|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
1-453 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 978.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 1 MALWGGRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNPELIIASG 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 81 AEDIHSFVEQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 161 QPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 241 DASISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 321 MQEDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQT 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 527111731 401 PLEDLPLEELQSFSAIIEADVYECLTIESCLAKREALGGTSLPQVKSALAGKQ 453
Cdd:PRK04833 401 PLEDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAK 453
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
1-449 |
0e+00 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 814.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 1 MALWGGRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNPELIIASG 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 81 AEDIHSFVEQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 161 QPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 241 DASISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 321 MQEDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQT 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 527111731 401 PLEDLPLEELQSFSAIIEADVYECLTIESCLAKREALGGTSLPQVKSAL 449
Cdd:PRK12308 401 ALEELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAV 449
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
1-450 |
0e+00 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 724.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 1 MALWGGRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNpELIIASG 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAG-AFEFDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 81 AEDIHSFVEQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRA 160
Cdd:COG0165 82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 161 QPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 241 DASISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 321 MQEDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQT 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 527111731 401 PLEDLPLEELQSFSAIIEADVYECLTIESCLAKREALGGTSLPQVKSALA 450
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIA 451
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
1-450 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 694.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 1 MALWGGRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNpELIIASG 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAG-KFEFSPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 81 AEDIHSFVEQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRA 160
Cdd:PRK00855 83 LEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 161 QPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 241 DASISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 321 MQEDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQT 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 527111731 401 PLEDLPLEELQSFSAIIEADVYECLTIESCLAKREALGGTSLPQVKSALA 450
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIA 452
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
3-450 |
0e+00 |
|
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: 662.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 3 LWGGRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNPeLIIASGAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGP-FILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 83 DIHSFVEQSLIAKVG-DLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 162 PVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICSD 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 242 ASISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 322 QEDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQTP 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 527111731 402 LEDLPLEELQSFSAIIEADVYECLTIESCLAKREALGGTSLPQVKSALA 450
Cdd:TIGR00838 400 LEELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIA 448
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
22-450 |
0e+00 |
|
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: 637.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 22 SLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETStNPELIIASGAEDIHSFVEQSLIAKVGDLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIE-AGAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 102 KLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDIS 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 182 RLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICSDASISMMHLSRMAEDLIFFNS 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 262 GEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKDMQEDKEGLFDVMDSWAICLEM 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 342 AALVLSGLQVNRERTLSAAQQGYANSTELADYLVA-KGMPFREAHHVVGEAVVNAIAKQTPLEDLPLEELQSFSAIIEAD 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|
gi 527111731 421 VYECLTIESCLAKREALGGTSLPQVKSALA 450
Cdd:cd01359 400 VREALDPENSVERRTSYGGTAPAEVREQIA 429
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-450 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 543.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 3 LWGGRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNpELIIASGAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAG-KFEWRPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 83 DIHSFVEQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 163 VLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICSDA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 243 SISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 323 EDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQTPL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 527111731 403 EDLPLEELQSFSAIIEADVYECLTIESCLAKREALGGTSLPQVKSALA 450
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLE 464
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
30-352 |
1.52e-124 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 364.90 E-value: 1.52e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 30 IEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETStNPELIIASGAEDIHSFVEQSLIAKVGDL-GKKLHTGRS 108
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIA-ADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 109 RNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALK 188
Cdd:cd01334 80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 189 RADTCPLGTGALAGTAY--PMDRVKLAQSLGFASPTLNSLDTVSDRDHVVEICSDASISMMHLSRMAEDLIFFNSGEAGF 266
Cdd:cd01334 160 RLNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 267 IELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKDMQEDKEGLFDVMDSWAICLEMAALVL 346
Cdd:cd01334 240 VELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319
|
....*.
gi 527111731 347 SGLQVN 352
Cdd:cd01334 320 EGLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
8.37e-102 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 306.60 E-value: 8.37e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 6 GRFSQESSALFKLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDECTQLHAALNELLAETSTNPELIIASGAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 86 SFVEQSLIAKVGDL-------GKKLHTGRSRNDQVATDLKLWCKKEGQELLE-LLGKLRTALIELAEREIDAVMPGYTHL 157
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALSEVLLpALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 158 QRAQPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDR---VKLAQSLGF----ASPTLNSLDTVS 230
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPefaELVAKELGFftglPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527111731 231 DRDHVVEICSDASISMMHLSRMAEDLIFFNSGEAGFIELDD-EVTSGSSLMPQKKNPDALELIRGKTGRVYG 301
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLaEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
88-397 |
3.30e-60 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 211.24 E-value: 3.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 88 VEQSLIAKVG-DLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFG 166
Cdd:PRK02186 494 YEAYLIERLGeDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 167 HWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDRDHVVE-ICSDASIS 245
Cdd:PRK02186 574 HYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHfLSAMAAIS 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 246 MMhLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPlaYNKDMQEDK 325
Cdd:PRK02186 654 TV-LSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGS 730
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527111731 326 EGLFDVMDSWAICLEMAA---LVLSGLQVNRERTLSAAQQGYANSTELADYLVA-KGMPFREAHHVVGEAVVNAIA 397
Cdd:PRK02186 731 PMNGPIAQACAAIEDAAAvlvLLIDGLEADQARMRAHLEDGGVSATAVAESLVVrRSISFRSAHTQVGQAIRQSLD 806
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
88-343 |
1.70e-56 |
|
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: 187.05 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 88 VEQSLIAKVGDLGKKLH------TGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQ 161
Cdd:cd01594 16 VEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 162 PVLFGHWCLAYVEMFERDISRLQDAlkradtcplgtgalagtaypmdrvklaqslgfasptlnsldtvsdrdHVVEICSD 241
Cdd:cd01594 96 PVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALDA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 242 ASISMMHLSRMAEDLIFFNSGEAGFIELDDEV-TSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKALPLAYNKD 320
Cdd:cd01594 129 LALAAAHLSKIAEDLRLLLSGEFGELGEPFLPgQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNED 208
|
250 260
....*....|....*....|...
gi 527111731 321 MQEDKEGLFDVMDSWAICLEMAA 343
Cdd:cd01594 209 SPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
74-441 |
3.38e-46 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 167.08 E-value: 3.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 74 ELIIASGAEDIHSFVEQSLIAKVG-DLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMP 152
Cdd:PRK06705 80 QLLYTEQHEDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 153 GYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLDTVSDR 232
Cdd:PRK06705 160 AYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 233 DHVVEICSDASISMMHLSRMAEDLIFFNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKA 312
Cdd:PRK06705 240 DYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 313 LPLAYNKDMQEDKEG-LFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYLVAK-GMPFREAHHVVGE 390
Cdd:PRK06705 320 TPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKRRSYKHAITITDFADVLTKNyGIPFRHAHHAASV 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 527111731 391 AVVNAIAKQTPLEDLPLEELQSF------SAIIEADVYECLTIESCLAKREALGGTS 441
Cdd:PRK06705 400 IANMSLEQKKELHELCFKDVNIYlqekfkIQLLEKEWEEIISPEAFIQKRNVYGGPS 456
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-394 |
6.41e-35 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 135.02 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 1 MALWGGRFSQESSALF--KLFNDSLPVDYRLIEQDIIGSIAWASAITQVGVLTTDE-CTQLHAALNELLAETSTNPELii 77
Cdd:PRK06389 1 MKIWSGGAGEELENDFydNIVKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKApKCVINALIDIYKNGIEIDLDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 78 asgaEDIHSFVEQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWckkegqeLLELLGKLRTALIELAEREIDA----VMPG 153
Cdd:PRK06389 79 ----EDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLF-------IIDKIIEIEKILYEIIKVIPGFnlkgRLPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 154 YTHLQRAQPVLFGHWcLAYVE-MFERDISRLQDALKRADTCPLGTGALAGTAYPMDRVKLAQSLGFA----SPTLNSLDT 228
Cdd:PRK06389 148 YTHFRQAMPMTVNTY-INYIKsILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEknikNPVYSSSLY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 229 VSDrdhVVEICSDASISMMHLSRMAEDLIffNSGEAGFIELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILT 308
Cdd:PRK06389 227 IKT---IENISYLISSLAVDLSRICQDII--IYYENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 309 TMKALPLAYNKDMQEDKEGLFDVMDSWAICLEMAALVLSGLQVNRERTLSAAQQGYANSTELADYlvAKGMPFREAHHVV 388
Cdd:PRK06389 302 SELNKTTGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITNEKNIKNSVYATYNAWLAF--KNGMDWKSAYAYI 379
|
....*.
gi 527111731 389 GEAVVN 394
Cdd:PRK06389 380 GNKIRE 385
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
1.18e-30 |
|
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of argininosuccinate lyase.
Pssm-ID: 464268 [Multi-domain] Cd Length: 68 Bit Score: 112.90 E-value: 1.18e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527111731 364 YANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQTPLEDLPLEELQSFSAIIEADVYECLTIESCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
39-409 |
3.43e-29 |
|
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: 118.89 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 39 AWASAITQVGVLTTDECTQLHAA-------LNELLAETSTNPELIIAsgaedihsFVEQsLIAKVGD-LGKKLHTGRSRN 110
Cdd:cd01597 30 ALARAQAELGVIPKEAAAEIAAAadverldLEALAEATARTGHPAIP--------LVKQ-LTAACGDaAGEYVHWGATTQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 111 DQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALKRA 190
Cdd:cd01597 101 DIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 191 DTCPL----GTGALAGTAYPMDRVKLAQSLGFASPTLNSLdtvSDRDHVVEICSdaSISMMH--LSRMAEDLIFFNSGEA 264
Cdd:cd01597 181 LVVQFggaaGTLASLGDQGLAVQEALAAELGLGVPAIPWH---TARDRIAELAS--FLALLTgtLGKIARDVYLLMQTEI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 265 GfielddEVTS-------GSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMKalplaynkdmQEDKEGLFDVMDSWAI 337
Cdd:cd01597 256 G------EVAEpfakgrgGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMV----------QEHERDAGAWHAEWIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 338 CLEMAAL----------VLSGLQVNRERTLS--AAQQGYANStELADYLVAKGMPFREAHHVVGEAVVNAIAKQTPLEDL 405
Cdd:cd01597 320 LPEIFLLasgaleqaefLLSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREV 398
|
....
gi 527111731 406 PLEE 409
Cdd:cd01597 399 LLED 402
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
38-388 |
1.90e-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: 107.21 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 38 IAWASAITQVGVLTTDECTQLHAALN------ELLAEtstnpelIIASGAEDIHSFVEQsLIAKVGDLGKK-LHTGRSRN 110
Cdd:cd01595 19 AALAEAQAELGLIPKEAAEEIRAAADvfeidaERIAE-------IEKETGHDVIAFVYA-LAEKCGEDAGEyVHFGATSQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 111 DQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALKRA 190
Cdd:cd01595 91 DINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 191 DTC----PLGTGALAGTAYPMDRVKLAQSLGFASPTLNSLdtVSDRDHVVEICSdaSISMMH--LSRMAEDLIFFNSGEA 264
Cdd:cd01595 171 LVGgisgAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQ--IEPRDRIAELLS--ALALIAgtLEKIATDIRLLQRTEI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 265 GFIEL---DDEVtsGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTMkALPLaynkdmqedkEGlfDVMDS---WAIC 338
Cdd:cd01595 247 GEVEEpfeKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWH----------ER--DLSDSsveRNIL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527111731 339 LEM-----AAL-----VLSGLQVNRERTLS-AAQQGYANSTE---LAdyLVAKGMPFREAHHVV 388
Cdd:cd01595 312 PDAfllldAALsrlqgLLEGLVVNPERMRRnLDLTWGLILSEavmMA--LAKKGLGRQEAYELV 373
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
128-405 |
2.35e-22 |
|
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: 99.00 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 128 LLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALKRADTCPLG--TGALA--GT 203
Cdd:COG0015 118 LLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGgaVGTYAahGE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 204 AYPMDRVKLAQSLGFASptlNSLDT-VSDRDHVVEICSDASISMMHLSRMAEDLIFFNSGEAGFIElddEVTS----GSS 278
Cdd:COG0015 198 AWPEVEERVAEKLGLKP---NPVTTqIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEVGEVE---EPFAkgqvGSS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 279 LMPQKKNPDALELIRGKTGRVYGSLIGILTTMkalplaynkdMQEDkEGlfDVMDS---WAICLEMAAL----------V 345
Cdd:COG0015 272 AMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWH-ER--DLSDSsveRNILPDAFLLldgalerllkL 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527111731 346 LSGLQVNRERTLS--AAQQGYANSTELADYLVAKGMPFREAHHVVGEAVVNAIAKQTPLEDL 405
Cdd:COG0015 339 LEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-292 |
8.18e-17 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 82.34 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 106 GRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQD 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 186 ALKRADTCPL-----GTGALAGTAYpMDRV--KLAQSLGFA-SPTLNSLDTVSDRDHVVEICSDASISMMHLSRMAEDLI 257
Cdd:PRK13353 218 AREHLYEVNLggtavGTGLNADPEY-IERVvkHLAAITGLPlVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190
....*....|....*....|....*....|....*..
gi 527111731 258 FFNSG-EAGFIELD-DEVTSGSSLMPQKKNPDALELI 292
Cdd:PRK13353 297 LLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVV 333
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-286 |
2.41e-15 |
|
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: 77.95 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 106 GRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQD 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 186 ALKRADTCPL-----GTGALAGTAYpMDRV--KLAQSLGF---ASPTLnsLDTVSDRDHVVEICSDASISMMHLSRMAED 255
Cdd:cd01357 213 ARERLREVNLggtaiGTGINAPPGY-IELVveKLSEITGLplkRAENL--IDATQNTDAFVEVSGALKRLAVKLSKIAND 289
|
170 180 190
....*....|....*....|....*....|...
gi 527111731 256 LIFFNSG-EAGFIELD-DEVTSGSSLMPQKKNP 286
Cdd:cd01357 290 LRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNP 322
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
83-388 |
2.70e-15 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 77.21 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 83 DIHSFVeQSLIAKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQP 162
Cdd:cd01360 66 DVIAFV-TAIAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 163 VLFGH-WCLAYVEMfERDISRLQDALKRADTC----PLGTGALAGtayPMDRVKLAQSLGFASPTLNSldTVSDRDHVVE 237
Cdd:cd01360 145 TTFGLkFALWYAEF-KRHLERLKEARERILVGkisgAVGTYANLG---PEVEERVAEKLGLKPEPIST--QVIQRDRHAE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 238 ICSDASISMMHLSRMAEDLIFFNSGEAGfiELDDEVTS---GSSLMPQKKNPDALELIRGkTGRVYGSLigILTTMKALP 314
Cdd:cd01360 219 YLSTLALIASTLEKIATEIRHLQRTEVL--EVEEPFSKgqkGSSAMPHKRNPILSENICG-LARVIRSN--VIPALENVA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 315 LAYNKDMQE---------DKEGLFDVMdswaicLEMAALVLSGLQVNRERTLS--AAQQGYANSTELADYLVAKGMPFRE 383
Cdd:cd01360 294 LWHERDISHssvervilpDATILLDYI------LRRMTRVLENLVVYPENMRRnlNLTKGLIFSQRVLLALVEKGMSREE 367
|
....*
gi 527111731 384 AHHVV 388
Cdd:cd01360 368 AYEIV 372
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
126-286 |
1.86e-13 |
|
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: 72.07 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 126 QELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALKRAdtCPLGTGALA-GT- 203
Cdd:cd01596 153 ERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERL--RELNLGGTAvGTg 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 204 --AYP--MDRV--KLAQ--SLGFASPTlNSLDTVSDRDHVVEICSDASISMMHLSRMAEDLIFFNSG-EAGFIELD-DEV 273
Cdd:cd01596 231 lnAPPgyAEKVaaELAEltGLPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGpRAGLGEINlPAN 309
|
170
....*....|...
gi 527111731 274 TSGSSLMPQKKNP 286
Cdd:cd01596 310 QPGSSIMPGKVNP 322
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
94-404 |
5.03e-13 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 70.81 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 94 AKVGDLGKKLHTGRSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYV 173
Cdd:PRK09053 93 ARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 174 EMFERDISRLqDALkRADTCPLGTGALAGT-------AYPMDRvKLAQSLGFASPTLnSLDTvsDRDHVVEICSDASISM 246
Cdd:PRK09053 173 DALLRHRQRL-AAL-RPRALVLQFGGAAGTlaslgeqALPVAQ-ALAAELQLALPAL-PWHT--QRDRIAEFASALGLLA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 247 MHLSRMAEDLIFFNSGEAGFI-ELDDEVTSGSSLMPQKKNPDALELIRGKTGRVYGSLIGILTTM-----KALPLaynkd 320
Cdd:PRK09053 247 GTLGKIARDVSLLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMpqeheRALGG----- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 321 MQEDKEGLFDVMDSWAICLEMAALVLSGLQVNRER---TLSAAQQ---GYANSTELADYLvakGMPfrEAHHVVGEAVVN 394
Cdd:PRK09053 322 WHAEWDTLPELACLAAGALAQMAQIVEGLEVDAARmraNLDLTHGlilAEAVMLALADRI---GRL--DAHHLVEQASKR 396
|
330
....*....|
gi 527111731 395 AIAKQTPLED 404
Cdd:PRK09053 397 AVAEGRHLRD 406
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
107-302 |
1.14e-12 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 69.64 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 107 RSRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAErEIDAVMP-GYTHLQRAQPVLFGHWCLAYVEMFERDISRLQD 185
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAE-QFDHVIKmGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 186 ALKR-----ADTCPLGTGALAGTAYPMDRVK-LAQSLGFASPTLNSL-DTVSDRDHVVEICSDASISMMHLSRMAEDLIF 258
Cdd:PRK14515 224 SRQHlyevnMGATAVGTGLNADPEYIEAVVKhLAAISELPLVGAEDLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 527111731 259 FNSG-EAGFIELD-DEVTSGSSLMPQKKNPDALELIRGKTGRVYGS 302
Cdd:PRK14515 304 MASGpRVGLAEIMlPARQPGSSIMPGKVNPVMPEVINQIAFQVIGN 349
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
126-384 |
9.45e-11 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 63.57 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 126 QELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDALKRAdtCPLgtgALAGTA- 204
Cdd:PRK00485 158 ERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHL--YEL---ALGGTAv 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 205 ---------YPmDRV--KLAQSLGFA-SPTLNSLDTVSDRDHVVEiCSDA----SISMMhlsRMAEDLIFFNSG-EAGFI 267
Cdd:PRK00485 233 gtglnahpgFA-ERVaeELAELTGLPfVTAPNKFEALAAHDALVE-ASGAlktlAVSLM---KIANDIRWLASGpRCGLG 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 268 EL---DDEvtSGSSLMPQKKNP---DALELIrgkTGRVYG--SLIGI--------LTTMKALpLAYNkdMQEDKEGLFDV 331
Cdd:PRK00485 308 EIslpENE--PGSSIMPGKVNPtqcEALTMV---CAQVMGndAAVTFagsqgnfeLNVFKPV-IAYN--FLQSIRLLADA 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527111731 332 MDSwaicleMAALVLSGLQVNRERTLSAAQQ------------GYANSTELADYLVAKGMPFREA 384
Cdd:PRK00485 380 MRS------FADHCVVGIEPNRERIKELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKEA 438
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
108-286 |
2.04e-10 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 62.45 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 108 SRNDQVATDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDAl 187
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRA- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 188 kRADTCPLGTGALA-GT------AYPmDRV--KLAQSLGFA-SPTLNSLDTVSDRDHVVEICSDASISMMHLSRMAEDLI 257
Cdd:PRK12273 221 -AELLREVNLGATAiGTglnappGYI-ELVveKLAEITGLPlVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLR 298
|
170 180 190
....*....|....*....|....*....|.
gi 527111731 258 FFNSG-EAGFIELD-DEVTSGSSLMPQKKNP 286
Cdd:PRK12273 299 LLSSGpRAGLNEINlPAVQAGSSIMPGKVNP 329
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
106-384 |
8.36e-10 |
|
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: 60.59 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 106 GRSRND------QVATDLKLwckkeGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERD 179
Cdd:cd01362 133 SQSSNDtfptamHIAAALAL-----QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 180 ISRLQDALKRADTCPLGtGALAGT---AYP--MDRV--KLAQSLGFA-SPTLNSLDTVSDRDHVVEIcSDA----SISMM 247
Cdd:cd01362 208 IARIEAALPRLYELALG-GTAVGTglnAHPgfAEKVaaELAELTGLPfVTAPNKFEALAAHDALVEA-SGAlktlAVSLM 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 248 HLsrmAEDLIFFNSG-EAGFIELD-DEVTSGSSLMPQKKNP---DALELIrgkTGRVYG--SLIGI--------LTTMKA 312
Cdd:cd01362 286 KI---ANDIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNPtqcEALTMV---AAQVMGndAAITIagssgnfeLNVFKP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 313 LpLAYNkdMQEDKEGLFDVMDSwaicleMAALVLSGLQVNRERTLSAAQQ------------GYANSTELADYLVAKGMP 380
Cdd:cd01362 360 V-IIYN--LLQSIRLLADACRS------FADKCVAGIEPNRERIAELLERslmlvtalnphiGYDKAAKIAKKAHKEGLT 430
|
....
gi 527111731 381 FREA 384
Cdd:cd01362 431 LKEA 434
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
106-286 |
7.56e-09 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 57.78 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 106 GRSRNDQVATDLKLWCKKEGQE-LLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQ 184
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIHSrLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 185 DALKRADTCPLGtGALAGTAYPMDR---VKLAQS------LGFASPTlNSLDTVSDRDHVVEiCSDASISM-MHLSRMAE 254
Cdd:PLN00134 209 CTLPRLYELAQG-GTAVGTGLNTKKgfdEKIAAAvaeetgLPFVTAP-NKFEALAAHDAFVE-LSGALNTVaVSLMKIAN 285
|
170 180 190
....*....|....*....|....*....|....
gi 527111731 255 DLIFFNSG-EAGFIELD-DEVTSGSSLMPQKKNP 286
Cdd:PLN00134 286 DIRLLGSGpRCGLGELNlPENEPGSSIMPGKVNP 319
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
39-292 |
2.32e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 55.83 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 39 AWASAITQVGVLTTDECTQLHAALNELlaetSTNPELIIASGAED---IHSFVEQsLIAKVG-DLGKKLHTGRSRNDQVA 114
Cdd:PRK05975 39 ALAEAEAEHGIIPAEAAERIAAACETF----EPDLAALRHATARDgvvVPALVRQ-LRAAVGeEAAAHVHFGATSQDVID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 115 TDLKLWCKKEGQELLELLGKLRTALIELAEREIDAVMPGYTHLQRAQPVLFGHWCLAYVEMFERDISRLQDAlkRADTCP 194
Cdd:PRK05975 114 TSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEAL--RADVFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 195 LGTGALAGT------AYPMDRVKLAQSLGFA-SPTLNsldtvSDRDHVVEICSDASISMMHLSRMAEDLiffnsgeAGFI 267
Cdd:PRK05975 192 LQFGGAAGTleklggKAAAVRARLAKRLGLEdAPQWH-----SQRDFIADFAHLLSLVTGSLGKFGQDI-------ALMA 259
|
250 260
....*....|....*....|....*....
gi 527111731 268 ELDDEVT----SGSSLMPQKKNPDALELI 292
Cdd:PRK05975 260 QAGDEISlsggGGSSAMPHKQNPVAAETL 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-405 |
1.38e-04 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 43.09 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 249 LSRMAEDLIFFNSGEAGFIELDDEVTS-GSSLMPQKKNPDALELIrgktgrvyGSLIgilTTMKALPLAYNKDMQEDKEG 327
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGQkGSSAMPHKRNPIGSERI--------TGLA---RVLRSYLVTALENVPLWHER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 328 lfDVMDS---WAICLEMAAL----------VLSGLQVNRERTLS--AAQQGYANSTELADYLVAKGMPFREAHHVVGEAV 392
Cdd:PRK08937 99 --DLSHSsaeRIALPDAFLAldyilnrfvnILENLVVFPENIERnlDKTLGFIATERVLLELVEKGMGREEAHELIREKA 176
|
170
....*....|...
gi 527111731 393 VNAIAKQTPLEDL 405
Cdd:PRK08937 177 MEAWKNQKDLREL 189
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
128-286 |
1.22e-03 |
|
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: 41.15 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 128 LLELLGKLRTALIELAEREI---DAVMPGYTHLQRAQPVLFG-HWCLAYVEMF--ERDISRLQDALK-RADTCPLGTGAL 200
Cdd:cd03302 112 LDLILPKLAAVIDRLAEFALeykDLPTLGFTHYQPAQLTTVGkRACLWIQDLLmdLRNLERLRDDLRfRGVKGTTGTQAS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111731 201 AGTAYPMDRVK-------LAQSLGFASpTLNSLDTVSDRDHVVEICSDASISMMHLSRMAEDLIFFnsgeAGFIELDDEV 273
Cdd:cd03302 192 FLDLFEGDHDKvealdelVTKKAGFKK-VYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL----ANLKEVEEPF 266
|
170
....*....|....*.
gi 527111731 274 TS---GSSLMPQKKNP 286
Cdd:cd03302 267 EKgqiGSSAMPYKRNP 282
|
|
| |
