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Conserved domains on  [gi|31541964|ref|NP_000039|]
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argininosuccinate lyase isoform 1 [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 ...
 27-459 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: 683.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  27 SIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 187 LLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 266
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 267 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVA 346
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 347 TGVISTLQIHQENMGQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDV 424
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 31541964 425 ICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 459
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-459 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: 683.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  27 SIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 187 LLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 266
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 267 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVA 346
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 347 TGVISTLQIHQENMGQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDV 424
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 31541964 425 ICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 459
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
PLN02646 PLN02646
argininosuccinate lyase
 1-463 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 672.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    1 MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFK 80
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   81 LNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTH 160
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  161 LQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA 240
Cdd:PLN02646 171 LQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  241 EFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST 320
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  321 YNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAE 399
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31541964  400 TKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQ 463
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 5-464 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: 672.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   5 SGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSN 84
Cdd:COG0165   2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  85 DEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:COG0165  82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 165 QPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 244
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 245 WASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 324
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 325 LQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 403
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31541964 404 ALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA 464
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 8-459 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: 590.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964     8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDED 87
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    88 IHTANERRLKELIGATAG-KLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:TIGR00838  81 IHMAIERELIDRVGEDLGgKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   167 IRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   247 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   327 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 31541964   406 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 459
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
Lyase_1 pfam00206
Lyase;
11-305 1.10e-134

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 390.58  E-value: 1.10e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    11 GRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQG-TFKLNSNDEDIH 89
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    90 TANERRLKELIG-------ATAGKLHTGRSRNDQVVTDLRLWMRQTCST-LSGLLWELIRTMVDRAEAERDVLFPGYTHL 161
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   162 QRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRE---LLRAELNF----GAITLNSMDATS 234
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31541964   235 ERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYST-GSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-459 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: 683.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  27 SIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 187 LLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTK 266
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 267 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVA 346
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 347 TGVISTLQIHQENMGQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDV 424
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 31541964 425 ICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 459
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
PLN02646 PLN02646
argininosuccinate lyase
 1-463 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 672.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    1 MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFK 80
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   81 LNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTH 160
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  161 LQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA 240
Cdd:PLN02646 171 LQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  241 EFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST 320
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  321 YNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAE 399
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31541964  400 TKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQ 463
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 5-464 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: 672.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   5 SGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSN 84
Cdd:COG0165   2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  85 DEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:COG0165  82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 165 QPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 244
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 245 WASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 324
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 325 LQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 403
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31541964 404 ALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA 464
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 5-460 0e+00

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 651.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    5 SGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSN 84
Cdd:PRK00855   3 SNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   85 DEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:PRK00855  83 LEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  165 QPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 244
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  245 WASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 324
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  325 LQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDM-LATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 403
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31541964  404 ALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQ 460
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 8-459 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: 590.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964     8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDED 87
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    88 IHTANERRLKELIGATAG-KLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:TIGR00838  81 IHMAIERELIDRVGEDLGgKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   167 IRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   247 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   327 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 31541964   406 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALL 459
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
PRK04833 PRK04833
argininosuccinate lyase; Provisional
 8-463 1.65e-167

argininosuccinate lyase; Provisional


Pssm-ID: 179883 [Multi-domain]  Cd Length: 455  Bit Score: 479.48  E-value: 1.65e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFK-LNSNDE 86
Cdd:PRK04833   3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQiLASDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   87 DIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:PRK04833  83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  167 IRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:PRK04833 163 VTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  247 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:PRK04833 243 SISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  327 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:PRK04833 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYAnATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 31541964  406 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTArssvdwqIRQVR-ALLQAQQ 463
Cdd:PRK04833 403 EDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVS-------PQQVAqAIAAAKA 454
PRK12308 PRK12308
argininosuccinate lyase;
8-464 1.60e-147

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 434.21  E-value: 1.60e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    8 LWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEE-WAQGTFKLNSNDE 86
Cdd:PRK12308   3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEvMEDPEQILLSDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   87 DIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:PRK12308  83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  167 IRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  247 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  327 EDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYAnATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 31541964  406 NQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA 464
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAARDT 461
Lyase_1 pfam00206
Lyase;
11-305 1.10e-134

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 390.58  E-value: 1.10e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    11 GRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQG-TFKLNSNDEDIH 89
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    90 TANERRLKELIG-------ATAGKLHTGRSRNDQVVTDLRLWMRQTCST-LSGLLWELIRTMVDRAEAERDVLFPGYTHL 161
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   162 QRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRE---LLRAELNF----GAITLNSMDATS 234
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31541964   235 ERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYST-GSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 35-356 4.97e-133

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: 386.86  E-value: 4.97e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  35 WEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIG-ATAGKLHTGRSR 113
Cdd:cd01334   1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGeLNGGYVHTGRSS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 114 NDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKR 193
Cdd:cd01334  81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 194 INVLPLGSGAIAGNPLGV--DRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFV 271
Cdd:cd01334 161 LNVLPLGGGAVGTGANAPpiDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 272 QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVIS 351
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320


                ....*
gi 31541964 352 TLQIH 356
Cdd:cd01334 321 GLEVN 325
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 93-347 4.36e-58

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: 191.28  E-value: 4.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  93 ERRLKELIGATAGKLH------TGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:cd01594  17 EEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQP 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 167 IRWSHWILSHAVALTRDSERLLEVrkrinvlplgsgaiagnplgvdrellraelnfgaitlnsmdatserdFVAEFLFWA 246
Cdd:cd01594  97 VTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALDAL 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 247 SLCMTHLSRMAEDLILYCTKEFSFVQLSDA-YSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDL 325
Cdd:cd01594 130 ALAAAHLSKIAEDLRLLLSGEFGELGEPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDS 209

                       250       260
                ....*....|....*....|..
gi 31541964 326 QEDKEAVFEVSDTMSAVLQVAT 347
Cdd:cd01594 210 PSMREILADSLLLLIDALRLLL 231
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 103-464 8.27e-56

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 199.30  E-value: 8.27e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  103 TAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTR 182
Cdd:PRK02186 506 VGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALAR 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  183 DSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLIL 262
Cdd:PRK02186 586 ETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQL 665

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  263 YCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPstYNKDLQEDKEAVFEVSDTMSAV 342
Cdd:PRK02186 666 WTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMNGPIAQACAAI 743

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  343 ---LQVATGVISTLQIHQENMGQAL-SPDMLATDLAYYLV-RKGMPFRQAHEASGKAVfmaeTKGVALNQLSLQELQTIS 417
Cdd:PRK02186 744 edaAAVLVLLIDGLEADQARMRAHLeDGGVSATAVAESLVvRRSISFRSAHTQVGQAI----RQSLDQGRSSADALAALD 819

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 31541964  418 PLFSGDVICVWDYGHsveQYGalGGTARSSVDWQIRQVRALLQAQQA 464
Cdd:PRK02186 820 PQFVSRAPLEWARSH---RFG--GGPGAADLNAGLARACAALRDDEA 861
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 40-413 2.60e-40

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 151.29  E-value: 2.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   40 QGSKAYSRGLEKAGLLTKAEMDQILHGLDKVaEEWAQGTFKLNSNDEDIHTANERRL-KELIGATAGKLHTGRSRNDQVV 118
Cdd:PRK06705  43 QVHKAHIVMLTEENLMKKEEAKFILHALKKV-EEIPEEQLLYTEQHEDLFFLVEHLIsQEAKSDFVSNMHIGRSRNDMGV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  119 TDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLP 198
Cdd:PRK06705 122 TMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSP 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  199 LGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYS 278
Cdd:PRK06705 202 MGAAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYV 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  279 TGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEA-VFEVSDTMSAVLQVATGVISTLQIHQ 357
Cdd:PRK06705 282 QISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEE 361

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 31541964  358 ENM-GQALSPDMLATDLAYYLVRK-GMPFRQAHEASGKAVFMAETKGVALNQLSLQEL 413
Cdd:PRK06705 362 DTLkRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDV 419
PRK06389 PRK06389
argininosuccinate lyase; Provisional
 7-395 4.15e-34

argininosuccinate lyase; Provisional


Pssm-ID: 235791 [Multi-domain]  Cd Length: 434  Bit Score: 132.71  E-value: 4.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964    7 KLWGGrfvGAVDPIMEKFNAS-----IAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAeewaQGTFKL 81
Cdd:PRK06389   2 KIWSG---GAGEELENDFYDNivkddIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIY----KNGIEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   82 NSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDraeAERDVLFPGYTHL 161
Cdd:PRK06389  75 DLDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIPG---FNLKGRLPGYTHF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  162 QRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAE 241
Cdd:PRK06389 152 RQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  242 FLFW--ASLCMThLSRMAEDLILYctKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPS 319
Cdd:PRK06389 232 NISYliSSLAVD-LSRICQDIIIY--YENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTT 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31541964  320 TYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENmGQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAV 395
Cdd:PRK06389 309 GYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITN-EKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKI 383
ASL_C2 pfam14698
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ...
 368-434 7.63e-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: 105.19  E-value: 7.63e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31541964   368 MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDVICVWDYGHSV 434
Cdd:pfam14698   2 STATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 44-389 4.78e-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: 111.83  E-value: 4.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  44 AYSRGLEKAGLLTK---AEMDQILHGLDKVAEEWAQGTFKLNsndediHT--ANERRLKELIGATAGK-LHTGRSRNDQV 117
Cdd:cd01595  20 ALAEAQAELGLIPKeaaEEIRAAADVFEIDAERIAEIEKETG------HDviAFVYALAEKCGEDAGEyVHFGATSQDIN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 118 VTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVL 197
Cdd:cd01595  94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 198 ----PLGSGAIAG-NPLGVDRELLrAELNFGAITLNSMdaTSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQ 272
Cdd:cd01595 174 gisgAVGTHASLGpKGPEVEERVA-EKLGLKVPPITTQ--IEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVE 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 273 L-SDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLkglpstyNKDLQED-------KEAVFEVSDTMSAVLQ 344
Cdd:cd01595 251 EpFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-------VQWHERDlsdssveRNILPDAFLLLDAALS 323

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 31541964 345 VATGVISTLQIHQENMGQALS---PDMLATDLAYYLVRKGMPFRQAHE 389
Cdd:cd01595 324 RLQGLLEGLVVNPERMRRNLDltwGLILSEAVMMALAKKGLGRQEAYE 371
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 44-413 8.15e-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: 100.16  E-value: 8.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  44 AYSRGLEKAGLLTKAEMDQIlhglDKVAEEwaqGTFKLNSNDEDIHTAN------ERRLKELIGATAGK-LHTGRSRNDq 116
Cdd:COG0015  30 ALAEAQAELGLIPAEAAAAI----RAAADD---FEIDAERIKEIEKETRhdvkafVYALKEKVGAEAGEyIHFGATSQD- 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 117 vVTD--LRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRI 194
Cdd:COG0015 102 -INDtaLALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERV 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 195 NVLPLGsGAiAGN-------PLGVDRELLrAELNFGAitlnSMDAT--SERDFVAEFLFWASLCMTHLSRMAEDLILYCT 265
Cdd:COG0015 181 LVGKIG-GA-VGTyaahgeaWPEVEERVA-EKLGLKP----NPVTTqiEPRDRHAELFSALALIAGSLEKIARDIRLLQR 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 266 KEFSFV-QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLkglpstynkdLQEdkeavFEVSDTMSAV-- 342
Cdd:COG0015 254 TEVGEVeEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASW-----HERDLSDSSVer 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 343 -------------LQVATGVISTLQIHQENMGQALS---PDMLATDLAYYLVRKGMPFRQAHEASGKAvfmaeTKGVALN 406
Cdd:COG0015 319 nilpdafllldgaLERLLKLLEGLVVNPERMRANLDltgGLVLSEAVLMALVRRGLGREEAYELVKEL-----ARGAWEE 393


                ....*..
gi 31541964 407 QLSLQEL 413
Cdd:COG0015 394 GNDLREL 400
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 94-365 4.32e-22

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: 98.08  E-value: 4.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  94 RRLKELIGATAGK-LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHW 172
Cdd:cd01597  79 KQLTAACGDAAGEyVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLK 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 173 ILSHAVALTRDSERLLEVRKRINVLPLGsGAiAGN--PLGVD----RELLRAELNFGAITLNSMdatSERDFVAEFLFWA 246
Cdd:cd01597 159 VAVWLSELLRHRERLDELRPRVLVVQFG-GA-AGTlaSLGDQglavQEALAAELGLGVPAIPWH---TARDRIAELASFL 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 247 SLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTG-SSLMPQKKNPDSLELIRSKAGRVFGRCAGLlmtLKGLPSTYNKDL 325
Cdd:cd01597 234 ALLTGTLGKIARDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALL---LDAMVQEHERDA 310

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 31541964 326 QEDK---EAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALS 365
Cdd:cd01597 311 GAWHaewIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLD 353
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 96-389 4.28e-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: 76.82  E-value: 4.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  96 LKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILS 175
Cdd:cd01360  74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFAL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 176 HAVALTRDSERLLEVRKRINVLPLgSGAIaGN--PLGVDRELLRAELnfgaITLNSMDATSE---RDFVAEFLFWASLCM 250
Cdd:cd01360 154 WYAEFKRHLERLKEARERILVGKI-SGAV-GTyaNLGPEVEERVAEK----LGLKPEPISTQviqRDRHAEYLSTLALIA 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 251 THLSRMAEDL-------ILYCTKEFSFVQlsdaysTGSSLMPQKKNPDSLElirskagrvfgRCAGLLMTLKGL--PSTY 321
Cdd:cd01360 228 STLEKIATEIrhlqrteVLEVEEPFSKGQ------KGSSAMPHKRNPILSE-----------NICGLARVIRSNviPALE 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 322 NKDLQEDK-------EAVF--EVSDTMSAVLQVATGVISTLQIHQENMGQAL---------SPDMLAtdlayyLVRKGMP 383
Cdd:cd01360 291 NVALWHERdishssvERVIlpDATILLDYILRRMTRVLENLVVYPENMRRNLnltkglifsQRVLLA------LVEKGMS 364


                ....*.
gi 31541964 384 FRQAHE 389
Cdd:cd01360 365 REEAYE 370
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 91-305 4.54e-14

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 73.86  E-value: 4.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   91 ANE---RRLKELIGATAGK---LH------TGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGY 158
Cdd:PRK13353 107 ANEviaNRALELLGGEKGDyhyVSpndhvnMAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGR 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  159 THLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIaGNPLGVDRE-LLRAELNFGAIT-------LNSM 230
Cdd:PRK13353 187 TQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAV-GTGLNADPEyIERVVKHLAAITglplvgaEDLV 265

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31541964  231 DATSERDFVAEFLFWASLCMTHLSRMAEDLILY----CTKeFSFVQLSdAYSTGSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:PRK13353 266 DATQNTDAFVEVSGALKVCAVNLSKIANDLRLLssgpRTG-LGEINLP-AVQPGSSIMPGKVNPVMPEVVNQIAFQVIG 342
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 94-300 1.66e-11

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 65.46  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   94 RRLKELIGATAG-KLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTM--VDRAEAERDVLfpGYTHLQRAQPIRWS 170
Cdd:PRK05975  88 RQLRAAVGEEAAaHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLdaLEATFGQNALM--GHTRMQAAIPITVA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  171 HWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELnfgAITLNSMDAT---SERDFVAEFLFWAS 247
Cdd:PRK05975 166 DRLASWRAPLLRHRDRLEALRADVFPLQFGGAAGTLEKLGGKAAAVRARL---AKRLGLEDAPqwhSQRDFIADFAHLLS 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31541964  248 LCMTHLSRMAEDLILyctkefsFVQLSDAYST----GSSLMPQKKNPDSLELIRSKA 300
Cdd:PRK05975 243 LVTGSLGKFGQDIAL-------MAQAGDEISLsgggGSSAMPHKQNPVAAETLVTLA 292
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 49-305 3.27e-11

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 65.02  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964   49 LEKAGLLTKAEmDQILHGL--DKVAEEWAQG----TFKLNSNDEdihTANerRLKELIGATAGKLH---------TGRSR 113
Cdd:PRK14515  74 LNKGGAIAEAA-QEILDGKwhDHFIVDPIQGgagtSMNMNANEV---IAN--RALELLGMEKGDYHyispnshvnMAQST 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  114 NDQVVTDLRLwmrQTCSTLSGLLwELIRTMVD----RAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLE 189
Cdd:PRK14515 148 NDAFPTAIHI---ATLNALEGLL-QTMGYMHDvfelKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQ 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  190 VRKRINVLPLGSGAIaGNPLGVDRELLRAEL----NFGAITLNS----MDATSERDFVAEFLFWASLCMTHLSRMAEDLI 261
Cdd:PRK14515 224 SRQHLYEVNMGATAV-GTGLNADPEYIEAVVkhlaAISELPLVGaedlVDATQNTDAYTEVSAALKVCMMNMSKIANDLR 302

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 31541964  262 LYCTKE---FSFVQLSdAYSTGSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:PRK14515 303 LMASGPrvgLAEIMLP-ARQPGSSIMPGKVNPVMPEVINQIAFQVIG 348
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 107-360 2.19e-10

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


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 62.34  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  107 LHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:PRK09053 102 VHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQR 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  187 LLEVRKRINVLPLG--SGAIA---GNPLGVdRELLRAELNfgaITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLI 261
Cdd:PRK09053 182 LAALRPRALVLQFGgaAGTLAslgEQALPV-AQALAAELQ---LALPALPWHTQRDRIAEFASALGLLAGTLGKIARDVS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  262 LYCTKEFSFV-QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVfgrcAGLLMTL-KGLPSTYNKDL---QEDKEAVFEVS 336
Cdd:PRK09053 258 LLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRA----PGLVATLfAAMPQEHERALggwHAEWDTLPELA 333

                        250       260
                 ....*....|....*....|....
gi 31541964  337 DTMSAVLQVATGVISTLQIHQENM 360
Cdd:PRK09053 334 CLAAGALAQMAQIVEGLEVDAARM 357
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 110-290 2.39e-10

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 62.16  E-value: 2.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 110 GRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLE 189
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 190 VRKRINVLPLGSGAIaGNPLGVD---RELLRAELNfgAIT-------LNSMDATSERD-FVAeflFWASL--CMTHLSRM 256
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPpgyIELVVEKLS--EITglplkraENLIDATQNTDaFVE---VSGALkrLAVKLSKI 286

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31541964 257 AEDLILyctkefsfvqLSD------------AYSTGSSLMPQKKNP 290
Cdd:cd01357 287 ANDLRL----------LSSgpraglgeinlpAVQPGSSIMPGKVNP 322
aspA PRK12273
aspartate ammonia-lyase; Provisional
 112-290 2.00e-08

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 56.29  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  112 SRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVR 191
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  192 KRINVLPLGSGAIaGNPLGVD---RELLRAELNfgAIT-------LNSMDATSERD-FVAeflFWASL--CMTHLSRMAE 258
Cdd:PRK12273 222 ELLREVNLGATAI-GTGLNAPpgyIELVVEKLA--EITglplvpaEDLIEATQDTGaFVE---VSGALkrLAVKLSKICN 295

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 31541964  259 DLILyctkefsfvqLSD------------AYSTGSSLMPQKKNP 290
Cdd:PRK12273 296 DLRL----------LSSgpraglneinlpAVQAGSSIMPGKVNP 329
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 138-290 3.20e-06

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 49.34  E-value: 3.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 138 ELIRTMVDRAEAERDVLFPGYTHLQRAQPIR----WSHWilshAVALTRDSERLLEVRKRINVLPLGSGAIaGNPLGVDR 213
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTlgqeFSGY----AAQLARDIARIEAALERLRELNLGGTAV-GTGLNAPP 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964 214 ---ELLRAELNfgAITL-------NSMDATSERD-FVAeflFWASL--CMTHLSRMAEDLILyctkefsfvqLS------ 274
Cdd:cd01596 236 gyaEKVAAELA--ELTGlpfvtapNLFEATAAHDaLVE---VSGALktLAVSLSKIANDLRL----------LSsgprag 300

                       170       180
                ....*....|....*....|..
gi 31541964 275 ------DAYSTGSSLMPQKKNP 290
Cdd:cd01596 301 lgeinlPANQPGSSIMPGKVNP 322
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 280-389 4.05e-05

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 44.63  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541964  280 GSSLMPQKKNPDSLELIRSKAGRVFGRcagLLMTLKGLPSTYNKDLQEDKE---AVFEVSDTMSAVLQVATGVISTLQIH 356
Cdd:PRK08937  58 GSSAMPHKRNPIGSERITGLARVLRSY---LVTALENVPLWHERDLSHSSAeriALPDAFLALDYILNRFVNILENLVVF 134

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 31541964  357 QENMGQAL---SPDMLATDLAYYLVRKGMPFRQAHE 389
Cdd:PRK08937 135 PENIERNLdktLGFIATERVLLELVEKGMGREEAHE 170
 
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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