|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
56-522 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 897.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 56 SPENRDDKEVKLWGGRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIES 135
Cdd:PLN02646 7 ASEEEAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 136 GDFVWRTDREDVHMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVP 215
Cdd:PLN02646 87 GKFEWRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 216 GYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDR 295
Cdd:PLN02646 167 GYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 296 DFALEFLSANAITAIHLSRLGEEWVLWASEEFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKG 375
Cdd:PLN02646 247 DFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 376 LPLAYNRDLQEDKEPVFDSVKTILGMLEVSAEFAQNISFNRERIEKALPAGYLDATTLADYLVKKGIPFRTGHDIVGKSV 455
Cdd:PLN02646 327 LPTAYNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAV 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333123913 456 ALCVTKSCCLQDLSLDELRSISPVFEEDVYEFLGAENAINKFCSYGSTGAACVATQMEYWVNKLQIN 522
Cdd:PLN02646 407 ALAESKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEIT 473
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
66-520 |
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: 728.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 66 KLWGGRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESGDFVWRTDRE 145
Cdd:COG0165 4 KLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 146 DVHMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQP 225
Cdd:COG0165 84 DIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 226 VLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSAN 305
Cdd:COG0165 164 VTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLSAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 306 AITAIHLSRLGEEWVLWASEEFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQ 385
Cdd:COG0165 244 SLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDLQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 386 EDKEPVFDSVKTILGMLEVSAEFAQNISFNRERIEKALPAGYLDATTLADYLVKKGIPFRTGHDIVGKSVALCVTKSCCL 465
Cdd:COG0165 324 EDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKDL 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1333123913 466 QDLSLDELRSISPVFEEDVYEFLGAENAINKFCSYGSTGAACVATQMEYWVNKLQ 520
Cdd:COG0165 404 EDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLA 458
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
62-520 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 712.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 62 DKEVKLWGGRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESGDFVWR 141
Cdd:PRK00855 1 MMSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 142 TDREDVHMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQ 221
Cdd:PRK00855 81 PELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 222 RAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEF 301
Cdd:PRK00855 161 RAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 302 LSANAITAIHLSRLGEEWVLWASEEFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYN 381
Cdd:PRK00855 241 LSAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 382 RDLQEDKEPVFDSVKTILGMLEVSAEFAQNISFNRERIEKALPAGYLDATTLADYLVKKGIPFRTGHDIVGKSVALCVTK 461
Cdd:PRK00855 321 RDLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1333123913 462 SCCLQDLSLDELRSISPVFEEDVYEFLGAENAINKFCSYGSTGAACVATQMEYWVNKLQ 520
Cdd:PRK00855 401 GVDLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
86-519 |
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: 644.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 86 SISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESGDFVWRTDREDVHMNIEAALIDMIGEPAKK 165
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 166 LHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGR 245
Cdd:cd01359 81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 246 LSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASE 325
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 326 EFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQEDKEPVFDSVKTILGMLEVS 405
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 406 AEFAQNISFNRERIEKALPAGYLDATTLADYLVK-KGIPFRTGHDIVGKSVALCVTKSCCLQDLSLDELRSISPVFEEDV 484
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400
|
410 420 430
....*....|....*....|....*....|....*
gi 1333123913 485 YEFLGAENAINKFCSYGSTGAACVATQMEYWVNKL 519
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
67-513 |
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: 582.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 67 LWGGRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESGDFVWRTDRED 146
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 147 VHMNIEAALIDMIGEP-AKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQP 225
Cdd:TIGR00838 81 IHMAIERELIDRVGEDlGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 226 VLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSAN 305
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 306 AITAIHLSRLGEEWVLWASEEFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQ 385
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 386 EDKEPVFDSVKTILGMLEVSAEFAQNISFNRERIEKALPAGYLDATTLADYLVKKGIPFRTGHDIVGKSVALCVTKSCCL 465
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1333123913 466 QDLSLDELRSISPVFEEDVYEFLGAENAINKFCSYGSTGAACVATQME 513
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIA 448
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
67-509 |
1.36e-173 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 497.20 E-value: 1.36e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 67 LWGGRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESG-DFVWRTDRE 145
Cdd:PRK04833 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANpQQILASDAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 146 DVHMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQP 225
Cdd:PRK04833 83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 226 VLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSAN 305
Cdd:PRK04833 163 VTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 306 AITAIHLSRLGEEWVLWASEEFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQ 385
Cdd:PRK04833 243 SISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 386 EDKEPVFDSVKTILGMLEVSAEFAQNISFNRERIEKALPAGYLDATTLADYLVKKGIPFRTGHDIVGKSVALCVTKSCCL 465
Cdd:PRK04833 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1333123913 466 QDLSLDELRSISPVFEEDVYEFLGAENAINKFCSYGSTGAACVA 509
Cdd:PRK04833 403 EDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVA 446
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
67-513 |
2.38e-164 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 479.66 E-value: 2.38e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 67 LWGGRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESG-DFVWRTDRE 145
Cdd:PRK12308 3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDpEQILLSDAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 146 DVHMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQP 225
Cdd:PRK12308 83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 226 VLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSAN 305
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 306 AITAIHLSRLGEEWVLWASEEFGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQ 385
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 386 EDKEPVFDSVKTILGMLEVSAEFAQNISFNRERIEKALPAGYLDATTLADYLVKKGIPFRTGHDIVGKSVALCVTKSCCL 465
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1333123913 466 QDLSLDELRSISPVFEEDVYEFLGAENAINKFCSYGSTGAACVATQME 513
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVE 450
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
94-415 |
6.22e-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: 362.98 E-value: 6.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 94 YKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESGDFVWRTDREDVHMNIEAALIDMIGE-PAKKLHTARSR 172
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGElNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 173 NDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVR 252
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 253 LNLCPLGACALAGTGL--PIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASEEFGFI 330
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 331 TPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQEDKEPVFDSVKTILGMLEVSAEFAQ 410
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....*
gi 1333123913 411 NISFN 415
Cdd:cd01334 321 GLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
70-364 |
4.63e-77 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 244.97 E-value: 4.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 70 GRFEESVTDAVERFTESISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGLDEIERRIESGD-FVWRTDREDVH 148
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDqFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 149 MNIEAALIDMIGE-------PAKKLHTARSRNDQVLTDFRLWCRDAIDA-ILDAIRYLQVSMVTLALKNEGLIVPGYTHL 220
Cdd:pfam00206 81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 221 QRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMT---AEALGF----TAPLRNSIDAVS 293
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAelvAKELGFftglPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333123913 294 DRDFALEFLSANAITAIHLSRLGEEWVLWASEEFGFITPNDSVST-GSSIMPQKKNPDPMELVRGKSARVIG 364
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
103-456 |
4.06e-62 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 218.56 E-value: 4.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 103 AHASMLASQGLMSVAERDSIiegLDEIERRIESGdFVWRTDR---EDVHMNIEAALIDMIGEPAKK-LHTARSRNDQVLT 178
Cdd:PRK02186 447 AHLVMLGDTGIVAPERARPL---LDAHRRLRDAG-FAPLLARpapRGLYMLYEAYLIERLGEDVGGvLQTARSRNDINAT 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 179 DFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPL 258
Cdd:PRK02186 523 TTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 259 GACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASEEFGFITPNDSVST 338
Cdd:PRK02186 603 GAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTG 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 339 GSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPlaYNRDLQ---EDKEPVFDSVKTILGMLEVSAEFAQNISFN 415
Cdd:PRK02186 683 GSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEagsPMNGPIAQACAAIEDAAAVLVLLIDGLEAD 760
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1333123913 416 RERIEKALPAGYLDATTLADYLV-KKGIPFRTGHDIVGKSVA 456
Cdd:PRK02186 761 QARMRAHLEDGGVSATAVAESLVvRRSISFRSAHTQVGQAIR 802
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
149-404 |
2.00e-53 |
|
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: 180.50 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 149 MNIEAALIDMIGEPAKKLH------TARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQR 222
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 223 AQPVLLQHLLLAFVEQLERDAGRLSDCRVrlnlcplgacalagtglpidrfmtaealgftaplrnsidavsdrdfaLEFL 302
Cdd:cd01594 94 AQPVTLGYELRAWAQVLGRDLERLEEAAV-----------------------------------------------AEAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 303 SANAITAIHLSRLGEEWVLWASEEFGFIT-PNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYN 381
Cdd:cd01594 127 DALALAAAHLSKIAEDLRLLLSGEFGELGePFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDN 206
|
250 260
....*....|....*....|...
gi 1333123913 382 RDLQEDKEPVFDSVKTILGMLEV 404
Cdd:cd01594 207 EDSPSMREILADSLLLLIDALRL 229
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
102-501 |
5.24e-48 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 173.63 E-value: 5.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 102 RAHASMLASQGLMSVAERDSIIEGLDEIERrIESGDFVWRTDREDVHMNIEaaliDMIGEPAK-----KLHTARSRNDQV 176
Cdd:PRK06705 46 KAHIVMLTEENLMKKEEAKFILHALKKVEE-IPEEQLLYTEQHEDLFFLVE----HLISQEAKsdfvsNMHIGRSRNDMG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 177 LTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLC 256
Cdd:PRK06705 121 VTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 257 PLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASEEFGFITPNDSV 336
Cdd:PRK06705 201 PMGAAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 337 STGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLAYNRDLQEDKEP-----------VFDSVKTILGMLEVS 405
Cdd:PRK06705 281 VQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPylykgiekairVFCIMNAVIRTMKVE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 406 AEFAQNISFNREriekalpagyLDATTLADYLVKK-GIPFRTGHDIVGKSVALCVTKSCCLQDLSLDEL------RSISP 478
Cdd:PRK06705 361 EDTLKRRSYKHA----------ITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVniylqeKFKIQ 430
|
410 420
....*....|....*....|...
gi 1333123913 479 VFEEDVYEFLGAENAINKFCSYG 501
Cdd:PRK06705 431 LLEKEWEEIISPEAFIQKRNVYG 453
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
65-455 |
5.82e-33 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 130.40 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 65 VKLW-GGRFEESVTDAVERFTE-SISYDKQLYKHDIRGSRAHASMLASQGLMSVAERDSIIEGL-DEIERRIEsgdfvWR 141
Cdd:PRK06389 1 MKIWsGGAGEELENDFYDNIVKdDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALiDIYKNGIE-----ID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 142 TDREDVHMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWcrdAIDAILDAIRYLQVSM-VTLALKNEGLIvPGYTHL 220
Cdd:PRK06389 76 LDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLF---IIDKIIEIEKILYEIIkVIPGFNLKGRL-PGYTHF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 221 QRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALAGTGLPIDRFMTAEALGFTAPLRNSIDAVSDRDFALE 300
Cdd:PRK06389 152 RQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 301 FLSANAIT-AIHLSRLGEEWVLWASEefGFITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCKGLPLA 379
Cdd:PRK06389 232 NISYLISSlAVDLSRICQDIIIYYEN--GIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333123913 380 YNRDLQEDKEPVFDSVKTILGMLEVSAEFAQNISFnRERIEKALPaGYLDATTLADYLVKKGIPFRTGHDIVGKSV 455
Cdd:PRK06389 310 YHRDFQIVKDSTISFINNFERILLGLPDLLYNIKF-EITNEKNIK-NSVYATYNAWLAFKNGMDWKSAYAYIGNKI 383
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
427-494 |
1.31e-27 |
|
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: 105.19 E-value: 1.31e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333123913 427 YLDATTLADYLVKKGIPFRTGHDIVGKSVALCVTKSCCLQDLSLDELRSISPVFEEDVYEFLGAENAI 494
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
123-451 |
7.82e-19 |
|
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: 88.33 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 123 IEGLDEIERRIesgdfvwrtdREDVhMNIEAALIDMIGEPAKK-LHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVS 201
Cdd:cd01595 50 AERIAEIEKET----------GHDV-IAFVYALAEKCGEDAGEyVHFGATSQDINDTALALQLRDALDIILPDLDALIDA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 202 MVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPL-GA----CALAGTGLPIDRFMtA 276
Cdd:cd01595 119 LAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGIsGAvgthASLGPKGPEVEERV-A 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 277 EALGFTAPLRNSidAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASEEFGFIT-PNDSVSTGSSIMPQKKNPDPMELV 355
Cdd:cd01595 198 EKLGLKVPPITT--QIEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVEePFEKGQVGSSTMPHKRNPIDSENI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 356 RGKSARVIGDLVTTLTlckGLPLAYNRDLQEDK-EPVF--DSVKTILGMLEVSAEFAQNISFNRERIEKALPA--GYLDA 430
Cdd:cd01595 276 EGLARLVRALAAPALE---NLVQWHERDLSDSSvERNIlpDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLtwGLILS 352
|
330 340
....*....|....*....|.
gi 1333123913 431 TTLADYLVKKGIPFRTGHDIV 451
Cdd:cd01595 353 EAVMMALAKKGLGRQEAYELV 373
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
169-368 |
6.17e-17 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 83.49 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 169 ARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSD 248
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 249 CRVRLNLCPLGACALaGTGLPID-----------RFMTAEALgftAPLRNSIDAVSDRDFALEFLSANAITAIHLSRLGE 317
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADpeyiervvkhlAAITGLPL---VGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIAN 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1333123913 318 EWVLWAS---EEFGFIT-PndSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVT 368
Cdd:PRK13353 294 DLRLLSSgprTGLGEINlP--AVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVT 346
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
120-451 |
3.02e-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: 77.59 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 120 DSIIEGLDEIERRIesgdfvwrtdREDVhMNIEAALIDMIGEPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQ 199
Cdd:cd01360 50 KFDVERVKEIEAET----------KHDV-IAFVTAIAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 200 VSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPL-GAcalAGTGLPIDRFM---T 275
Cdd:cd01360 119 EVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKIsGA---VGTYANLGPEVeerV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 276 AEALGFT-APLRNSidaVSDRDFALEFLSANAITAIHLSRLGEEW-------VLWASEEFgfitpnDSVSTGSSIMPQKK 347
Cdd:cd01360 196 AEKLGLKpEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIrhlqrteVLEVEEPF------SKGQKGSSAMPHKR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 348 NPDPMELVRGkSARVI-GDLVTTLtlcKGLPLAYNRDLQEDK-EPVF--DSVKTILGMLEVSAEFAQNISFNRERIEK-- 421
Cdd:cd01360 267 NPILSENICG-LARVIrSNVIPAL---ENVALWHERDISHSSvERVIlpDATILLDYILRRMTRVLENLVVYPENMRRnl 342
|
330 340 350
....*....|....*....|....*....|
gi 1333123913 422 ALPAGYLDATTLADYLVKKGIPFRTGHDIV 451
Cdd:cd01360 343 NLTKGLIFSQRVLLALVEKGMSREEAYEIV 372
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
108-451 |
1.14e-13 |
|
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: 72.81 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 108 LASQGLMSVAERDSI----------IEGLDEIERRIesgdfvwrtdREDVhMNIEAALIDMIGEPAKK-LH---TARSRN 173
Cdd:COG0015 35 QAELGLIPAEAAAAIraaaddfeidAERIKEIEKET----------RHDV-KAFVYALKEKVGAEAGEyIHfgaTSQDIN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 174 DqvlTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRL 253
Cdd:COG0015 104 D---TALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 254 NLCPL-GAcalAGT-------GLPIDRFMtAEALGFT-APLRNSIdavSDRDFALEFLSANAITAIHLSRLGEEWVLWAS 324
Cdd:COG0015 181 LVGKIgGA---VGTyaahgeaWPEVEERV-AEKLGLKpNPVTTQI---EPRDRHAELFSALALIAGSLEKIARDIRLLQR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 325 EEFGFIT-PNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTlckGLPLAYNRDLqedkepvFDS-VK------ 396
Cdd:COG0015 254 TEVGEVEePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLE---ALASWHERDL-------SDSsVErnilpd 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 397 ---TILGMLEVSAEFAQNISFNRERIEKALPA--GYLDATTLADYLVKKGIPFRTGHDIV 451
Cdd:COG0015 324 aflLLDGALERLLKLLEGLVVNPERMRANLDLtgGLVLSEAVLMALVRRGLGREEAYELV 383
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
169-370 |
4.22e-12 |
|
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: 67.93 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 169 ARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSD 248
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 249 CRVRLNLCPLGACALaGTGLPID---RFMTAEAL----GFtaPLR---NSIDAVSDRDFALEFLSANAITAIHLSRLGEE 318
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPpgyIELVVEKLseitGL--PLKraeNLIDATQNTDAFVEVSGALKRLAVKLSKIAND 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 319 WVLWASeefG-------FITPndSVSTGSSIMPQKKNPDPMELVRGKSARVIG-DLVTTL 370
Cdd:cd01357 290 LRLLSS---GpraglgeINLP--AVQPGSSIMPGKVNPVIPEVVNQVAFQVIGnDLTITM 344
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
162-365 |
5.21e-12 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 68.10 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 162 PAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLER 241
Cdd:PRK14515 137 PNSHVNMAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLER 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 242 DAGRLSDCRVRLNLCPLGACALaGTGLPID-RFMTAEALGFTA----PLRNS---IDAVSDRDFALEFLSANAITAIHLS 313
Cdd:PRK14515 217 DMKRIQQSRQHLYEVNMGATAV-GTGLNADpEYIEAVVKHLAAiselPLVGAedlVDATQNTDAYTEVSAALKVCMMNMS 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1333123913 314 RLGEEWVLWAS-EEFGF---ITPndSVSTGSSIMPQKKNPDPMELVRGKSARVIGD 365
Cdd:PRK14515 296 KIANDLRLMASgPRVGLaeiMLP--ARQPGSSIMPGKVNPVMPEVINQIAFQVIGN 349
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
182-368 |
5.70e-12 |
|
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: 67.65 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 182 LWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPL-GA 260
Cdd:cd01597 109 LQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFgGA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 261 C----ALAGTGLPIDRFMtAEALGFTAPlrnSIDAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASEEFGFIT-PNDS 335
Cdd:cd01597 189 AgtlaSLGDQGLAVQEAL-AAELGLGVP---AIPWHTARDRIAELASFLALLTGTLGKIARDVYLLMQTEIGEVAePFAK 264
|
170 180 190
....*....|....*....|....*....|...
gi 1333123913 336 VSTGSSIMPQKKNPDPMELVRGKSARVIGDLVT 368
Cdd:cd01597 265 GRGGSSTMPHKRNPVGCELIVALARRVPGLAAL 297
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
192-445 |
1.91e-10 |
|
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: 62.83 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 192 LDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALaGTGL--P 269
Cdd:cd01596 156 LPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAV-GTGLnaP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 270 ID-RFMTAEAL----GF---TAPlrNSIDAVSDRDFALEFLSANAITAIHLSR---------------LGEewvlwasee 326
Cdd:cd01596 235 PGyAEKVAAELaeltGLpfvTAP--NLFEATAAHDALVEVSGALKTLAVSLSKiandlrllssgpragLGE--------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 327 fgFITPndSVSTGSSIMPQKKNPDPMELVRGKSARVIG-DlvTTLTLCKG---------LPL-AYNrdlqedkepVFDSV 395
Cdd:cd01596 304 --INLP--ANQPGSSIMPGKVNPVIPEAVNMVAAQVIGnD--TAITMAGSagqlelnvfKPViAYN---------LLQSI 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333123913 396 kTILGmlEVSAEFAQN----ISFNRERIEKAL-----------PA-GYLDATTLADYLVKKGIPFR 445
Cdd:cd01596 369 -RLLA--NACRSFRDKcvegIEANEERCKEYVenslmlvtalnPHiGYEKAAEIAKEALKEGRTLR 431
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
190-446 |
1.01e-09 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 60.86 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 190 AILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALaGTGLP 269
Cdd:PLN00134 151 RLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAV-GTGLN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 270 ID-RFMTAEA--------LGF-TAPlrNSIDAVSDRDFALEFLSANAITAIHLSRLGEEWVLWASEE---FGFIT-PndS 335
Cdd:PLN00134 230 TKkGFDEKIAaavaeetgLPFvTAP--NKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPrcgLGELNlP--E 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 336 VSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTT----------LTLCKGLpLAYNrdlqedkepVFDSVKtILGmlEVS 405
Cdd:PLN00134 306 NEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAItvggsaghfeLNVFKPL-IAYN---------LLHSIR-LLG--DAS 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1333123913 406 AEFAQN----ISFNRERIEKAL-----------PA-GYLDATTLADYLVKKGIPFRT 446
Cdd:PLN00134 373 ASFRKNcvrgIEANRERISKLLheslmlvtalnPKiGYDKAAAVAKKAHKEGTTLKE 429
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
171-370 |
2.60e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 56.29 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 171 SRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCR 250
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 251 VRLNLCPLGACAlAGTGL---PIDRFMTAEAL----GFT-APLRNSIDAVSDRDFALEFLSANAITAIHLSR-------- 314
Cdd:PRK12273 222 ELLREVNLGATA-IGTGLnapPGYIELVVEKLaeitGLPlVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKicndlrll 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333123913 315 -------LGEewvlwaseefgFITPndSVSTGSSIMPQKKNPDPMELVRGKSARVIG-DLVTTL 370
Cdd:PRK12273 301 ssgpragLNE-----------INLP--AVQAGSSIMPGKVNPVIPEVVNQVCFQVIGnDTTVTM 351
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
161-370 |
6.57e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 51.94 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 161 EPAKKLHTARSRNDQVLTDFRLWCRDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLE 240
Cdd:PRK09053 97 EAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 241 RDAGRLSDCRVRLNLCPLGACA-----LAGTGLPIDRFMtAEALGFTAPlrnsidAVS---DRDFALEFLSANAITAIHL 312
Cdd:PRK09053 177 RHRQRLAALRPRALVLQFGGAAgtlasLGEQALPVAQAL-AAELQLALP------ALPwhtQRDRIAEFASALGLLAGTL 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1333123913 313 SRLGEEWVLWASEEFG-FITPNDSVSTGSSIMPQKKNPDPMELVRGKSARVIGdLVTTL 370
Cdd:PRK09053 250 GKIARDVSLLMQTEVGeVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPG-LVATL 307
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
192-445 |
2.63e-05 |
|
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: 46.72 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 192 LDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACALaGTGL--- 268
Cdd:cd01362 157 LPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAV-GTGLnah 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 269 P------IDRFMTAEALGF-TAPlrNSIDAVSDRDfALEFLS------ANAITAIH----------LSRLGeEWVLWASE 325
Cdd:cd01362 236 PgfaekvAAELAELTGLPFvTAP--NKFEALAAHD-ALVEASgalktlAVSLMKIAndirwlgsgpRCGLG-ELSLPENE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 326 efgfitPndsvstGSSIMPQKKNPDPMELVRGKSARVIGDLVT--------TLTLCKGLPL-AYNrdlqedkepVFDSVk 396
Cdd:cd01362 312 ------P------GSSIMPGKVNPTQCEALTMVAAQVMGNDAAitiagssgNFELNVFKPViIYN---------LLQSI- 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333123913 397 TILGmlEVSAEFAQN----ISFNRERIEKAL-----------PA-GYLDATTLADYLVKKGIPFR 445
Cdd:cd01362 370 RLLA--DACRSFADKcvagIEPNRERIAELLerslmlvtalnPHiGYDKAAKIAKKAHKEGLTLK 432
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
194-445 |
9.16e-05 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 45.08 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 194 AIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLLQHLLLAFVEQLERDAGRLSDCRVRLNLCPLGACAlAGTGL--PID 271
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTA-VGTGLnaHPG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 272 ---RFmtAEAL------GFTaPLRNSIDAVSDRDfALEFLS------ANAITAIH----------LSRLGEewvlwasee 326
Cdd:PRK00485 242 faeRV--AEELaeltglPFV-TAPNKFEALAAHD-ALVEASgalktlAVSLMKIAndirwlasgpRCGLGE--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 327 fgfIT-----PndsvstGSSIMPQKKNPDPMELVRGKSARVIG-DlvTTLT---------LCKGLPL-AYNrdlqedkep 390
Cdd:PRK00485 309 ---ISlpeneP------GSSIMPGKVNPTQCEALTMVCAQVMGnD--AAVTfagsqgnfeLNVFKPViAYN--------- 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333123913 391 VFDSVkTILGmlEVSAEFAQN----ISFNRERIEKAL-----------PA-GYLDATTLADYLVKKGIPFR 445
Cdd:PRK00485 369 FLQSI-RLLA--DAMRSFADHcvvgIEPNRERIKELLerslmlvtalnPHiGYDKAAKIAKKAHKEGLTLK 436
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
339-451 |
2.68e-03 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 39.24 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 339 GSSIMPQKKNPDPMELVRGKSARVIGDLVTTLTLCkglPLAYNRDLQEDKEP---VFDSVKTILGMLEVSAEFAQNISFN 415
Cdd:PRK08937 58 GSSAMPHKRNPIGSERITGLARVLRSYLVTALENV---PLWHERDLSHSSAEriaLPDAFLALDYILNRFVNILENLVVF 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 1333123913 416 RERIEKAL--PAGYLDATTLADYLVKKGIPFRTGHDIV 451
Cdd:PRK08937 135 PENIERNLdkTLGFIATERVLLELVEKGMGREEAHELI 172
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
185-349 |
8.12e-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: 38.84 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 185 RDAIDAILDAIRYLQVSMVTLALKNEGLIVPGYTHLQRAQPVLL--------QHLLLAFvEQLERdagRLSDCRVRlnlc 256
Cdd:cd03302 109 RDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVgkraclwiQDLLMDL-RNLER---LRDDLRFR---- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333123913 257 plGACALAGTGlpiDRFMT----------------AEALGF---------TAPLRNSIDAVSdrdfALEFLSANA---IT 308
Cdd:cd03302 181 --GVKGTTGTQ---ASFLDlfegdhdkvealdelvTKKAGFkkvypvtgqTYSRKVDIDVLN----ALSSLGATAhkiAT 251
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1333123913 309 AI-HLSRLGEewvlwaSEEfgfitPNDSVSTGSSIMPQKKNP 349
Cdd:cd03302 252 DIrLLANLKE------VEE-----PFEKGQIGSSAMPYKRNP 282
|
|
| |
