|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
58-519 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 913.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 58 RKETKLWGGRFEEGVTDAVEGFTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDGKFEWR 137
Cdd:PLN02646 13 AKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEWR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 138 TDREDVHMNIEAALIEKVGEPAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQ 217
Cdd:PLN02646 93 PDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 218 RAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEF 297
Cdd:PLN02646 173 RAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 298 LAANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYN 377
Cdd:PLN02646 253 LFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 378 RDLQEDKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPAGYLDATTLADYLVKKGVPFRTSHEIVGRSVALCVSK 457
Cdd:PLN02646 333 RDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESK 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256501 458 NCQLAELGLDDLKSVHPVFEGDVYEYLGVENAVNKFISYGSTGSEQVKKQLEDWRTQLGISS 519
Cdd:PLN02646 413 GCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
59-516 |
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: 746.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 59 KETKLWGGRFEEGVTDAVEGFTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDGKFEWRT 138
Cdd:COG0165 1 MSMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 139 DREDVHMNIEAALIEKVGEPAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQR 218
Cdd:COG0165 81 ELEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 219 AQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFL 298
Cdd:COG0165 161 AQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 299 AANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNR 378
Cdd:COG0165 241 SAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 379 DLQEDKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPAGYLDATTLADYLVKKGVPFRTSHEIVGRSVALCVSKN 458
Cdd:COG0165 321 DLQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256501 459 CQLAELGLDDLKSVHPVFEGDVYEYLGVENAVNKFISYGSTGSEQVKKQLEDWRTQLG 516
Cdd:COG0165 401 KDLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLA 458
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
59-516 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 719.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 59 KETKLWGGRFEEGVTDAVEGFTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDGKFEWRT 138
Cdd:PRK00855 2 MSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 139 DREDVHMNIEAALIEKVGEPAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQR 218
Cdd:PRK00855 82 ELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 219 AQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFL 298
Cdd:PRK00855 162 AQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 299 AANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNR 378
Cdd:PRK00855 242 SAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 379 DLQEDKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPAGYLDATTLADYLVKKGVPFRTSHEIVGRSVALCVSKN 458
Cdd:PRK00855 322 DLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256501 459 CQLAELGLDDLKSVHPVFEGDVYEYLGVENAVNKFISYGSTGSEQVKKQLEDWRTQLG 516
Cdd:PRK00855 402 VDLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
82-515 |
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: 655.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 82 SISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDGKFEWRTDREDVHMNIEAALIEKVGEPAKK 161
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 162 LHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGR 241
Cdd:cd01359 81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 242 LVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASE 321
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 322 EFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNRDLQEDKEPLFDSVKAVLGMLEVC 401
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 402 TEFAQNISFNSKRIQSSLPAGYLDATTLADYLVK-KGVPFRTSHEIVGRSVALCVSKNCQLAELGLDDLKSVHPVFEGDV 480
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400
|
410 420 430
....*....|....*....|....*....|....*
gi 1002256501 481 YEYLGVENAVNKFISYGSTGSEQVKKQLEDWRTQL 515
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
63-516 |
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: 593.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 63 LWGGRFEEGVTDAVEGFTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDGKFEWRTDRED 142
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 143 VHMNIEAALIEKVGEP-AKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQP 221
Cdd:TIGR00838 81 IHMAIERELIDRVGEDlGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 222 VLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFLAAN 301
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 302 SIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNRDLQ 381
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 382 EDKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPAGYLDATTLADYLVKKGVPFRTSHEIVGRSVALCVSKNCQL 461
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256501 462 AELGLDDLKSVHPVFEGDVYEYLGVENAVNKFISYGSTGSEQVKKQLEDWRTQLG 516
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG 455
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
63-510 |
1.00e-168 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 484.49 E-value: 1.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 63 LWGGRFEEGVTDAVEGFTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGD--------KDIILEGLDQIEKLIQDgkf 134
Cdd:PRK04833 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEqqqleealNELLEEVRANPQQILAS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 135 ewrtDREDVHMNIEAALIEKVGEPAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYT 214
Cdd:PRK04833 80 ----DAEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 215 HLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFV 294
Cdd:PRK04833 156 HLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 295 LEFLAANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQ 374
Cdd:PRK04833 236 LELLSDASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 375 AYNRDLQEDKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPAGYLDATTLADYLVKKGVPFRTSHEIVGRSVALC 454
Cdd:PRK04833 316 AYNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256501 455 VSKNCQLAELGLDDLKSVHPVFEGDVYEYLGVENAVNKFISYGSTGSEQVKKQLED 510
Cdd:PRK04833 396 IRQGKPLEDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAA 451
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
63-513 |
1.94e-160 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 469.26 E-value: 1.94e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 63 LWGGRFEEGVTDAVEGFTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQI-EKLIQDGKFEWRTDRE 141
Cdd:PRK12308 3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELkLEVMEDPEQILLSDAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 142 DVHMNIEAALIEKVGEPAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQP 221
Cdd:PRK12308 83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 222 VLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFLAAN 301
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 302 SIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNRDLQ 381
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 382 EDKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPAGYLDATTLADYLVKKGVPFRTSHEIVGRSVALCVSKNCQL 461
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256501 462 AELGLDDLKSVHPVFEGDVYEYLGVENAVNKFISYGSTGSEQV-------KKQLEDWRT 513
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVayaveqaDKRLAARDT 461
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
90-411 |
1.64e-132 |
|
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: 387.63 E-value: 1.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 90 YKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDGKFEWRTDREDVHMNIEAALIEKVGE-PAKKLHTARSR 168
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGElNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 169 NDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRER 248
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 249 LNFCPLGACALAGTGL--PIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASEEFGFL 326
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 327 TPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNRDLQEDKEPLFDSVKAVLGMLEVCTEFAQ 406
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....*
gi 1002256501 407 NISFN 411
Cdd:cd01334 321 GLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
66-360 |
1.30e-78 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 248.82 E-value: 1.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 66 GRFEeGVTDAVEG-FTESISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQI-EKLIQDGKFEWRTDREDV 143
Cdd:pfam00206 1 GRFT-VPADALMGiFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVaEEGKLDDQFPLKVWQEGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 144 HMNIEAALIEKVGE-------PAKKLHTARSRNDQIVTDLRLWCRDAIDKILFR-IKQFQVSLVLLASKYVDLIVPGYTH 215
Cdd:pfam00206 80 GTAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPaLRQLIDALKEKAKEFADIVKPGRTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 216 LQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRF---KTAKDLKF----TAPMKNSIDAV 288
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEAT 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256501 289 SDRDFVLEFLAANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVST-GSSIMPQKKNPDPMELVRGKSARVFG 360
Cdd:pfam00206 240 SDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
98-452 |
1.44e-66 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 230.89 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 98 KAHASMLAAQGLItagDKDIILEGLDQIEKLiQDGKFEWRTDR---EDVHMNIEAALIEKVGEPAKK-LHTARSRNDQIV 173
Cdd:PRK02186 446 EAHLVMLGDTGIV---APERARPLLDAHRRL-RDAGFAPLLARpapRGLYMLYEAYLIERLGEDVGGvLQTARSRNDINA 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 174 TDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCP 253
Cdd:PRK02186 522 TTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCP 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 254 LGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVS 333
Cdd:PRK02186 602 LGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALT 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 334 TGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPqaYNRDLQ---EDKEPLFDSVKAVLGMLEVCTEFAQNISF 410
Cdd:PRK02186 682 GGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEagsPMNGPIAQACAAIEDAAAVLVLLIDGLEA 759
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002256501 411 NSKRIQSSLPAGYLDATTLADYLV-KKGVPFRTSHEIVGRSVA 452
Cdd:PRK02186 760 DQARMRAHLEDGGVSATAVAESLVvRRSISFRSAHTQVGQAIR 802
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
145-402 |
3.34e-61 |
|
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: 200.53 E-value: 3.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 145 MNIEAALIEKVGEPAKKLH------TARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQR 218
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 219 AQPVLLPHLLLSYVEQLERDagrlvncRERLNFCplgacalagtglpidrfktakdlkftapmknsidavsdrdFVLEFL 298
Cdd:cd01594 94 AQPVTLGYELRAWAQVLGRD-------LERLEEA----------------------------------------AVAEAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 299 AANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSV-STGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYN 377
Cdd:cd01594 127 DALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPgQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDN 206
|
250 260
....*....|....*....|....*
gi 1002256501 378 RDLQEDKEPLFDSVKAVLGMLEVCT 402
Cdd:cd01594 207 EDSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
98-484 |
8.78e-46 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 167.47 E-value: 8.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 98 KAHASMLAAQGLITAGDKDIILEGLDQIEKLIQDgKFEWRTDREDVHMNIEAALI-EKVGEPAKKLHTARSRNDQIVTDL 176
Cdd:PRK06705 46 KAHIVMLTEENLMKKEEAKFILHALKKVEEIPEE-QLLYTEQHEDLFFLVEHLISqEAKSDFVSNMHIGRSRNDMGVTMY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 177 RLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGA 256
Cdd:PRK06705 125 RMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 257 CALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASEEFGFLTPSDSVSTGS 336
Cdd:PRK06705 205 AALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 337 SIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYNRDLQEDKEP-LFDSVKAVLGMLEVCTEFAQNISFNSKRI 415
Cdd:PRK06705 285 SIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTL 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 416 QSSLPAGYLDATTLADYLVKK-GVPFRTSHEIVGrsvalcvskncQLAELGLDDLKSVHPVFEGDVYEYL 484
Cdd:PRK06705 365 KRRSYKHAITITDFADVLTKNyGIPFRHAHHAAS-----------VIANMSLEQKKELHELCFKDVNIYL 423
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
62-423 |
4.64e-31 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 125.01 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 62 KLW-GGRFEEGVTDAVEGFTE-SISYDWQLYKYDIMGSKAHASMLAAQGLITAGDKDIILEGLDQIEKliqdGKFEWRTD 139
Cdd:PRK06389 2 KIWsGGAGEELENDFYDNIVKdDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIYK----NGIEIDLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 140 REDVHMNIEAALIEKVGEPAKKLHTARSRNDQIVTDLRLWcrdAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRA 219
Cdd:PRK06389 78 LEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLF---IIDKIIEIEKILYEIIKVIPGFNLKGRLPGYTHFRQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 220 QPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALAGTGLPIDRFKTAKDLKFTAPMKNSIDAVSDRDFVLEfLA 299
Cdd:PRK06389 155 MPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIE-NI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 300 ANSIA--AVHLSRIGEEWVLWASEefGFLTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCKGLPQAYN 377
Cdd:PRK06389 234 SYLISslAVDLSRICQDIIIYYEN--GIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYH 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1002256501 378 RDLQEDKEPLFDSVKAVLGMLEVCTEFAQNISF---NSKRIQSSLPAGY 423
Cdd:PRK06389 312 RDFQIVKDSTISFINNFERILLGLPDLLYNIKFeitNEKNIKNSVYATY 360
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
423-490 |
1.13e-29 |
|
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: 110.97 E-value: 1.13e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256501 423 YLDATTLADYLVKKGVPFRTSHEIVGRSVALCVSKNCQLAELGLDDLKSVHPVFEGDVYEYLGVENAV 490
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
117-447 |
1.49e-23 |
|
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: 102.20 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 117 IILEGLDQIEKLIQDGKFEW-------RTDREDVhMNIEAALIEKVGEPAKK-LHTARSRNDQIVTDLRLWCRDAIDKIL 188
Cdd:cd01595 31 IPKEAAEEIRAAADVFEIDAeriaeieKETGHDV-IAFVYALAEKCGEDAGEyVHFGATSQDINDTALALQLRDALDIIL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 189 FRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPL-GA----CALAGTG 263
Cdd:cd01595 110 PDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGIsGAvgthASLGPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 264 LPIDRFkTAKDLKFTAPmknsidAVS----DRDFVLEFLAANSIAAVHLSRIGEEWVLWASEEFGFLT-PSDSVSTGSSI 338
Cdd:cd01595 190 PEVEER-VAEKLGLKVP------PITtqiePRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVEePFEKGQVGSST 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 339 MPQKKNPDPMELVRGKSARVFGDLMTVLTlckGLPQAYNRDLQE---DKEPLFDSVKAVLGMLEVCTEFAQNISFNSKRI 415
Cdd:cd01595 263 MPHKRNPIDSENIEGLARLVRALAAPALE---NLVQWHERDLSDssvERNILPDAFLLLDAALSRLQGLLEGLVVNPERM 339
|
330 340 350
....*....|....*....|....*....|....
gi 1002256501 416 QSSLPA--GYLDATTLADYLVKKGVPFRTSHEIV 447
Cdd:cd01595 340 RRNLDLtwGLILSEAVMMALAKKGLGRQEAYELV 373
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
104-447 |
2.00e-19 |
|
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: 90.53 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 104 LAAQGLITAGDkdiilegLDQIEKLIQDGKFEW-------RTDREDVhMNIEAALIEKVGEPAKK-LHTARSRNDqiVTD 175
Cdd:COG0015 35 QAELGLIPAEA-------AAAIRAAADDFEIDAerikeieKETRHDV-KAFVYALKEKVGAEAGEyIHFGATSQD--IND 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 176 --LRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCP 253
Cdd:COG0015 105 taLALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 254 L-GAcalAGT-------GLPIDRfKTAKDLKFTAPMknSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASEEFGF 325
Cdd:COG0015 185 IgGA---VGTyaahgeaWPEVEE-RVAEKLGLKPNP--VTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEVGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 326 LT-PSDSVSTGSSIMPQKKNpdPM--ELVRGKSARVFGDLMTVLTlckGLPQAYNRDlqedkepLFDS-VK--------- 392
Cdd:COG0015 259 VEePFAKGQVGSSAMPHKRN--PIdsENIEGLARLARALAAALLE---ALASWHERD-------LSDSsVErnilpdafl 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256501 393 AVLGMLEVCTEFAQNISFNSKRIQSSLPA--GYLDATTLADYLVKKGVPFRTSHEIV 447
Cdd:COG0015 327 LLDGALERLLKLLEGLVVNPERMRANLDLtgGLVLSEAVLMALVRRGLGREEAYELV 383
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
149-468 |
3.61e-19 |
|
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: 90.00 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 149 AALIEKVGEPAKK-LHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHL 227
Cdd:cd01597 79 KQLTAACGDAAGEyVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 228 LLSYVEQLERDAGRLVNCRERLNFCPL-GAC----ALAGTGLPIDRfKTAKDLKFTAPmknSIDAVSDRDFVLEFLAANS 302
Cdd:cd01597 159 VAVWLSELLRHRERLDELRPRVLVVQFgGAAgtlaSLGDQGLAVQE-ALAAELGLGVP---AIPWHTARDRIAELASFLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 303 IAAVHLSRIGEEWVLWASEEFGFLT-PSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLtlcKGLPQAYNRDLQ 381
Cdd:cd01597 235 LLTGTLGKIARDVYLLMQTEIGEVAePFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLL---DAMVQEHERDAG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 382 EDK---EPLFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSLPA--GYLDATT----LADYLVKKgvpfrTSHEIVGRSVA 452
Cdd:cd01597 312 AWHaewIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLtgGLILSEAvmmaLAPKLGRQ-----EAHDLVYEACM 386
|
330
....*....|....*.
gi 1002256501 453 LCVSKNCQLAELGLDD 468
Cdd:cd01597 387 RAVEEGRPLREVLLED 402
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
165-481 |
1.55e-18 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 88.12 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 165 ARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVN 244
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 245 CRERLNFCPLGACALaGTGLPIDR---FKTAKDLKFT-----APMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWV 316
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPeyiERVVKHLAAItglplVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 317 LWAS---EEFG--FLTPsdsVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVlTLCKGLPQaynrdLQEDK-EPL--F 388
Cdd:PRK13353 297 LLSSgprTGLGeiNLPA---VQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTI-TLAAEAGQ-----LELNVmEPViaF 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 389 DSVKAVLGMLEVCTEFAQN----ISFNSKRIQSSLPAGYLDATTLADYLvkkGvpFRTSHEIV------GRSVA-LCVSK 457
Cdd:PRK13353 368 NLLESISILTNACRAFTDNcvkgIEANEERCKEYVEKSVGIATALNPHI---G--YEAAARIAkeaiatGRSVReLALEN 442
|
330 340
....*....|....*....|....*...
gi 1002256501 458 NC----QLAELgLDDLKSVHPVFEGDVY 481
Cdd:PRK13353 443 GLlseeELDLI-LDPFRMTHPGIAGATL 469
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
104-345 |
7.96e-14 |
|
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: 72.97 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 104 LAAQGLITAGDKDII-------LEGLDQIEKLIqdgkfewrtdREDVhMNIEAALIEKVGEPAKKLHTARSRNDQIVTDL 176
Cdd:cd01360 31 WAKLGVIPAEAAEEIrkkakfdVERVKEIEAET----------KHDV-IAFVTAIAEYCGEAGRYIHFGLTSSDVVDTAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 177 RLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPL-G 255
Cdd:cd01360 100 ALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKIsG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 256 AcalAGTGLPIDRF---KTAKDLKFT-APMKNSidaVSDRDFVLEFLAANSIAAVHLSRIGEEW-------VLWASEEFg 324
Cdd:cd01360 180 A---VGTYANLGPEveeRVAEKLGLKpEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIrhlqrteVLEVEEPF- 252
|
250 260
....*....|....*....|.
gi 1002256501 325 fltpsDSVSTGSSIMPQKKNP 345
Cdd:cd01360 253 -----SKGQKGSSAMPHKRNP 268
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
158-365 |
1.18e-13 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 73.11 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 158 PAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLER 237
Cdd:PRK14515 137 PNSHVNMAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLER 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 238 DAGRLVNCRERLNFCPLGACALaGTGLPIDRFKTAKDLKFTA-----PMKNS---IDAVSDRDFVLEFLAANSIAAVHLS 309
Cdd:PRK14515 217 DMKRIQQSRQHLYEVNMGATAV-GTGLNADPEYIEAVVKHLAaiselPLVGAedlVDATQNTDAYTEVSAALKVCMMNMS 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 310 RIGEEWVLWASEEFGFLT----PSDsvSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTV 365
Cdd:PRK14515 296 KIANDLRLMASGPRVGLAeimlPAR--QPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTI 353
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
165-365 |
2.46e-13 |
|
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: 71.79 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 165 ARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVN 244
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 245 CRERLNFCPLGACALaGTGLPID---RFKTAKDL-KFT----APMKNSIDAVSDRD-FVlEFLAANSIAAVHLSRIGEEW 315
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPpgyIELVVEKLsEITglplKRAENLIDATQNTDaFV-EVSGALKRLAVKLSKIANDL 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256501 316 VLWASeefG-------FLTPsdSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTV 365
Cdd:cd01357 291 RLLSS---GpraglgeINLP--AVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTI 342
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
191-365 |
1.95e-11 |
|
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: 65.91 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 191 IKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALaGTGL--PID- 267
Cdd:cd01596 159 LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAV-GTGLnaPPGy 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 268 RFKTAKDL-KFT----APMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASeefGFLT-------PsdSVSTG 335
Cdd:cd01596 238 AEKVAAELaELTglpfVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSS---GPRAglgeinlP--ANQPG 312
|
170 180 190
....*....|....*....|....*....|
gi 1002256501 336 SSIMPQKKNPDPMELVRGKSARVFGDLMTV 365
Cdd:cd01596 313 SSIMPGKVNPVIPEAVNMVAAQVIGNDTAI 342
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
157-380 |
4.78e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 64.65 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 157 EPAKKLHTARSRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLE 236
Cdd:PRK09053 97 EAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 237 RDAGRLVNCRERLNFCPLGACA-----LAGTGLPIDRfKTAKDLKFTAPmknsidAVS---DRDFVLEFLAANSIAAVHL 308
Cdd:PRK09053 177 RHRQRLAALRPRALVLQFGGAAgtlasLGEQALPVAQ-ALAAELQLALP------ALPwhtQRDRIAEFASALGLLAGTL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256501 309 SRIGEEWVLWASEEFGFL-TPSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTlckGLPQAYNRDL 380
Cdd:PRK09053 250 GKIARDVSLLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFA---AMPQEHERAL 319
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
191-365 |
2.04e-08 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 56.62 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 191 IKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFCPLGACALaGTGLPID-RF 269
Cdd:PLN00134 156 LKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAV-GTGLNTKkGF 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 270 --KTAK------DLKFTAPmKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWVLWASEE---FGFLT-PSdsVSTGSS 337
Cdd:PLN00134 235 deKIAAavaeetGLPFVTA-PNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPrcgLGELNlPE--NEPGSS 311
|
170 180
....*....|....*....|....*...
gi 1002256501 338 IMPQKKNPDPMELVRGKSARVFGDLMTV 365
Cdd:PLN00134 312 IMPGKVNPTQCEALTMVCAQVMGNHVAI 339
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
167-345 |
4.31e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 55.52 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 167 SRNDQIVTDLRLWCRDAIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCR 246
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 247 ERLNFCPLGACAlAGTGL---PIDRFKTAK------DLKFtAPMKNSIDAVSDRD-FVlEFLAANSIAAVHLSRIGEEWV 316
Cdd:PRK12273 222 ELLREVNLGATA-IGTGLnapPGYIELVVEklaeitGLPL-VPAEDLIEATQDTGaFV-EVSGALKRLAVKLSKICNDLR 298
|
170 180 190
....*....|....*....|....*....|....
gi 1002256501 317 LWASEEF-GF----LTPsdsVSTGSSIMPQKKNP 345
Cdd:PRK12273 299 LLSSGPRaGLneinLPA---VQAGSSIMPGKVNP 329
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
294-468 |
2.87e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 51.18 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 294 VLEFLAANsIAAVhLSRIGEEWVLWASEEFGFLT-PSDSVSTGSSIMPQKKNPDPMELVRGKSARVFGDLMTVLTLCkgl 372
Cdd:PRK08937 18 IAEIVLAL-IATS-LEKFANEIRLLQRSEIREVEePFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 373 PQAYNRDLQEDKEP---LFDSVKAVLGMLEVCTEFAQNISFNSKRIQSSL--PAGYLDATTLADYLVKKGVPFRTSHEIV 447
Cdd:PRK08937 93 PLWHERDLSHSSAEriaLPDAFLALDYILNRFVNILENLVVFPENIERNLdkTLGFIATERVLLELVEKGMGREEAHELI 172
|
170 180
....*....|....*....|.
gi 1002256501 448 GRSVALCVSKNCQLAELGLDD 468
Cdd:PRK08937 173 REKAMEAWKNQKDLRELLEAD 193
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
167-360 |
8.73e-07 |
|
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: 51.35 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 167 SRNDQIVTDLRLWCRDAIDKILF-RIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNC 245
Cdd:cd01362 135 SSNDTFPTAMHIAAALALQERLLpALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 246 RERLNFCPLGACALaGTGL---P------IDRFKTAKDLKFTaPMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEWV 316
Cdd:cd01362 215 LPRLYELALGGTAV-GTGLnahPgfaekvAAELAELTGLPFV-TAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIR 292
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002256501 317 LWASEE---FGFLT-PSDsvSTGSSIMPQKKNPDPMELVRGKSARVFG 360
Cdd:cd01362 293 WLGSGPrcgLGELSlPEN--EPGSSIMPGKVNPTQCEALTMVAAQVMG 338
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
167-345 |
8.13e-06 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 48.16 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 167 SRNDQIVTDLRLWCRDAIDKILF-RIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNC 245
Cdd:PRK00485 139 SSNDTFPTAMHIAAVLAIVERLLpALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 246 RERLNFCPLGACAlAGTGL--PiDRF--KTAK------DLKFTaPMKNSIDAVSDRDFVLEFLAANSIAAVHLSRIGEEW 315
Cdd:PRK00485 219 LPHLYELALGGTA-VGTGLnaH-PGFaeRVAEelaeltGLPFV-TAPNKFEALAAHDALVEASGALKTLAVSLMKIANDI 295
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002256501 316 VLWASeefGFLT-----------PsdsvstGSSIMPQKKNP 345
Cdd:PRK00485 296 RWLAS---GPRCglgeislpeneP------GSSIMPGKVNP 327
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
105-345 |
1.89e-05 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 46.97 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 105 AAQGLITAGDKDIILEGLDQIEklIQDGKFEWRTDREDVHM-NIEAALIEKVGEP-AKKLHTARSRNDQIVTDLRLWCRD 182
Cdd:PRK05975 45 AEHGIIPAEAAERIAAACETFE--PDLAALRHATARDGVVVpALVRQLRAAVGEEaAAHVHFGATSQDVIDTSLMLRLKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 183 AIDKILFRIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCR---ERLNFCplGAcal 259
Cdd:PRK05975 123 ASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRadvFPLQFG--GA--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 260 AGTG------LPIDRFKTAKDLKFT-APMknsidAVSDRDFVLEFlaANSIAAV--HLSRIGEEWVLWASEEfgfltpsD 330
Cdd:PRK05975 198 AGTLeklggkAAAVRARLAKRLGLEdAPQ-----WHSQRDFIADF--AHLLSLVtgSLGKFGQDIALMAQAG-------D 263
|
250
....*....|....*....
gi 1002256501 331 SVST----GSSIMPQKKNP 345
Cdd:PRK05975 264 EISLsgggGSSAMPHKQNP 282
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
116-345 |
9.60e-05 |
|
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: 45.00 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 116 DIILEGLDQIEKLIQDGKFEW-----RTDREDVHMNIEAaLIEKVGEPAKKLHT-ARSRNDQIVTDLrLWCRDAIDKILF 189
Cdd:cd03302 40 DISDEQIEEMKANVENIDFEIaaaeeKKLRHDVMAHVHA-FGLLCPAAAGIIHLgATSCFVTDNTDL-IQIRDALDLILP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 190 RIKQFQVSLVLLASKYVDLIVPGYTHLQRAQPVLLPHLLLSYVEQLERDAGRLVNCRERLNFcpLGACALAGTG---LPI 266
Cdd:cd03302 118 KLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRF--RGVKGTTGTQasfLDL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256501 267 ---DRFKTAKDLKFTAPM---KNSIDAVS---DRDFVLEFLAANSIAAVHLSRIGEEWVLWAS----EEfgfltPSDSVS 333
Cdd:cd03302 196 fegDHDKVEALDELVTKKagfKKVYPVTGqtySRKVDIDVLNALSSLGATAHKIATDIRLLANlkevEE-----PFEKGQ 270
|
250
....*....|..
gi 1002256501 334 TGSSIMPQKKNP 345
Cdd:cd03302 271 IGSSAMPYKRNP 282
|
|
| |
