|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
18-472 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 844.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 18 MWGGRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFEWRIDLED 97
Cdd:PRK00855 6 LWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPELED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 98 VHMNIESRLTQRIGIAGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPV 177
Cdd:PRK00855 86 IHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 178 TFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAAS 257
Cdd:PRK00855 166 TFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLSAAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 258 LIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQE 337
Cdd:PRK00855 246 LLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRDLQE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 338 DKEPLFDAIDTVRGSLMAFADMIPALVPNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGKDLS 417
Cdd:PRK00855 326 DKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGVDLA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1844060874 418 ELTLEQLQQFSDLIQADVFEkALTLEASVNARNHIGGTAPAQVEAAIARAYVRLE 472
Cdd:PRK00855 406 DLSLEELQAFSPLITEDVYE-VLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
15-476 |
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: 840.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 15 TSGMWGGRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFEWRID 94
Cdd:COG0165 2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 95 LEDVHMNIESRLTQRIGIAGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTA 174
Cdd:COG0165 82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 175 QPVTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNA 254
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 255 AASLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKD 334
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 335 NQEDKEPLFDAIDTVRGSLMAFADMIPALVPNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGK 414
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844060874 415 DLSELTLEQLQQFSDLIQADVFEkALTLEASVNARNHIGGTAPAQVEAAIARAYVRLEKLYA 476
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYE-ALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
37-471 |
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: 702.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 37 SVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFEWRIDLEDVHMNIESRLTQRIGIAGKK 116
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 117 LHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSER 196
Cdd:cd01359 81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 197 LIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILWTSA 276
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 277 QFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQEDKEPLFDAIDTVRGSLMAF 356
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 357 ADMIPALVPNIEIMREAALRGFSTATDLADYLVKN-GVAFRDAHEIVGKAVALGVQEGKDLSELTLEQLQQFSDLIQADV 435
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGFSTATDLADYLVREkGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1844060874 436 FEkALTLEASVNARNHIGGTAPAQVEAAIARAYVRL 471
Cdd:cd01359 401 RE-ALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
18-472 |
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: 670.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 18 MWGGRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFEWRIDLED 97
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 98 VHMNIESRLTQRIGI-AGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQP 176
Cdd:TIGR00838 81 IHMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 177 VTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAA 256
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 257 SLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQ 336
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 337 EDKEPLFDAIDTVRGSLMAFADMIPALVPNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGKDL 416
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844060874 417 SELTLEQLQQFSDLIQADVFEkALTLEASVNARNHIGGTAPAQVEAAIARAYVRLE 472
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYE-ALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG 455
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
12-473 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 605.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 12 QAQTSGMWGGRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFEW 91
Cdd:PLN02646 12 AAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 92 RIDLEDVHMNIESRLTQRIGIAGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHL 171
Cdd:PLN02646 92 RPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 172 QTAQPVTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIE 251
Cdd:PLN02646 172 QRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 252 FNAAASLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAY 331
Cdd:PLN02646 252 FLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 332 NKDNQEDKEPLFDAIDTVRGSLMAFADMIPALVPNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQ 411
Cdd:PLN02646 332 NRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAES 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844060874 412 EGKDLSELTLEQLQQFSDLIQADVFEkALTLEASVNARNHIGGTAPAQVEAAIA--RAYVRLEK 473
Cdd:PLN02646 412 KGCELSDLTLEDLKSINPVFEEDVYE-VLGVENSVEKFDSYGSTGSRSVLEQLEkwRTKLEITS 474
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
17-470 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 559.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 17 GMWGGRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFE-WRIDL 95
Cdd:PRK04833 2 ALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQiLASDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 96 EDVHMNIESRLTQRIGIAGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQ 175
Cdd:PRK04833 82 EDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 176 PVTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAA 255
Cdd:PRK04833 162 PVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 256 ASLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDN 335
Cdd:PRK04833 242 ASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 336 QEDKEPLFDAIDTVRGSLMAFADMIPALVPNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGKD 415
Cdd:PRK04833 322 QEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKP 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1844060874 416 LSELTLEQLQQFSDLIQADVFeKALTLEASVNARNHIGGTAPAQVEAAIARAYVR 470
Cdd:PRK04833 402 LEDLPLAELQKFSSVIGDDVY-PILSLQSCLDKRAAKGGVSPQQVAQAIAAAKAR 455
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
18-476 |
2.64e-172 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 498.15 E-value: 2.64e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 18 MWGGRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFE-WRIDLE 96
Cdd:PRK12308 3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQiLLSDAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 97 DVHMNIESRLTQRIGIAGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQP 176
Cdd:PRK12308 83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 177 VTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAA 256
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 257 SLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQ 336
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 337 EDKEPLFDAIDTVRGSLMAFADMIPALVPNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGKDL 416
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 417 SELTLEQLQQFSDLIQADVFEkALTLEASVNARNHIGGTAPAQVEAAIARAYVRLEKLYA 476
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQ-ILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAARDT 461
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-366 |
7.08e-140 |
|
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: 404.58 E-value: 7.08e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 45 YKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAGNFEWRIDLEDVHMNIESRLTQRIG-IAGKKLHTGRSR 123
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGeLNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 124 NDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCRKR 203
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 204 VNRMPLGSAALAGTTY--PIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILWTSAQFKFV 281
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 282 NIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQEDKEPLFDAIDTVRGSLMAFADMIP 361
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....*
gi 1844060874 362 ALVPN 366
Cdd:cd01334 321 GLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
21-315 |
1.60e-83 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 259.99 E-value: 1.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 21 GRFTEATDAFVAEFTASVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLRTIQAEIEAG-NFEWRIDLEDVH 99
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 100 MNIESRLTQRIGI-------AGKKLHTGRSRNDQVATDIRLYVRDEIDAILE-LLAKLQKGILSLAVKNTDTIMPGFTHL 171
Cdd:pfam00206 81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALSEVLLpALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 172 QTAQPVTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSAALAGTTYPIDRAYT-------AELLGFEAVSENSLDAVS 244
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAelvakelGFFTGLPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844060874 245 DRDFGIEFNAAASLIMMHLSRMSEELILWTSAQFKFVNIPDRFCT-GSSIMPQKKNPDVPELVRGKTGRVYG 315
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
54-471 |
2.48e-62 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 217.79 E-value: 2.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 54 AHATMLAKVGVLTESERDAITEGLRTIQaeiEAG--NFEWRIDLEDVHMNIESRLTQRIGI-AGKKLHTGRSRNDQVATD 130
Cdd:PRK02186 447 AHLVMLGDTGIVAPERARPLLDAHRRLR---DAGfaPLLARPAPRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATT 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 131 IRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLG 210
Cdd:PRK02186 524 TKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLG 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 211 SAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTG 290
Cdd:PRK02186 604 AGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGG 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 291 SSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKD-NQEDKEPLFDAIDTVRGSLMAFADMIPALVPNIEI 369
Cdd:PRK02186 684 SSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFSNSFEaGSPMNGPIAQACAAIEDAAAVLVLLIDGLEADQAR 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 370 MREAALRGFSTATDLADYLV-KNGVAFRDAHEIVGKAVALGVQEGKDLSELTLEQLQQFSDLIQADvFEKALTLEasvna 448
Cdd:PRK02186 764 MRAHLEDGGVSATAVAESLVvRRSISFRSAHTQVGQAIRQSLDQGRSSADALAALDPQFVSRAPLE-WARSHRFG----- 837
|
410 420
....*....|....*....|...
gi 1844060874 449 rnhiGGTAPAQVEAAIARAYVRL 471
Cdd:PRK02186 838 ----GGPGAADLNAGLARACAAL 856
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
54-464 |
2.60e-60 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 205.60 E-value: 2.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 54 AHATMLAKVGVLTESERDAITEGLRTIqAEIEAGNFEWRIDLEDVHMNIESRLTQRIGIAG-KKLHTGRSRNDQVATDIR 132
Cdd:PRK06705 47 AHIVMLTEENLMKKEEAKFILHALKKV-EEIPEEQLLYTEQHEDLFFLVEHLISQEAKSDFvSNMHIGRSRNDMGVTMYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 133 LYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCRKRVNRMPLGSA 212
Cdd:PRK06705 126 MSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 213 ALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILWTSAQFKFVNIPDRFCTGSS 292
Cdd:PRK06705 206 ALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 293 IMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQEDKEP-LFDAID-TVRGSLMAFAdMIPALVPNIEIM 370
Cdd:PRK06705 286 IMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEkAIRVFCIMNA-VIRTMKVEEDTL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 371 REAALRGFSTATDLADYLVKN-GVAFRDAHEIVGKAVALGVQEGKDLSELTLEQL-----QQFSDLIQADVFEKALTLEA 444
Cdd:PRK06705 365 KRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVniylqEKFKIQLLEKEWEEIISPEA 444
|
410 420
....*....|....*....|
gi 1844060874 445 SVNARNHIGGTAPAQVEAAI 464
Cdd:PRK06705 445 FIQKRNVYGGPSKKEMERMI 464
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
100-353 |
1.15e-59 |
|
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: 195.52 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 100 MNIESRLTQRIGIAGKKLH------TGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQT 173
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 174 AQPVTFGHHLLAWFEMLVRDSERLidcrkrvnrmplgsaalagttypiDRAYTAELLGfeavsensldavsdrdfgiefn 253
Cdd:cd01594 94 AQPVTLGYELRAWAQVLGRDLERL------------------------EEAAVAEALD---------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 254 aAASLIMMHLSRMSEELILWTSAQFKFVNIPD-RFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYN 332
Cdd:cd01594 128 -ALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDN 206
|
250 260
....*....|....*....|.
gi 1844060874 333 KDNQEDKEPLFDAIDTVRGSL 353
Cdd:cd01594 207 EDSPSMREILADSLLLLIDAL 227
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
27-430 |
3.52e-39 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 146.96 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 27 TDAFVAEftaSVQFDQRFYKQDIAGSIAHATMLAKVGVLTESERDAITEGLrtiqAEIEAGNFEWRIDLEDVHMNIESRL 106
Cdd:PRK06389 17 YDNIVKD---DIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINAL----IDIYKNGIEIDLDLEDVHTAIENFV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 107 TQRIGIAGKKLHTGRSRNDQVATDIRLYVrdeIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFG---HHL 183
Cdd:PRK06389 90 IRRCGDMFKNFRLFLSRNEQVHADLNLFI---IDKIIEIEKILYEIIKVIPGFNLKGRLPGYTHFRQAMPMTVNtyiNYI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 184 LAWFEMLVRDSER-LIDCRKrvnrMPLGSAALAGTTYPIDRAYTAELLGFEAVSENSLDAVSDRDFGIEfNAAASL--IM 260
Cdd:PRK06389 167 KSILYHHINNLDSfLMDLRE----MPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIE-NISYLIssLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 261 MHLSRMSEELILWTSAQFkfVNIPDRFCTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKGQPLAYNKDNQEDKE 340
Cdd:PRK06389 242 VDLSRICQDIIIYYENGI--ITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHRDFQIVKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 341 PLFDAIDTVRGSLMAFADMIPALvpNIEIMREAALRGFSTATDLADYLVKNGVAFRDAHEIVGKAvalgVQEGKDLSELT 420
Cdd:PRK06389 320 STISFINNFERILLGLPDLLYNI--KFEITNEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNK----IREGEVLDEYQ 393
|
410
....*....|
gi 1844060874 421 LEQLQQFSDL 430
Cdd:PRK06389 394 PEDLTDYIDV 403
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
378-446 |
6.21e-32 |
|
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: 116.36 E-value: 6.21e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844060874 378 FSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGKDLSELTLEQLQQFSDLIQADVFEkALTLEASV 446
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYE-ALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
113-466 |
9.67e-26 |
|
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: 109.26 E-value: 9.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 113 AGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVR 192
Cdd:cd01597 89 AGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 193 DSERLIDCRKRVNRMPLGSAA-----LAGTTYPIDRAYTAEL-LGFEAVSENsldavSDRDFGIEFNAAASLIMMHLSRM 266
Cdd:cd01597 169 HRERLDELRPRVLVVQFGGAAgtlasLGDQGLAVQEALAAELgLGVPAIPWH-----TARDRIAELASFLALLTGTLGKI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 267 SEELILWTSAQFKFVNIPDRFCTG-SSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMKgqplaynKDNQEDK------ 339
Cdd:cd01597 244 ARDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMV-------QEHERDAgawhae 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 340 -EPLFDAIDTVRGSLMAFADMIPALVPNIEIMRE--AALRGF----STATDLADYLVKNgvafrDAHEIVGKAVALGVQE 412
Cdd:cd01597 317 wIALPEIFLLASGALEQAEFLLSGLEVNEDRMRAnlDLTGGLilseAVMMALAPKLGRQ-----EAHDLVYEACMRAVEE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1844060874 413 GKDLSELTLEQLQQFSDLIQADvfekaltLEASVNARNHIgGTAPAQVEAAIAR 466
Cdd:cd01597 392 GRPLREVLLEDPEVAAYLSDEE-------LDALLDPANYL-GSAPALVDRVLAR 437
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
120-423 |
2.60e-25 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 108.15 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 120 GRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLID 199
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 200 CRKRVNRMPLGSAALaGTTYPIDRAYT-------AELLGFEAV-SENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELI 271
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEYIervvkhlAAITGLPLVgAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 272 LWTS---AQFKFVNIPDRFCtGSSIMPQKKNPDVPELVRGKTGRVYG-DLMSLLTLMKGQ-------PL-AYNkdnqedk 339
Cdd:PRK13353 297 LLSSgprTGLGEINLPAVQP-GSSIMPGKVNPVMPEVVNQIAFQVIGnDVTITLAAEAGQlelnvmePViAFN------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 340 epLFDAIDTVRGSLMAFAD-MIPALVPNIEIMREAALRGFSTATDLADYLvkngvafrdAHEIVGKAVALGVQEGKDLSE 418
Cdd:PRK13353 369 --LLESISILTNACRAFTDnCVKGIEANEERCKEYVEKSVGIATALNPHI---------GYEAAARIAKEAIATGRSVRE 437
|
....*
gi 1844060874 419 LTLEQ 423
Cdd:PRK13353 438 LALEN 442
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
59-324 |
3.85e-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: 100.66 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 59 LAKVGVLTESERDAITEGLRTIQ------AEIEAgnfEWRIDLedvhMNIESRLTQRIG-IAGKKLHTGRSRNDQVATDI 131
Cdd:cd01595 25 QAELGLIPKEAAEEIRAAADVFEidaeriAEIEK---ETGHDV----IAFVYALAEKCGeDAGEYVHFGATSQDINDTAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 132 RLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCRKRVNRM---- 207
Cdd:cd01595 98 ALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGgisg 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 208 PLGSAALAGTTYPIDRAYTAELLGFEAvsENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILWTSAQFKFVN---IP 284
Cdd:cd01595 178 AVGTHASLGPKGPEVEERVAEKLGLKV--PPITTQIEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVEepfEK 255
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1844060874 285 DRfcTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLM 324
Cdd:cd01595 256 GQ--VGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL 293
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
53-463 |
6.07e-22 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 97.85 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 53 IAHATMLAKVGVLTESERDAITEGLRTIQ------AEIEA--GNfewridleDVhMNIESRLTQRIGIAGKK-LHTGrsr 123
Cdd:COG0015 29 IALAEAQAELGLIPAEAAAAIRAAADDFEidaeriKEIEKetRH--------DV-KAFVYALKEKVGAEAGEyIHFG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 124 ndqvAT--DI-----RLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSER 196
Cdd:COG0015 97 ----ATsqDIndtalALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 197 LIDCRKRVnrmPLGsaALAGT--TY-------PIDRAYTAELLGFEAVSENSldAVSDRDFGIEFNAAASLIMMHLSRMS 267
Cdd:COG0015 173 LEEARERV---LVG--KIGGAvgTYaahgeawPEVEERVAEKLGLKPNPVTT--QIEPRDRHAELFSALALIAGSLEKIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 268 EELILWTSAQFKFVN---IPDRfcTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSLLTLMkgqplaynkdNQED------ 338
Cdd:COG0015 246 RDIRLLQRTEVGEVEepfAKGQ--VGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHerdlsd 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 339 ----KEPLFDAIDTVRGSLMAFADMIPALVPNIEIMRE--AALRGFSTATDLADYLVKNGVAFRDAHEIVgKAVALGV-Q 411
Cdd:COG0015 314 ssveRNILPDAFLLLDGALERLLKLLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELV-KELARGAwE 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1844060874 412 EGKDLSELtLEQLQQFSDLIQADvfekalTLEASVNARNHIgGTAPAQVEAA 463
Cdd:COG0015 393 EGNDLREL-LAADPEIPAELSKE------ELEALFDPANYL-GAADEIVDRV 436
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
120-424 |
1.24e-21 |
|
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: 97.21 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 120 GRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLID 199
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 200 CRKRVNRMPLGSAALaGTTYPIDRAYT-------AELLGFE-AVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELI 271
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPPGYIelvveklSEITGLPlKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 272 LWTS---AQFKFVNIPDRfCTGSSIMPQKKNPDVPELVRGKTGRVYG-DLMSLLTLMKGQ-------PL-AYNkdnqedk 339
Cdd:cd01357 292 LLSSgprAGLGEINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGnDLTITMAAEAGQlelnvfePViAYN------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 340 epLFDAIDTVRGSLMAFAD-MIPALVPNIEIMREAALRGFSTATDLADYLvkngvAFRDAHEIVGKAVALG------VQE 412
Cdd:cd01357 364 --LLESIDILTNAVRTLRErCIDGITANEERCREYVENSIGIVTALNPYI-----GYEAAAEIAKEALETGrsvrelVLE 436
|
330
....*....|..
gi 1844060874 413 GKDLSELTLEQL 424
Cdd:cd01357 437 EGLLTEEELDEI 448
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
106-300 |
2.43e-18 |
|
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: 86.45 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 106 LTQRIGIAGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLA 185
Cdd:cd01360 74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFAL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 186 WFEMLVRDSERLIDCRKRVNRM----PLGSAALAGttyPIDRAYTAELLGFEAVSENSldAVSDRDFGIEFNAAASLIMM 261
Cdd:cd01360 154 WYAEFKRHLERLKEARERILVGkisgAVGTYANLG---PEVEERVAEKLGLKPEPIST--QVIQRDRHAEYLSTLALIAS 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844060874 262 HLSRMSEEL-------ILWTSAQFkfvnipDRFCTGSSIMPQKKNP 300
Cdd:cd01360 229 TLEKIATEIrhlqrteVLEVEEPF------SKGQKGSSAMPHKRNP 268
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
122-444 |
2.01e-17 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 84.33 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 122 SRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCR 201
Cdd:COG1027 137 STNDVYPTAIRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 202 KRVNRMPLGSAAlAGTTYPIDRAYT-------AELLGFE-AVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILW 273
Cdd:COG1027 217 ELLREVNLGGTA-IGTGLNAPPGYIelvvehlAEITGLPlVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 274 TS---AQFKFVNIPDRfCTGSSIMPQKKNPDVPELVRGKTGRVYG-DLmsLLTLM--KGQ-------PL-AYNkdnqedk 339
Cdd:COG1027 296 SSgprAGLGEINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGnDL--TVTMAaeAGQlelnvfePViAYN------- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 340 epLFDAIDTVRGSLMAFADM-IPALVPNIEIMREAALRGFSTATDLADYLvknGvafrdaHEIVGKAVALGVQEGKDLSE 418
Cdd:COG1027 366 --LLESIELLTNACRTLREKcIDGITANEERCREYVENSIGLVTALNPYI---G------YEKAAEIAKEALATGKSVRE 434
|
330 340
....*....|....*....|....*.
gi 1844060874 419 LTLEQlqqfsDLIQADVFEKALTLEA 444
Cdd:COG1027 435 LVLEK-----GLLTEEELDEILDPEN 455
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
122-424 |
4.74e-16 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 80.17 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 122 SRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCR 201
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 202 KRVNRMPLGSAAlAGTTYPIDRAYT-------AELLGFE-AVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILW 273
Cdd:PRK12273 222 ELLREVNLGATA-IGTGLNAPPGYIelvveklAEITGLPlVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 274 TS---AQFKFVNIPDRfCTGSSIMPQKKNPDVPELVRGKTGRVYG-DLMSLLTLMKGQ-------PL-AYNkdnqedkep 341
Cdd:PRK12273 301 SSgprAGLNEINLPAV-QAGSSIMPGKVNPVIPEVVNQVCFQVIGnDTTVTMAAEAGQlelnvmePViAYN--------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 342 LFDAIDTVRGSLMAFADM-IPALVPNIEIMREAALRGFSTATDLADYLvkngvAFRDAHEIVGKAVALG------VQEGK 414
Cdd:PRK12273 371 LFESISILTNACRTLREKcIDGITANEERCREYVENSIGIVTALNPYI-----GYENAAEIAKEALETGksvrelVLERG 445
|
330
....*....|
gi 1844060874 415 DLSELTLEQL 424
Cdd:PRK12273 446 LLTEEELDDI 455
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
122-422 |
7.30e-14 |
|
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: 73.23 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 122 SRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDCR 201
Cdd:cd01596 135 SNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 202 KRVNRMPLGSAALaGT---TYP--IDR--AYTAELLGFE-AVSENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILW 273
Cdd:cd01596 215 ERLRELNLGGTAV-GTglnAPPgyAEKvaAELAELTGLPfVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 274 TS---AQFKFVNIPDRfCTGSSIMPQKKNPDVPELVRGKTGRVYG-DL-MSL--------LTLMKgqPL-AYNkdnqedk 339
Cdd:cd01596 294 SSgprAGLGEINLPAN-QPGSSIMPGKVNPVIPEAVNMVAAQVIGnDTaITMagsagqleLNVFK--PViAYN------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 340 epLFDAIDTVRGSLMAFAD-MIPALVPNIEIMREAALRGFSTATDLADYLvkngvAFRDAHEIVGKAVAlgvqEGKDLSE 418
Cdd:cd01596 364 --LLQSIRLLANACRSFRDkCVEGIEANEERCKEYVENSLMLVTALNPHI-----GYEKAAEIAKEALK----EGRTLRE 432
|
....
gi 1844060874 419 LTLE 422
Cdd:cd01596 433 AALE 436
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
121-316 |
1.10e-13 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 73.11 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 121 RSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLIDC 200
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 201 RKRVNRMPLGSAALaGTTYPIDR-------AYTAELLGFEAVSENSL-DAVSDRDFGIEFNAAASLIMMHLSRMSEELIL 272
Cdd:PRK14515 225 RQHLYEVNMGATAV-GTGLNADPeyieavvKHLAAISELPLVGAEDLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844060874 273 WTS---AQFKFVNIPDRfCTGSSIMPQKKNPDVPELVRGKTGRVYGD 316
Cdd:PRK14515 304 MASgprVGLAEIMLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIGN 349
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
113-448 |
1.10e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 69.66 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 113 AGKKLHTGRSRNDQVATDIRLYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVR 192
Cdd:PRK09053 98 AARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 193 DSERLIDCRKRVNRMPLGSAA-----LAGTTYPIDRAYTAEL-LGFEAVSENsldavSDRDFGIEFNAAASLIMMHLSRM 266
Cdd:PRK09053 178 HRQRLAALRPRALVLQFGGAAgtlasLGEQALPVAQALAAELqLALPALPWH-----TQRDRIAEFASALGLLAGTLGKI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 267 SEELILWTSAQFKFVNIPDRFCT-GSSIMPQKKNPDVPELVRGKTGRVYGdLMSllTLMKGQPLAYNKDN---QEDKEPL 342
Cdd:PRK09053 253 ARDVSLLMQTEVGEVFEPAAAGKgGSSTMPHKRNPVGCAAVLTAATRAPG-LVA--TLFAAMPQEHERALggwHAEWDTL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 343 FDAIDTVRGSLMAFADMIPALVPNIEIMRE------AALRGFSTATDLADYLVKNgvafrDAHEIVGKAVALGVQEGKDL 416
Cdd:PRK09053 330 PELACLAAGALAQMAQIVEGLEVDAARMRAnldlthGLILAEAVMLALADRIGRL-----DAHHLVEQASKRAVAEGRHL 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1844060874 417 -----------SELTLEQLQQFSD----LIQADVF-EKALTLEASVNA 448
Cdd:PRK09053 405 rdvlaedpqvsAHLSPAALDRLLDpahyLGQAHAWvDRVLAEHASRHA 452
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
133-300 |
5.46e-08 |
|
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: 55.02 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 133 LYVRDEIDAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLidcRKRVNRMPLGSA 212
Cdd:cd03302 106 IQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNL---ERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 213 alAGTT---------YPIDRAYTAEL-------LGFEAVSeNSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELILWtsA 276
Cdd:cd03302 183 --KGTTgtqasfldlFEGDHDKVEALdelvtkkAGFKKVY-PVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL--A 257
|
170 180
....*....|....*....|....*
gi 1844060874 277 QFKFVNIP-DRFCTGSSIMPQKKNP 300
Cdd:cd03302 258 NLKEVEEPfEKGQIGSSAMPYKRNP 282
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
120-304 |
7.67e-08 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 54.70 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 120 GRSRNDQVATDIRLYVRDEI-DAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLI 198
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIhSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 199 DCRKRVNRMPLGSAALaGTTYPIDRAYT-------AELLGFEAVS-ENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEEL 270
Cdd:PLN00134 209 CTLPRLYELAQGGTAV-GTGLNTKKGFDekiaaavAEETGLPFVTaPNKFEALAAHDAFVELSGALNTVAVSLMKIANDI 287
|
170 180 190
....*....|....*....|....*....|....*..
gi 1844060874 271 ILWTS---AQFKFVNIPDRfCTGSSIMPQKKNPDVPE 304
Cdd:PLN00134 288 RLLGSgprCGLGELNLPEN-EPGSSIMPGKVNPTQCE 323
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
120-304 |
8.36e-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: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 120 GRSRNDQVATDIRlyvrdeIDAILEL-------LAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVR 192
Cdd:cd01362 133 SQSSNDTFPTAMH------IAAALALqerllpaLKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 193 DSERLIDCRKRVNRMPLGSAALaGT---TYP-IDR---AYTAELLGFEAVS-ENSLDAVSDRDFGIEFNA-----AASLi 259
Cdd:cd01362 207 AIARIEAALPRLYELALGGTAV-GTglnAHPgFAEkvaAELAELTGLPFVTaPNKFEALAAHDALVEASGalktlAVSL- 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844060874 260 mMHLSR----MSE-------ELILWTsaqfkfvNIPdrfctGSSIMPQKKNPDVPE 304
Cdd:cd01362 285 -MKIANdirwLGSgprcglgELSLPE-------NEP-----GSSIMPGKVNPTQCE 327
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
60-304 |
4.83e-06 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 48.93 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 60 AKVGVLTESERDAIteglrtIQA--EIEAGNFEWRIDLeDV---------HMN----IESRLTQRIG---IAGKKLH--- 118
Cdd:PRK00485 60 AELGLLDAEKADAI------VAAadEVIAGKHDDHFPL-DVwqtgsgtqsNMNvnevIANRASELLGgelGSKKPVHpnd 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 119 ---TGRSRNDQVATDIRLYVRDEIDAilELLAKLQKGILSLAVKNT---DTIMPGFTHLQTAQPVTFGHHLLAWFEMLVR 192
Cdd:PRK00485 133 hvnMSQSSNDTFPTAMHIAAVLAIVE--RLLPALEHLRDTLAAKAEefaDIVKIGRTHLQDATPLTLGQEFSGYAAQLEH 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 193 DSERLIDCRKRVNRMPLGSAAlAGT---TYP--IDR--AYTAELLGFEAVS-ENSLDAVSDRDFGIEFNA-----AASLi 259
Cdd:PRK00485 211 GIERIEAALPHLYELALGGTA-VGTglnAHPgfAERvaEELAELTGLPFVTaPNKFEALAAHDALVEASGalktlAVSL- 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844060874 260 mMHLS---R-MSE-------ELILWTsaqfkfvNIPdrfctGSSIMPQKKNPDVPE 304
Cdd:PRK00485 289 -MKIAndiRwLASgprcglgEISLPE-------NEP-----GSSIMPGKVNPTQCE 331
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
290-453 |
1.97e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 45.79 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 290 GSSIMPQKKNPDVPELVRGktgrvygdlmsLLTLMKGQPLAYNKDNQEDKEP-----------LFDAIDTVRGSLMAFAD 358
Cdd:PRK08937 58 GSSAMPHKRNPIGSERITG-----------LARVLRSYLVTALENVPLWHERdlshssaeriaLPDAFLALDYILNRFVN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 359 MIPALVPNIEIMRE--AALRGFSTATDLADYLVKNGVAFRDAHEIVGKAVALGVQEGKDLSELtleqlqqfsdLIQADVF 436
Cdd:PRK08937 127 ILENLVVFPENIERnlDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWKNQKDLREL----------LEADERF 196
|
170 180
....*....|....*....|
gi 1844060874 437 EKALT---LEASVNARNHIG 453
Cdd:PRK08937 197 TKQLTkeeLDELFDPEAFVG 216
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
131-300 |
2.90e-05 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 46.46 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 131 IRLYVRDEIDA-ILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFemlvrdsERLIDCRKRVNRMPL 209
Cdd:cd01598 109 YALMIKEARNEvILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFV-------YRLERQYKQLKQIEI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 210 gSAALAGTTypidRAYTAELLGFEAVSENSLDAVSDRDFGIEFNAAASLIMMH---------LSRMSEELI-----LWT- 274
Cdd:cd01598 182 -LGKFNGAV----GNFNAHLVAYPDVDWRKFSEFFVTSLGLTWNPYTTQIEPHdyiaelfdaLARINTILIdlcrdIWGy 256
|
170 180
....*....|....*....|....*..
gi 1844060874 275 -SAQFkFVNIPDRFCTGSSIMPQKKNP 300
Cdd:cd01598 257 iSLGY-FKQKVKKGEVGSSTMPHKVNP 282
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
120-422 |
1.02e-04 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 44.53 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 120 GRSRNDQVATDIRLYVRDEI-DAILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHHLLAWFEMLVRDSERLI 198
Cdd:PRK12425 135 SQSSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 199 DCRKRVNRMPLGSAALA-GTTYP--IDRAYTAELLGFEAV----SENSLDAVSDRDFGIEFNAAASLIMMHLSRMSEELI 271
Cdd:PRK12425 215 AALPAVCELAQGGTAVGtGLNAPhgFAEAIAAELAALSGLpfvtAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 272 LWTS---AQFKFVNIPDRFcTGSSIMPQKKNPDVPELVRGKTGRVYGDLMSL--------LTLMKGQP-LAYNkdnqedk 339
Cdd:PRK12425 295 LLGSgprAGLAEVRLPANE-PGSSIMPGKVNPTQCEALSMLACQVMGNDATIgfaasqghLQLNVFKPvIIHN------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 340 epLFDAIDTVRGSLMAFAD-MIPALVPNIEIMREAALRGFSTATDLADYlvkngVAFRDAHEIVGKAVAlgvqEGKDLSE 418
Cdd:PRK12425 367 --LLQSIRLLADGCRNFQQhCVAGLEPDAEQMAAHLERGLMLVTALNPH-----IGYDKAAEIAKKAYA----EGTTLRE 435
|
....
gi 1844060874 419 LTLE 422
Cdd:PRK12425 436 AALA 439
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
133-300 |
1.68e-03 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 40.88 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 133 LYVRDEIDA-ILELLAKLQKGILSLAVKNTDTIMPGFTHLQTAQPVTFGHhllawfEMLVRdSERLIDCRKRVNRMPL-G 210
Cdd:PLN02848 136 LMLKEGVNSvVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGK------EMANF-AYRLSRQRKQLSEVKIkG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844060874 211 SAALAGTTYPID-RAYTAelLGFEAVSENSLdavsdRDFGIEFNAAASLIMMH---------LSRMSEELI-----LWTS 275
Cdd:PLN02848 209 KFAGAVGNYNAHmSAYPE--VDWPAVAEEFV-----TSLGLTFNPYVTQIEPHdymaelfnaVSRFNNILIdfdrdIWSY 281
|
170 180
....*....|....*....|....*...
gi 1844060874 276 ---AQFKFVNIPDRfcTGSSIMPQKKNP 300
Cdd:PLN02848 282 islGYFKQITKAGE--VGSSTMPHKVNP 307
|
|
| |
