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Conserved domains on  [gi|78706858|ref|NP_001027234|]
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argininosuccinate lyase, isoform B [Drosophila melanogaster]

Protein Classification

argininosuccinate lyase( domain architecture ID 10102141)

argininosuccinate lyase catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 30-461 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: 619.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  30 SLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDEDVHTVNERLLVEITGELGQR 109
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 110 LHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQR 189
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 190 LLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTK 269
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 270 EFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQYDKQFCFQSFDKLSQVLEVT 349
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 350 DGVLQTIQVKQESMEAALSTD-MLATDWAYYLVK-KGVPFRQAHHIIGRVVSEAEKRGVDITDLPLGDLQKFSPLFGSDI 427
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGfSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 78706858 428 VAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKC 461
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARAL 434
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 30-461 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: 619.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  30 SLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDEDVHTVNERLLVEITGELGQR 109
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 110 LHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQR 189
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 190 LLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTK 269
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 270 EFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQYDKQFCFQSFDKLSQVLEVT 349
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 350 DGVLQTIQVKQESMEAALSTD-MLATDWAYYLVK-KGVPFRQAHHIIGRVVSEAEKRGVDITDLPLGDLQKFSPLFGSDI 427
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGfSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 78706858 428 VAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKC 461
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARAL 434
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 10-467 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: 613.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  10 KMWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDE 89
Cdd:COG0165   4 KLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPELE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  90 DVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:COG0165  84 DIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQP 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:COG0165 164 VTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLSAA 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:COG0165 244 SLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDLQ 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESMEAALSTD-MLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:COG0165 324 EDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKDL 403

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706858 409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKCARDLAK 467
Cdd:COG0165 404 EDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 9-460 0e+00

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 593.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    9 YKMWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGD 88
Cdd:PRK00855   4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   89 EDVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQ 168
Cdd:PRK00855  84 EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  169 TVQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYC 248
Cdd:PRK00855 164 PVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLSA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  249 CSMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDL 328
Cdd:PRK00855 244 ASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRDL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  329 QYDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESMEAALSTDM-LATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVD 407
Cdd:PRK00855 324 QEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEERGVD 403

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 78706858  408 ITDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKK 460
Cdd:PRK00855 404 LADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKA 456
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 11-461 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: 544.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    11 MWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDED 90
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    91 VHTVNERLLVEITGE-LGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:TIGR00838  81 IHMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESM-EAALSTDMLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMeEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 78706858   409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKC 461
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKAR 453
Lyase_1 pfam00206
Lyase;
14-306 1.92e-87

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 270.01  E-value: 1.92e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    14 GRFTeGPHEALHSL-NNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKIL-PGDEDV 91
Cdd:pfam00206   1 GRFT-VPADALMGIfTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLkVWQEGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    92 HTVNERLLVEITGEL-------GQRLHTGRSRNDQVVTDMKLWLRKAIRETL-GRLSGIIETATRQAELHLGVLMPGYTH 163
Cdd:pfam00206  80 GTAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALSEVLlPALRQLIDALKEKAKEFADIVKPGRTH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   164 LQRAQTVQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRL-------WLAERLGFSGVTANSMHAV 236
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaelvakELGFFTGLPVKAPNSFEAT 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706858   237 GDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSS-GSSLMPQKRNPDSLELIRGMAGVI 306
Cdd:pfam00206 240 SDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRV 310
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 30-461 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: 619.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  30 SLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDEDVHTVNERLLVEITGELGQR 109
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 110 LHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQR 189
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 190 LLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTK 269
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 270 EFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQYDKQFCFQSFDKLSQVLEVT 349
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 350 DGVLQTIQVKQESMEAALSTD-MLATDWAYYLVK-KGVPFRQAHHIIGRVVSEAEKRGVDITDLPLGDLQKFSPLFGSDI 427
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGfSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 78706858 428 VAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKC 461
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARAL 434
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 10-467 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: 613.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  10 KMWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDE 89
Cdd:COG0165   4 KLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPELE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  90 DVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:COG0165  84 DIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQP 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:COG0165 164 VTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLSAA 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:COG0165 244 SLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDLQ 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESMEAALSTD-MLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:COG0165 324 EDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKDL 403

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706858 409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKCARDLAK 467
Cdd:COG0165 404 EDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 9-460 0e+00

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 593.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    9 YKMWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGD 88
Cdd:PRK00855   4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   89 EDVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQ 168
Cdd:PRK00855  84 EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  169 TVQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYC 248
Cdd:PRK00855 164 PVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLSA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  249 CSMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDL 328
Cdd:PRK00855 244 ASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRDL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  329 QYDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESMEAALSTDM-LATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVD 407
Cdd:PRK00855 324 QEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEERGVD 403

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 78706858  408 ITDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKK 460
Cdd:PRK00855 404 LADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKA 456
PLN02646 PLN02646
argininosuccinate lyase
 10-455 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 575.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   10 KMWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDE 89
Cdd:PLN02646  17 KLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEWRPDRE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   90 DVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:PLN02646  97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESMEAALSTDML-ATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 78706858  409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQL 455
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQL 463
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 11-461 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: 544.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    11 MWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDED 90
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    91 VHTVNERLLVEITGE-LGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:TIGR00838  81 IHMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESM-EAALSTDMLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMeEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 78706858   409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKKC 461
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKAR 453
PRK04833 PRK04833
argininosuccinate lyase; Provisional
 11-455 2.02e-152

argininosuccinate lyase; Provisional


Pssm-ID: 179883 [Multi-domain]  Cd Length: 455  Bit Score: 441.35  E-value: 2.02e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   11 MWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGD-E 89
Cdd:PRK04833   3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASDaE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   90 DVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:PRK04833  83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:PRK04833 163 VTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:PRK04833 243 SISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQES-MEAALSTDMLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:PRK04833 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRcQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 78706858  409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQL 455
Cdd:PRK04833 403 EDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAI 449
PRK12308 PRK12308
argininosuccinate lyase;
11-460 9.00e-142

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 419.57  E-value: 9.00e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   11 MWGGRFTEGPHEALHSLNNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGD-E 89
Cdd:PRK12308   3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSDaE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   90 DVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:PRK12308  83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  170 VQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCC 249
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQ 329
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  330 YDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQE-SMEAALSTDMLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDI 408
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGErTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 78706858  409 TDLPLGDLQKFSPLFGSDIVAVADYSNNVQQYNAIGGTASSSIVEQLRLLKK 460
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADK 454
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 41-358 5.97e-118

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: 348.34  E-value: 5.97e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  41 DLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKILPGDEDVHTVNERLLVEITGEL-GQRLHTGRSRNDQ 119
Cdd:cd01334   4 DLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSSNDI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 120 VVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQRLLELRDRANV 199
Cdd:cd01334  84 VDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLNV 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 200 LPLGSGALAG--NPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTKEFDFIKLA 277
Cdd:cd01334 164 LPLGGGAVGTgaNAPPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEVELP 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 278 DGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQYDKQFCFQSFDKLSQVLEVTDGVLQTIQ 357
Cdd:cd01334 244 DAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGLE 323


                .
gi 78706858 358 V 358
Cdd:cd01334 324 V 324
Lyase_1 pfam00206
Lyase;
14-306 1.92e-87

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 270.01  E-value: 1.92e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    14 GRFTeGPHEALHSL-NNSLPYDSRLYADDLDASKAYAEALHRAGLINSAEADKLVKNLELLRFDWIEGTVKIL-PGDEDV 91
Cdd:pfam00206   1 GRFT-VPADALMGIfTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLkVWQEGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    92 HTVNERLLVEITGEL-------GQRLHTGRSRNDQVVTDMKLWLRKAIRETL-GRLSGIIETATRQAELHLGVLMPGYTH 163
Cdd:pfam00206  80 GTAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALSEVLlPALRQLIDALKEKAKEFADIVKPGRTH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   164 LQRAQTVQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRL-------WLAERLGFSGVTANSMHAV 236
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaelvakELGFFTGLPVKAPNSFEAT 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706858   237 GDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSS-GSSLMPQKRNPDSLELIRGMAGVI 306
Cdd:pfam00206 240 SDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRV 310
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 14-416 3.44e-53

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 191.98  E-value: 3.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   14 GRFTEGPH-EALHSLNNSLPYDSRLYADD--LDASKAYAEALHRAGLINSAEADKLVKNLELLR---FDWIEGTVKilpg 87
Cdd:PRK02186 411 GAARPGLPpEAQAIVYGPGASEAPLAELDhlAAIDEAHLVMLGDTGIVAPERARPLLDAHRRLRdagFAPLLARPA---- 486

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   88 DEDVHTVNERLLVEITGE-LGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQR 166
Cdd:PRK02186 487 PRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQP 566

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  167 AQTVQFSHWLLSHAFALREDGQRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFI 246
Cdd:PRK02186 567 ALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFL 646

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  247 YCCSMVSLHLSRLAEDLIIYSTKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNK 326
Cdd:PRK02186 647 SAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFSNSF 726

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  327 DL-QYDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESMEAAL-STDMLATDWAYYLV-KKGVPFRQAHHIIGRVVSEAEK 403
Cdd:PRK02186 727 EAgSPMNGPIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLeDGGVSATAVAESLVvRRSISFRSAHTQVGQAIRQSLD 806

                        410
                 ....*....|...
gi 78706858  404 RGVDITDlPLGDL 416
Cdd:PRK02186 807 QGRSSAD-ALAAL 818
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 96-348 3.11e-50

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: 170.87  E-value: 3.11e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  96 ERLLVEITGELGQRLH------TGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQT 169
Cdd:cd01594  17 EEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQP 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 170 VQFSHWLLSHAFALREDGQRLLELrdranvlplgsgalagnplgidrlwlaerlgfsgvtansmhavgdrdFVVDFIYCC 249
Cdd:cd01594  97 VTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALDAL 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 250 SMVSLHLSRLAEDLIIYSTKEFDFIKLADG-FSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDL 328
Cdd:cd01594 130 ALAAAHLSKIAEDLRLLLSGEFGELGEPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDS 209

                       250       260
                ....*....|....*....|
gi 78706858 329 QYDKQFCFQSFDKLSQVLEV 348
Cdd:cd01594 210 PSMREILADSLLLLIDALRL 229
PRK06389 PRK06389
argininosuccinate lyase; Provisional
 10-432 2.83e-45

argininosuccinate lyase; Provisional


Pssm-ID: 235791 [Multi-domain]  Cd Length: 434  Bit Score: 163.53  E-value: 2.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   10 KMWGGrftegphEALHSLNNSlPYDSrLYADDLDASK-----------AYAEALHRAGLINSAEADKLVKNLellrFDWI 78
Cdd:PRK06389   2 KIWSG-------GAGEELEND-FYDN-IVKDDIDADKnlikyeiinllAYHVALAQRRLITEKAPKCVINAL----IDIY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   79 EGTVKILPGDEDVHTVNERLLVEITGELGQRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATrqaELHLGVLM 158
Cdd:PRK06389  69 KNGIEIDLDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIP---GFNLKGRL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  159 PGYTHLQRAQTVQFSHW----LLSHAFALREDGQRLLELRdranVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMH 234
Cdd:PRK06389 146 PGYTHFRQAMPMTVNTYinyiKSILYHHINNLDSFLMDLR----EMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVY 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  235 AVGDRDF-VVDFIYCCSMVSLHLSRLAEDLIIYSTKefDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGI 313
Cdd:PRK06389 222 SSSLYIKtIENISYLISSLAVDLSRICQDIIIYYEN--GIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFI 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  314 MMTIKGTPSTYNKDLQYDKQFCFQSFDKLSQVLEVTDGVLQTIQVKQESmEAALSTDMLATDWAYYLVKKGVPFRQAHHI 393
Cdd:PRK06389 300 AQSELNKTTGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITN-EKNIKNSVYATYNAWLAFKNGMDWKSAYAY 378

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 78706858  394 IGRVVSEAEkrgvditdlplgDLQKFSPLFGSDIVAVAD 432
Cdd:PRK06389 379 IGNKIREGE------------VLDEYQPEDLTDYIDVNE 405
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 37-419 2.07e-40

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 151.68  E-value: 2.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   37 LYADDLDASKAYAEALHRAGLINSAEADKLVKNLEllrfdwiegTVKILPGD--------EDVHTVNERLLV-EITGELG 107
Cdd:PRK06705  37 LLKDMFQVHKAHIVMLTEENLMKKEEAKFILHALK---------KVEEIPEEqllyteqhEDLFFLVEHLISqEAKSDFV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  108 QRLHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDG 187
Cdd:PRK06705 108 SNMHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  188 QRLLELRDRANVLPLGSGALAGNPLGIDRLWLAERLGFSGVTANSMHAVGDRDFVVDFIYCCSMVSLHLSRLAEDLIIYS 267
Cdd:PRK06705 188 ERMKKTYKLLNQSPMGAAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  268 TKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIKGTPSTYNKDLQYDKQ-FCFQSFDKLSQVL 346
Cdd:PRK06705 268 TKEYDGITVARPYVQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQpYLYKGIEKAIRVF 347

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706858  347 EVTDGVLQTIQVKQESMEA-ALSTDMLATDWAYYLVKK-GVPFRQAHHIIGRVVSEAEKRGVDITDLPLGDLQKF 419
Cdd:PRK06705 348 CIMNAVIRTMKVEEDTLKRrSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIY 422
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 42-394 1.27e-27

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: 113.37  E-value: 1.27e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  42 LDASKAYAEALHRAGLINSAEADKLVKNLELLRFDW-----IEGTVKilpgdedvHTVN--ERLLVEITGELGQR-LHTG 113
Cdd:cd01595  15 LDVEAALAEAQAELGLIPKEAAEEIRAAADVFEIDAeriaeIEKETG--------HDVIafVYALAEKCGEDAGEyVHFG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 114 RSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQRLLEL 193
Cdd:cd01595  87 ATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEA 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 194 RDRANVLPLG--SGALA---GNPLGIDRLwLAERLGFsGVTANSMHAVgDRDFVVDFIYCCSMVSLHLSRLAEDLIIYST 268
Cdd:cd01595 167 RERVLVGGISgaVGTHAslgPKGPEVEER-VAEKLGL-KVPPITTQIE-PRDRIAELLSALALIAGTLEKIATDIRLLQR 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 269 KEFDFIKLadGFSS---GSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIkgtpstyNKDLQYD------KQFCF-QS 338
Cdd:cd01595 244 TEIGEVEE--PFEKgqvGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-------VQWHERDlsdssvERNILpDA 314

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706858 339 FDKLSQVLEVTDGVLQTIQVKQESMEAALSTD---------MLAtdwayyLVKKGVPFRQAHHII 394
Cdd:cd01595 315 FLLLDAALSRLQGLLEGLVVNPERMRRNLDLTwglilseavMMA------LAKKGLGRQEAYELV 373
ASL_C2 pfam14698
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ...
 371-437 4.36e-27

Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of argininosuccinate lyase.


Pssm-ID: 464268 [Multi-domain]  Cd Length: 68  Bit Score: 103.27  E-value: 4.36e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706858   371 MLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDITDLPLGDLQKFSPLFGSDIVAVADYSNNV 437
Cdd:pfam14698   2 STATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 42-314 2.43e-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: 110.80  E-value: 2.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  42 LDASKAYAEALHRAGLINSAEADKLVKNLELLRFDW---IEGTVKIlpGDEDVHTVNErLLVEITGELGQRLHTGRSRND 118
Cdd:cd01597  25 LDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLealAEATART--GHPAIPLVKQ-LTAACGDAAGEYVHWGATTQD 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 119 QVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQRLLELRDRAN 198
Cdd:cd01597 102 IIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVL 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 199 VLPLG--SGALAGnpLGIDRL----WLAERLGFsGVTANSMHAvgDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTKEFD 272
Cdd:cd01597 182 VVQFGgaAGTLAS--LGDQGLavqeALAAELGL-GVPAIPWHT--ARDRIAELASFLALLTGTLGKIARDVYLLMQTEIG 256

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 78706858 273 fiKLADGFSSG---SSLMPQKRNPDSLELIRGMAGVITANLTGIM 314
Cdd:cd01597 257 --EVAEPFAKGrggSSTMPHKRNPVGCELIVALARRVPGLAALLL 299
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 47-317 7.55e-23

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: 100.54  E-value: 7.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  47 AYAEALHRAGLINSAEADKLVKNLELLRFDW-----IEGTVKilpgdedvHTV--NERLLVEITG-ELGQRLHTGRSRND 118
Cdd:COG0015  30 ALAEAQAELGLIPAEAAAAIRAAADDFEIDAerikeIEKETR--------HDVkaFVYALKEKVGaEAGEYIHFGATSQD 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 119 qvVTD--MKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQRLLELRDR 196
Cdd:COG0015 102 --INDtaLALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARER 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 197 ANVLPLGsGAlAGNPLGIDRLW------LAERLGFSGVTANSMHAvgDRDFVVDFIYCCSMVSLHLSRLAEDLIIYSTKE 270
Cdd:COG0015 180 VLVGKIG-GA-VGTYAAHGEAWpeveerVAEKLGLKPNPVTTQIE--PRDRHAELFSALALIAGSLEKIARDIRLLQRTE 255

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 78706858 271 FDFikLADGFSS---GSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTI 317
Cdd:COG0015 256 VGE--VEEPFAKgqvGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL 303
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 42-311 6.51e-18

adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273345 [Multi-domain]  Cd Length: 435  Bit Score: 85.86  E-value: 6.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858    42 LDASKAYAEALHRAGLINSAEADKL-----VKNLELLRFDWIEGTVKilpgdEDVHTVnERLLVEITGELGQRLHTGRSR 116
Cdd:TIGR00928  24 LDVEVAVLRALAELGVIPAEAVKEIrekanFTEVDLERIKEIEAVTR-----HDVKAV-VYALKEKCGAEGEFIHFGATS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   117 NDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQRLLELRDR 196
Cdd:TIGR00928  98 NDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKER 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   197 anvLPLG--SGA----LAGNPLG--IDRLwLAERLGFSGVTANSMhaVGDRDFVVDFIYCCSMVSLHLSRLAEDLIIY-S 267
Cdd:TIGR00928 178 ---IKVGgiSGAvgthAAAYPLVeeVEER-VTEFLGLKPVPISTQ--IEPRDRHAELLDALALLATTLEKFAVDIRLLqR 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 78706858   268 TKEFDFIKLADGFSSGSSLMPQKRNPDSLELIRGMAGVITANLT 311
Cdd:TIGR00928 252 TEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYAS 295
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 42-309 3.31e-15

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 77.21  E-value: 3.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  42 LDASKAYAEALHRAGLINSAEADKLVKNLE--LLRFDWIEGTVKilpgdedvHTVNE--RLLVEITGELGQRLHTGRSRN 117
Cdd:cd01360  21 LEVEAAVCEAWAKLGVIPAEAAEEIRKKAKfdVERVKEIEAETK--------HDVIAfvTAIAEYCGEAGRYIHFGLTSS 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 118 DQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAFALREDGQRLLELRDRA 197
Cdd:cd01360  93 DVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERI 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 198 NVLPLgSGALaGN----PLGIDRlWLAERLGFSGVTANSMhaVGDRDFVVDFiyccsmvslhLSRLAedlIIYSTKEfdf 273
Cdd:cd01360 173 LVGKI-SGAV-GTyanlGPEVEE-RVAEKLGLKPEPISTQ--VIQRDRHAEY----------LSTLA---LIASTLE--- 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 78706858 274 iKLA---------------DGFSS---GSSLMPQKRNPDSLELIRGMAGVITAN 309
Cdd:cd01360 232 -KIAteirhlqrtevleveEPFSKgqkGSSAMPHKRNPILSENICGLARVIRSN 284
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 110-308 5.62e-12

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 67.35  E-value: 5.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  110 LHTGRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTV----QFSHWLlshaFALRE 185
Cdd:PRK09053 102 VHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVtlglKFAGWL----DALLR 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  186 DGQRLLELRDRANVLPLG--SGALAGnpLGIDRLWLAERLGFS---GVTANSMHAvgDRDFVVDFIYCCSMVSLHLSRLA 260
Cdd:PRK09053 178 HRQRLAALRPRALVLQFGgaAGTLAS--LGEQALPVAQALAAElqlALPALPWHT--QRDRIAEFASALGLLAGTLGKIA 253

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 78706858  261 EDLIIYSTKEFD--FIKLADGfSSGSSLMPQKRNPdsleliRGMAGVITA 308
Cdd:PRK09053 254 RDVSLLMQTEVGevFEPAAAG-KGGSSTMPHKRNP------VGCAAVLTA 296
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 104-303 2.10e-11

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 65.08  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  104 GELGQRLHTGRSRNDqvVTDMKLWLR-KAIRETL-GRLSGIIETATRQAELHLGVLMPGYTHLQRAQTVQFSHWLLSHAF 181
Cdd:PRK05975  96 EEAAAHVHFGATSQD--VIDTSLMLRlKAASEILaARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  182 ALREDGQRLLELRDRANVLPLGSGALAGNPLG----IDRLWLAERLGFsgvtANSMHAVGDRDFVVDFIYCCSMVSLHLS 257
Cdd:PRK05975 174 PLLRHRDRLEALRADVFPLQFGGAAGTLEKLGgkaaAVRARLAKRLGL----EDAPQWHSQRDFIADFAHLLSLVTGSLG 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 78706858  258 RLAEDLIIYSTKEfDFIKLADGfsSGSSLMPQKRNPDSLELIRGMA 303
Cdd:PRK05975 250 KFGQDIALMAQAG-DEISLSGG--GGSSAMPHKQNPVAAETLVTLA 292
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 46-315 4.11e-10

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 61.54  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858   46 KAYAEALHRAGLINSAEADKLVKN-LELLRFDWIEG-TVKILPGDEDVHT---VNE----RLLVEITGELGQRLHT---- 112
Cdd:PRK13353  54 KAAALANADLGLLPRRIAEAIVQAcDEILAGKLHDQfIVDPIQGGAGTSTnmnANEvianRALELLGGEKGDYHYVspnd 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  113 ----GRSRNDQVVTDMKLWLRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQTV----QFSHWllshAFALR 184
Cdd:PRK13353 134 hvnmAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPItlgqEFSAY----ARALK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  185 EDGQRLLELRDRANVLPLGSGALaGNPLGIDRLW-------LAERLGFSGVTA-NSMHAVGDRDFVVDFIYCCSMVSLHL 256
Cdd:PRK13353 210 RDRKRIQQAREHLYEVNLGGTAV-GTGLNADPEYiervvkhLAAITGLPLVGAeDLVDATQNTDAFVEVSGALKVCAVNL 288

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706858  257 SRLAEDLIIYSTKE---FDFIKLAdGFSSGSSLMPQKRNPDSLELIRGMAGVITANLTGIMM 315
Cdd:PRK13353 289 SKIANDLRLLSSGPrtgLGEINLP-AVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITL 349
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 283-437 1.04e-06

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 49.26  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  283 GSSLMPQKRNPDSLELIRGMAGVITANLTGIMMTIkgtpSTYN-KDLQYDKQ---FCFQSFDKLSQVLEVTDGVLQTIQV 358
Cdd:PRK08937  58 GSSAMPHKRNPIGSERITGLARVLRSYLVTALENV----PLWHeRDLSHSSAeriALPDAFLALDYILNRFVNILENLVV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858  359 KQESMEAALSTD---MLATDWAYYLVKKGVPFRQAHHIIGRVVSEAEKRGVDITDLPLGDLQKFSPLFGSDIVAVADYSN 435
Cdd:PRK08937 134 FPENIERNLDKTlgfIATERVLLELVEKGMGREEAHELIREKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFDPEA 213


                 ..
gi 78706858  436 NV 437
Cdd:PRK08937 214 FV 215
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 128-437 9.09e-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: 44.62  E-value: 9.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 128 LRKAIRETLGRLSGIIETATRQAELHLGVLMPGYTHLQRAQ--TV--QFSHWLLSHAFALREDGQRLLELRDRANVLPLG 203
Cdd:cd03302 108 IRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQltTVgkRACLWIQDLLMDLRNLERLRDDLRFRGVKGTTG 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 204 SGA-----LAGNPLGIDRL--WLAERLGFSGVTaNSMHAVGDRDFVVDFIYCCSMVSLHLSRLAEDL-IIYSTKEfdfik 275
Cdd:cd03302 188 TQAsfldlFEGDHDKVEALdeLVTKKAGFKKVY-PVTGQTYSRKVDIDVLNALSSLGATAHKIATDIrLLANLKE----- 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 276 LADGFSS---GSSLMPQKRNPDSLELIRGMAGVitanLTGIMMTIKGTPSTynkdlQYDKQFCFQSFDK---LSQVLEVT 349
Cdd:cd03302 262 VEEPFEKgqiGSSAMPYKRNPMRSERCCSLARH----LMNLASNAAQTAST-----QWFERTLDDSANRriaIPEAFLAA 332

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706858 350 DGVLQTIQ-------VKQESMEAALSTD---MLATDWAYYLVKKGVPFRQAHHIIgRVVSEAEKRGV-------DITDLP 412
Cdd:cd03302 333 DAILITLQniseglvVYPKVIERHIRQElpfMATENIIMAAVKAGGDRQDAHERI-RVLSHQAAAVVkqeggdnDLIERI 411

                       330       340
                ....*....|....*....|....*
gi 78706858 413 LGDlQKFSPLFGsDIVAVADYSNNV 437
Cdd:cd03302 412 KND-AYFKPIWD-ELDALLDPKTFI 434
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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