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Conserved domains on  [gi|68303549|ref|NP_001020117|]
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argininosuccinate lyase isoform 3 [Homo sapiens]

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 ...
 27-433 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: 630.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  27 SIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWIL------------ 174
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLayaemlerdler 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 175 --------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 240
Cdd:cd01359 161 ladaykrvnvsplgAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 241 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVA 320
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 321 TGVISTLQIHQENMGQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDV 398
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 68303549 399 ICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 433
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-433 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: 630.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  27 SIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWIL------------ 174
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLayaemlerdler 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 175 --------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 240
Cdd:cd01359 161 ladaykrvnvsplgAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 241 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVA 320
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 321 TGVISTLQIHQENMGQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDV 398
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 68303549 399 ICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 433
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
PLN02646 PLN02646
argininosuccinate lyase
 1-437 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 623.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    1 MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFK 80
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   81 LNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTH 160
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  161 LQRAQPIRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA 214
Cdd:PLN02646 171 LQRAQPVLLSHWLLshveqlerdagrlvdcrprvnfcplgSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  215 EFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST 294
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  295 YNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAE 373
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68303549  374 TKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQ 437
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 5-438 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: 621.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   5 SGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSN 84
Cdd:COG0165   2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  85 DEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:COG0165  82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 165 QPIRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 218
Cdd:COG0165 162 QPVTFGHHLLayaemllrdrerladaykrlnvsplgAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 219 WASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 298
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 299 LQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 377
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68303549 378 ALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA 438
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 8-433 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: 541.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549     8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDED 87
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    88 IHTANERRLKELIGATAG-KLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:TIGR00838  81 IHMAIERELIDRVGEDLGgKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   167 IRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 220
Cdd:TIGR00838 161 ITLAHHLLayaemllrdyerlqdalkrvnvsplgSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   221 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 300
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   301 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 379
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 68303549   380 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 433
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
Lyase_1 pfam00206
Lyase;
11-279 6.31e-117

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 344.35  E-value: 6.31e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    11 GRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQG-TFKLNSNDEDIH 89
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    90 TANERRLKELIG-------ATAGKLHTGRSRNDQVVTDLRLWMRQTCST-LSGLLWELIRTMVDRAEAERDVLFPGYTHL 161
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   162 QRAQPIRWSHW--------------------------ILSGAIAGNPLGVDRE---LLRAELNF----GAITLNSMDATS 208
Cdd:pfam00206 161 QDATPVTLGQElsgyavaltrdrerlqqllprllvlpLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68303549   209 ERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYST-GSSLMPQKKNPDSLELIRSKAGRVFG 279
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-433 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: 630.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  27 SIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWIL------------ 174
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLayaemlerdler 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 175 --------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 240
Cdd:cd01359 161 ladaykrvnvsplgAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 241 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVA 320
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 321 TGVISTLQIHQENMGQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDV 398
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 68303549 399 ICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 433
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
PLN02646 PLN02646
argininosuccinate lyase
 1-437 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 623.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    1 MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFK 80
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   81 LNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTH 160
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  161 LQRAQPIRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA 214
Cdd:PLN02646 171 LQRAQPVLLSHWLLshveqlerdagrlvdcrprvnfcplgSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  215 EFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST 294
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  295 YNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAE 373
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68303549  374 TKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQ 437
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 5-438 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: 621.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   5 SGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSN 84
Cdd:COG0165   2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  85 DEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:COG0165  82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 165 QPIRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 218
Cdd:COG0165 162 QPVTFGHHLLayaemllrdrerladaykrlnvsplgAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 219 WASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 298
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 299 LQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 377
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68303549 378 ALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA 438
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 5-434 0e+00

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 602.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    5 SGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSN 84
Cdd:PRK00855   3 SNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   85 DEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:PRK00855  83 LEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  165 QPIRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 218
Cdd:PRK00855 163 QPVTFGHHLLayaemlardlerlrdarkrvnrsplgSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  219 WASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 298
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  299 LQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDM-LATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 377
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68303549  378 ALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQ 434
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 8-433 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: 541.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549     8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDED 87
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    88 IHTANERRLKELIGATAG-KLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:TIGR00838  81 IHMAIERELIDRVGEDLGgKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   167 IRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 220
Cdd:TIGR00838 161 ITLAHHLLayaemllrdyerlqdalkrvnvsplgSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   221 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 300
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   301 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 379
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 68303549   380 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 433
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
PRK04833 PRK04833
argininosuccinate lyase; Provisional
 8-437 2.12e-154

argininosuccinate lyase; Provisional


Pssm-ID: 179883 [Multi-domain]  Cd Length: 455  Bit Score: 445.20  E-value: 2.12e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFK-LNSNDE 86
Cdd:PRK04833   3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQiLASDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   87 DIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:PRK04833  83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  167 IRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 220
Cdd:PRK04833 163 VTFAHWCLayvemlardesrlqdalkrldvsplgSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  221 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 300
Cdd:PRK04833 243 SISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  301 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 379
Cdd:PRK04833 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYAnATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68303549  380 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTArssvdwqIRQVR-ALLQAQQ 437
Cdd:PRK04833 403 EDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVS-------PQQVAqAIAAAKA 454
PRK12308 PRK12308
argininosuccinate lyase;
8-438 1.66e-134

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 399.93  E-value: 1.66e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEE-WAQGTFKLNSNDE 86
Cdd:PRK12308   3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEvMEDPEQILLSDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   87 DIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:PRK12308  83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  167 IRWSHWIL--------------------------SGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 220
Cdd:PRK12308 163 VTFAHWCLayvemferdysrledaltrldtcplgSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  221 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 300
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  301 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 379
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYAnATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68303549  380 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA 438
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAARDT 461
Lyase_1 pfam00206
Lyase;
11-279 6.31e-117

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 344.35  E-value: 6.31e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    11 GRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQG-TFKLNSNDEDIH 89
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    90 TANERRLKELIG-------ATAGKLHTGRSRNDQVVTDLRLWMRQTCST-LSGLLWELIRTMVDRAEAERDVLFPGYTHL 161
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   162 QRAQPIRWSHW--------------------------ILSGAIAGNPLGVDRE---LLRAELNF----GAITLNSMDATS 208
Cdd:pfam00206 161 QDATPVTLGQElsgyavaltrdrerlqqllprllvlpLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68303549   209 ERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYST-GSSLMPQKKNPDSLELIRSKAGRVFG 279
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 35-330 5.54e-115

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: 339.86  E-value: 5.54e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  35 WEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIG-ATAGKLHTGRSR 113
Cdd:cd01334   1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGeLNGGYVHTGRSS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 114 NDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWIL------------------- 174
Cdd:cd01334  81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAawaaelerdlerleealkr 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 175 -------SGAIAGNPLGV--DRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFV 245
Cdd:cd01334 161 lnvlplgGGAVGTGANAPpiDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 246 QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVIS 325
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320


                ....*
gi 68303549 326 TLQIH 330
Cdd:cd01334 321 GLEVN 325
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 93-321 1.62e-57

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: 188.97  E-value: 1.62e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  93 ERRLKELIGATAGKLH------TGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:cd01594  17 EEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQP 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 167 IRWSHWILSGAIAgnpLGVDRELLRaelnfgaitlnsmDAtserdFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQ 246
Cdd:cd01594  97 VTLGYELRAWAQV---LGRDLERLE-------------EA-----AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELG 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68303549 247 LSDA-YSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVAT 321
Cdd:cd01594 156 EPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 103-438 5.28e-46

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 170.41  E-value: 5.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  103 TAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILS------- 175
Cdd:PRK02186 506 VGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAvdgalar 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  176 -------------------GAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLIL 236
Cdd:PRK02186 586 ethalfalfehidvcplgaGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQL 665

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  237 YCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPstYNKDLQEDKEAVFEVSDTMSAV 316
Cdd:PRK02186 666 WTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMNGPIAQACAAI 743

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  317 ---LQVATGVISTLQIHQENMGQAL-SPDMLATDLAYYLV-RKGMPFRQAHEASGKAVfmaeTKGVALNQLSLQELQTIS 391
Cdd:PRK02186 744 edaAAVLVLLIDGLEADQARMRAHLeDGGVSATAVAESLVvRRSISFRSAHTQVGQAI----RQSLDQGRSSADALAALD 819

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 68303549  392 PLFSGDVICVWDYGHsveQYGalGGTARSSVDWQIRQVRALLQAQQA 438
Cdd:PRK02186 820 PQFVSRAPLEWARSH---RFG--GGPGAADLNAGLARACAALRDDEA 861
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 40-387 2.58e-31

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 125.48  E-value: 2.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   40 QGSKAYSRGLEKAGLLTKAEMDQILHGLDKVaEEWAQGTFKLNSNDEDIHTANERRL-KELIGATAGKLHTGRSRNDQVV 118
Cdd:PRK06705  43 QVHKAHIVMLTEENLMKKEEAKFILHALKKV-EEIPEEQLLYTEQHEDLFFLVEHLIsQEAKSDFVSNMHIGRSRNDMGV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  119 TDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILS----------------------- 175
Cdd:PRK06705 122 TMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAiydtmqrdlermkktykllnqsp 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  176 ---GAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYS 252
Cdd:PRK06705 202 mgaAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYV 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  253 TGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEA-VFEVSDTMSAVLQVATGVISTLQIHQ 331
Cdd:PRK06705 282 QISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEE 361

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 68303549  332 ENM-GQALSPDMLATDLAYYLVRK-GMPFRQAHEASGKAVFMAETKGVALNQLSLQEL 387
Cdd:PRK06705 362 DTLkRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDV 419
PRK06389 PRK06389
argininosuccinate lyase; Provisional
 7-369 6.85e-29

argininosuccinate lyase; Provisional


Pssm-ID: 235791 [Multi-domain]  Cd Length: 434  Bit Score: 117.69  E-value: 6.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549    7 KLWGGrfvGAVDPIMEKFNAS-----IAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAeewaQGTFKL 81
Cdd:PRK06389   2 KIWSG---GAGEELENDFYDNivkddIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIY----KNGIEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   82 NSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDraeAERDVLFPGYTHL 161
Cdd:PRK06389  75 DLDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIPG---FNLKGRLPGYTHF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  162 QRAQPIR---WSHWILS-----------------------GAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAE 215
Cdd:PRK06389 152 RQAMPMTvntYINYIKSilyhhinnldsflmdlrempygyGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  216 FLFW--ASLCMThLSRMAEDLILYctKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPS 293
Cdd:PRK06389 232 NISYliSSLAVD-LSRICQDIIIY--YENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTT 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68303549  294 TYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENmGQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAV 369
Cdd:PRK06389 309 GYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITN-EKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKI 383
ASL_C2 pfam14698
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ...
 342-408 4.03e-28

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


Pssm-ID: 464268 [Multi-domain]  Cd Length: 68  Bit Score: 105.58  E-value: 4.03e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68303549   342 MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDVICVWDYGHSV 408
Cdd:pfam14698   2 STATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 44-363 1.61e-19

Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176467 [Multi-domain]  Cd Length: 381  Bit Score: 89.49  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  44 AYSRGLEKAGLLTK---AEMDQILHGLDKVAEEWAQGTFKLNsndediHT--ANERRLKELIGATAGK-LHTGRSRNDQV 117
Cdd:cd01595  20 ALAEAQAELGLIPKeaaEEIRAAADVFEIDAERIAEIEKETG------HDviAFVYALAEKCGEDAGEyVHFGATSQDIN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 118 VTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSH----WI-------------------- 173
Cdd:cd01595  94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKkfavWAaellrhlerleearervlvg 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 174 -LSGA------IAGNPLGVDRELLrAELNFGAITLNSMdaTSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQ 246
Cdd:cd01595 174 gISGAvgthasLGPKGPEVEERVA-EKLGLKVPPITTQ--IEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVE 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 247 L-SDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLkglpstyNKDLQED-------KEAVFEVSDTMSAVLQ 318
Cdd:cd01595 251 EpFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-------VQWHERDlsdssveRNILPDAFLLLDAALS 323

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 68303549 319 VATGVISTLQIHQENMGQALS---PDMLATDLAYYLVRKGMPFRQAHE 363
Cdd:cd01595 324 RLQGLLEGLVVNPERMRRNLDltwGLILSEAVMMALAKKGLGRQEAYE 371
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 44-387 3.32e-17

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: 83.21  E-value: 3.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  44 AYSRGLEKAGLLTKAEMDQIlhglDKVAEEwaqGTFKLNSNDEDIHTAN------ERRLKELIGATAGK-LHTGRSRNDq 116
Cdd:COG0015  30 ALAEAQAELGLIPAEAAAAI----RAAADD---FEIDAERIKEIEKETRhdvkafVYALKEKVGAEAGEyIHFGATSQD- 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 117 vVTD--LRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWshwilsG---AIAGNPLGVDRELL- 190
Cdd:COG0015 102 -INDtaLALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTF------GkklAVWAAELLRQLERLe 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 191 --RAELNFGAI-----TLNSMDA-----------------------TSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 240
Cdd:COG0015 175 eaRERVLVGKIggavgTYAAHGEawpeveervaeklglkpnpvttqIEPRDRHAELFSALALIAGSLEKIARDIRLLQRT 254

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 241 EFSFV-QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLkglpstynkdLQEdkeavFEVSDTMSAV--- 316
Cdd:COG0015 255 EVGEVeEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASW-----HERDLSDSSVern 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 317 ------------LQVATGVISTLQIHQENMGQALS---PDMLATDLAYYLVRKGMPFRQAHEASGKAvfmaeTKGVALNQ 381
Cdd:COG0015 320 ilpdafllldgaLERLLKLLEGLVVNPERMRANLDltgGLVLSEAVLMALVRRGLGREEAYELVKEL-----ARGAWEEG 394


                ....*.
gi 68303549 382 LSLQEL 387
Cdd:COG0015 395 NDLREL 400
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 94-339 1.44e-14

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: 75.36  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  94 RRLKELIGATAGK-LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSH- 171
Cdd:cd01597  79 KQLTAACGDAAGEyVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLk 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 172 ---WI---------------------LSGAiAGN--PLGVD----RELLRAELNFGAITLNSMdatSERDFVAEFLFWAS 221
Cdd:cd01597 159 vavWLsellrhrerldelrprvlvvqFGGA-AGTlaSLGDQglavQEALAAELGLGVPAIPWH---TARDRIAELASFLA 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 222 LCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTG-SSLMPQKKNPDSLELIRSKAGRVFGRCAGLlmtLKGLPSTYNKDLQ 300
Cdd:cd01597 235 LLTGTLGKIARDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALL---LDAMVQEHERDAG 311

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 68303549 301 EDK---EAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALS 339
Cdd:cd01597 312 AWHaewIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLD 353
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 96-363 6.62e-08

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: 54.48  E-value: 6.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  96 LKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSH---- 171
Cdd:cd01360  74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLkfal 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 172 W-----------------ILSGAIAGnPLGvdrellraelNFGAIT------------LNSMDATSE---RDFVAEFLFW 219
Cdd:cd01360 154 WyaefkrhlerlkearerILVGKISG-AVG----------TYANLGpeveervaeklgLKPEPISTQviqRDRHAEYLST 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 220 ASLCMTHLSRMAEDL-------ILYCTKEFSFVQlsdaysTGSSLMPQKKNPDSLElirskagrvfgRCAGLLMTLKGL- 291
Cdd:cd01360 223 LALIASTLEKIATEIrhlqrteVLEVEEPFSKGQ------KGSSAMPHKRNPILSE-----------NICGLARVIRSNv 285

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549 292 -PSTYNKDLQEDK-------EAVF--EVSDTMSAVLQVATGVISTLQIHQENMGQAL---------SPDMLAtdlayyLV 352
Cdd:cd01360 286 iPALENVALWHERdishssvERVIlpDATILLDYILRRMTRVLENLVVYPENMRRNLnltkglifsQRVLLA------LV 359

                       330
                ....*....|.
gi 68303549 353 RKGMPFRQAHE 363
Cdd:cd01360 360 EKGMSREEAYE 370
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 94-274 6.99e-06

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 47.74  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   94 RRLKELIGATAG-KLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTM--VDRAEAERDVLfpGYTHLQRAQPIRWS 170
Cdd:PRK05975  88 RQLRAAVGEEAAaHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLdaLEATFGQNALM--GHTRMQAAIPITVA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  171 HWILS------------------------GAIAGN--PLGVDRELLRAELnfgAITLNSMDAT---SERDFVAEFLFWAS 221
Cdd:PRK05975 166 DRLASwrapllrhrdrlealradvfplqfGGAAGTleKLGGKAAAVRARL---AKRLGLEDAPqwhSQRDFIADFAHLLS 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68303549  222 LCMTHLSRMAEDLILyctkefsFVQLSDAYST----GSSLMPQKKNPDSLELIRSKA 274
Cdd:PRK05975 243 LVTGSLGKFGQDIAL-------MAQAGDEISLsgggGSSAMPHKQNPVAAETLVTLA 292
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 254-363 2.97e-05

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 45.02  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  254 GSSLMPQKKNPDSLELIRSKAGRVFGRcagLLMTLKGLPSTYNKDLQEDKE---AVFEVSDTMSAVLQVATGVISTLQIH 330
Cdd:PRK08937  58 GSSAMPHKRNPIGSERITGLARVLRSY---LVTALENVPLWHERDLSHSSAeriALPDAFLALDYILNRFVNILENLVVF 134

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 68303549  331 QENMGQAL---SPDMLATDLAYYLVRKGMPFRQAHE 363
Cdd:PRK08937 135 PENIERNLdktLGFIATERVLLELVEKGMGREEAHE 170
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 91-279 1.15e-04

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 44.20  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549   91 ANE---RRLKELIGATAGK---LH------TGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGY 158
Cdd:PRK13353 107 ANEviaNRALELLGGEKGDyhyVSpndhvnMAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGR 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303549  159 THLQRAQPIR-------WSHWI------------------LSGAIAGNPLGVDRE-LLRAELNFGAIT-------LNSMD 205
Cdd:PRK13353 187 TQLQDAVPITlgqefsaYARALkrdrkriqqarehlyevnLGGTAVGTGLNADPEyIERVVKHLAAITglplvgaEDLVD 266

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68303549  206 ATSERDFVAEFLFWASLCMTHLSRMAEDLILY----CTKeFSFVQLSdAYSTGSSLMPQKKNPDSLELIRSKAGRVFG 279
Cdd:PRK13353 267 ATQNTDAFVEVSGALKVCAVNLSKIANDLRLLssgpRTG-LGEINLP-AVQPGSSIMPGKVNPVMPEVVNQIAFQVIG 342
 
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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