrertaELLGFDGP---------------TENSLDAVSDRDFVLEFLSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 253 NTTACSLMKIANDIRFLGSGPRsGLGELilpeneP-----GSSIMPGKVNPTQCEAMTMVAAQVMGNHVAV--TVGG--S 323
Cdd:cd01359 221 ALLMVHLSRLAEDLILWSTQEF-GFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLltTLKGlpL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119590499 324 NGHFELNVFKPMM---IKNVLHSARLLGDasvsftenCVVGIQANTERINKLMNESLMLVTAL 383
Cdd:cd01359 294 AYNKDLQEDKEPLfdaVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
91-302 |
1.38e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 50.55 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 91 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 170
Cdd:PRK12308 97 GDLGKKL------HTGRSR--NDQVATDLKLWCRQQGQQLLL-ALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 171 EFSGYVQQVKYAMTRIKAAMPRIYELAAG-GTAVGTGLntrigfaekVAAKVAALTGLPFVTAP-NKFEALAAHDALVEL 248
Cdd:PRK12308 168 WCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTAY---------PIDREALAHNLGFRRATrNSLDSVSDRDHVMEL 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 119590499 249 SGAMNTTACSLMKIANDIRFLGSGpRSGLGEliLPEN-EPGSSIMPGKVNPTQCE 302
Cdd:PRK12308 239 MSVASISMLHLSRLAEDLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALE 290
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
258-432 |
4.61e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 47.33 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 258 SLMKIANDIRFLgSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvAVTVGGSNGH-FELNVFKPMM 336
Cdd:PRK08937 29 SLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY--LVTALENVPLwHERDLSHSSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 337 IKNVLHSARLLGDASVSFTENCVVGIQANTERINK--------LMNESLMLvTALNPHIG----YDKAAKIAKTAHKNGS 404
Cdd:PRK08937 106 ERIALPDAFLALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|..
gi 119590499 405 TLKETAIE----LGYLTAEQFDEWVKPKDMLG 432
Cdd:PRK08937 185 DLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
127-302 |
8.81e-06 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 47.81 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 127 VHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSgyvqQVKYAMTRIKAAMP--RIYELAAGGT--- 201
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMA----NFAYRLSRQRKQLSevKIKGKFAGAVgny 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 202 -------------AVGTGLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAMNTTACSLMKIANDIRF 268
Cdd:PLN02848 218 nahmsaypevdwpAVAEEFVTSLG-----------LTFNPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRDIWS 280
|
170 180 190
....*....|....*....|....*....|....
gi 119590499 269 LGSgprSGLGELILPENEPGSSIMPGKVNPTQCE 302
Cdd:PLN02848 281 YIS---LGYFKQITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
21-298 |
3.65e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 45.91 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 21 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvH 100
Cdd:PRK00855 51 GILSEEEAE---------KILAGLDEILEEIEAGKF-------EFSPE-----LEDIHMAIEARLTERIG-DVGGKL--H 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 101 P----NDHVnksqssndtfPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYV 176
Cdd:PRK00855 107 TgrsrNDQV----------ATDLRLYLRDEIDEIAE-LLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 177 QQVKYAMTRIKAAMPRIYELAAGGTA-VGTGLNT-------RIGFAEkvaakvaaltglpfVTApNKFEALAAHDALVEL 248
Cdd:PRK00855 176 EMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIdrertaeLLGFDG--------------VTE-NSLDAVSDRDFALEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 119590499 249 SGAMNTTACSLMKIANDIrFLGSGPRSGLGELilpeneP-----GSSIMPGKVNP 298
Cdd:PRK00855 241 LSAASLLMVHLSRLAEEL-ILWSSQEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
91-320 |
1.52e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 43.82 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 91 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 170
Cdd:PRK04833 97 GDLGKKL------HTGRSR--NDQVATDLKLWCKDQVAE-LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 171 EFSGYVQQVKYAMTRIKAAMPR--IYELAAGGTAvGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAA 241
Cdd:PRK04833 168 WCLAYVEMLARDESRLQDALKRldVSPLGSGALA-GTAyeidreqLAGWLGFASATR---------------NSLDSVSD 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119590499 242 HDALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGELIlPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 320
Cdd:PRK04833 232 RDHVLELLSDASISMVHLSRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLM 308
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
103-317 |
4.48e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 42.35 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 103 DHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYA 182
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRL-KAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 183 MTRIKAAMPRIYELAAGGtAVGTgLNTRIGFAEKVAAKVAALTGLPfvTAPnkfEALAAHDALVELSGAMNTTACSLMKI 262
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLGKF 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119590499 263 ANDIRFLgsgprSGLGELILPENEPGSSIMPGKVNPTQCEAMTMV----AAQVMGNHVA 317
Cdd:PRK05975 252 GQDIALM-----AQAGDEISLSGGGGSSAMPHKQNPVAAETLVTLarfnATQVSGLHQA 305
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
161-313 |
4.47e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 39.45 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 161 QDAVPLTLGQefsgYVQQVKYAMTRIKAAMPRIYE------LAAGGTAvGTGLNTRIGFAEKVaakvaaltgLPFVT-AP 233
Cdd:PRK02186 565 QPALPGSLGH----YLLAVDGALARETHALFALFEhidvcpLGAGAGG-GTTFPIDPEFVARL---------LGFEQpAP 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590499 234 NKFEALAAHDALVELSGAMNTTACSLMKIANDIRfLGSGPRSGLgeLILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVM 312
Cdd:PRK02186 631 NSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQ-LWTTREFAL--VSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVA 707
|
.
gi 119590499 313 G 313
Cdd:PRK02186 708 G 708
|
|
| |
