|
Name |
Accession |
Description |
Interval |
E-value |
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
14-468 |
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: 697.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 14 LWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDNKFIIKAGDED 93
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 94 IHTANERRLGEIIGKNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQP 173
Cdd:TIGR00838 81 IHMAIERELIDRVGEDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 174 IRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFWS 253
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 254 TLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDMQ 333
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 334 EDKEPLFDALTTVEHSILIATGVISTLLIDKQNM-EKALTMDMLATDLADYLVRKGVPFRETHHISGECVRKAEEEKLsG 412
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMeEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGK-G 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 336287733 413 IDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDALGGTAKSAVLKQLENLKSILS 468
Cdd:TIGR00838 400 LEELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG 455
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
11-467 |
0e+00 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 660.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 11 ENKLWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDNKFIIKAG 90
Cdd:COG0165 2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 91 DEDIHTANERRLGEIIGkNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQK 170
Cdd:COG0165 82 LEDIHMNIERRLIERIG-DVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 171 AQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESL 250
Cdd:COG0165 161 AQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 251 FWSTLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNK 330
Cdd:COG0165 241 SAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 331 DMQEDKEPLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMD-MLATDLADYLVRKGVPFRETHHISGECVRKAEEEK 409
Cdd:COG0165 321 DLQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 336287733 410 LSgIDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDALGGTAKSAVLKQLENLKSIL 467
Cdd:COG0165 401 KD-LEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARL 457
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
1-467 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 653.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 1 MSQQQDKQPSENKLWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEW 80
Cdd:PLN02646 5 MSASEEEAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 81 HDNKFIIKAGDEDIHTANERRLGEIIGKnISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDV 160
Cdd:PLN02646 85 EAGKFEWRPDREDVHMNNEARLTELIGE-PAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 161 LMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAV 240
Cdd:PLN02646 164 VVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 241 SDRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMS 320
Cdd:PLN02646 244 SDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 321 IKSIPSTYNKDMQEDKEPLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMDML-ATDLADYLVRKGVPFRETHHISG 399
Cdd:PLN02646 324 CKGLPTAYNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVG 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336287733 400 ECVRKAEEEKLSgIDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDALGGTAKSAVLKQLENLKSIL 467
Cdd:PLN02646 404 AAVALAESKGCE-LSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKL 470
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
33-467 |
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: 650.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 33 SLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDNKFIIKAGDEDIHTANERRLGEIIGKnISG 112
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGD-VGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 113 KVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYK 192
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 193 RLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSS 272
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 273 GEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDMQEDKEPLFDALTTVEHSILI 352
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 353 ATGVISTLLIDKQNMEKALTMD-MLATDLADYLVR-KGVPFRETHHISGECVRKAEEEKLSgIDQLSFEQFQQIDSRFEK 430
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGfSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKD-LSDLTLAELQAISPLFEE 398
|
410 420 430
....*....|....*....|....*....|....*..
gi 336287733 431 DVMETFDFEASVERRDALGGTAKSAVLKQLENLKSIL 467
Cdd:cd01359 399 DVREALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
10-468 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 643.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 10 SENKLWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDNKFIIKA 89
Cdd:PRK00855 2 MSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 90 GDEDIHTANERRLGEIIGkNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQ 169
Cdd:PRK00855 82 ELEDIHMAIEARLTERIG-DVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 170 KAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVES 249
Cdd:PRK00855 161 RAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 250 LFWSTLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYN 329
Cdd:PRK00855 241 LSAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 330 KDMQEDKEPLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMDM-LATDLADYLVRKGVPFRETHHISGECVRKAEEE 408
Cdd:PRK00855 321 RDLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEER 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 409 KLSgIDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDALGGTAKSAVLKQLENLKSILS 468
Cdd:PRK00855 401 GVD-LADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
14-464 |
1.94e-173 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 494.50 E-value: 1.94e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 14 LWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDN-KFIIKAGDE 92
Cdd:PRK04833 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANpQQILASDAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 93 DIHTANERRLGEIIGkNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQ 172
Cdd:PRK04833 83 DIHSWVEGKLIDKVG-DLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 173 PIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFW 252
Cdd:PRK04833 162 PVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 253 STLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDM 332
Cdd:PRK04833 242 ASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 333 QEDKEPLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMDML-ATDLADYLVRKGVPFRETHHISGECVRKAEEEKlS 411
Cdd:PRK04833 322 QEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYAnATELADYLVAKGVPFREAHHIVGEAVVEAIRQG-K 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 336287733 412 GIDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDALGGTAKSAVLKQLENLK 464
Cdd:PRK04833 401 PLEDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAK 453
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
14-468 |
4.64e-157 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 458.86 E-value: 4.64e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 14 LWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDN-KFIIKAGDE 92
Cdd:PRK12308 3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDpEQILLSDAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 93 DIHTANERRLGEIIGkNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQ 172
Cdd:PRK12308 83 DIHSWVEQQLIGKVG-DLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 173 PIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFW 252
Cdd:PRK12308 162 PVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 253 STLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDM 332
Cdd:PRK12308 242 ASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 333 QEDKEPLFDALTTVEHSILIATGVISTLLIDKQ-NMEKALTMDMLATDLADYLVRKGVPFRETHHISGECVRKAEEEKLS 411
Cdd:PRK12308 322 QEDKEGLFDALDTWNDCMEMAALCFDGIKVNGErTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 336287733 412 gIDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDALGGTAKSAVLKQLENLKSILS 468
Cdd:PRK12308 402 -LEELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLA 457
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
17-312 |
1.23e-135 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 392.89 E-value: 1.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 17 GRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDN-KFIIKAGDEDIH 95
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 96 TANERRLGEIIG------KNISGKVHTGRSRNDQVATDMRIFVRESLLN-LSKILHQFITAILERAHKEIDVLMPGYTHL 168
Cdd:pfam00206 81 TAVNMNLNEVIGellgqlVHPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 169 QKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREF---LAKGLGFDG----VIGNSLTAVS 241
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFaelVAKELGFFTglpvKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336287733 242 DRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEFGFIKLADAYST-GSSLMPQKKNPDSLELLRGKSGRVFG 312
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
41-363 |
6.19e-132 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 384.16 E-value: 6.19e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 41 YDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQEWHDNKFIIKAGDEDIHTANERRLGEIIGKNISGKVHTGRSR 120
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 121 NDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITR 200
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 201 VNQSPLGSGALAGHPYG--IDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEFGFI 278
Cdd:cd01334 161 LNVLPLGGGAVGTGANAppIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 279 KLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDMQEDKEPLFDALTTVEHSILIATGVIS 358
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....*
gi 336287733 359 TLLID 363
Cdd:cd01334 321 GLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
101-354 |
1.89e-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: 189.74 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 101 RLGEIIGKNI-SGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHW 179
Cdd:cd01594 23 RAGELAGGLHgSALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 180 LSSYATYFTEDYKRLQEIitrvnqsplgsgalaghpygidreflakglgfdgvignsltavsdrdFVVESLFWSTLFMNH 259
Cdd:cd01594 103 LRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALDALALAAAH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 260 ISRFSEDLIIYSSGEFGFIKLADA-YSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDMQEDKEP 338
Cdd:cd01594 136 LSKIAEDLRLLLSGEFGELGEPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSMREI 215
|
250
....*....|....*.
gi 336287733 339 LFDALTTVEHSILIAT 354
Cdd:cd01594 216 LADSLLLLIDALRLLL 231
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
99-417 |
1.22e-47 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 175.81 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 99 ERRLGEIIGKNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAH 178
Cdd:PRK02186 495 EAYLIERLGEDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGH 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 179 WLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFWSTLFMN 258
Cdd:PRK02186 575 YLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAIST 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 259 HISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDM-QEDKE 337
Cdd:PRK02186 655 VLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFSNSFEAgSPMNG 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 338 PLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMDML-ATDLADYLV-RKGVPFRETHHISGECVRKAEEEKLSGIDQ 415
Cdd:PRK02186 735 PIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLEDGGVsATAVAESLVvRRSISFRSAHTQVGQAIRQSLDQGRSSADA 814
|
..
gi 336287733 416 LS 417
Cdd:PRK02186 815 LA 816
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
60-464 |
2.61e-46 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 167.85 E-value: 2.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 60 LITTEELNLIHQGLEQIRQEWHDnKFIIKAGDEDIHTANERRLGEIIGKNISGKVHTGRSRNDQVATDMRIFVRESLLNL 139
Cdd:PRK06705 57 LMKKEEAKFILHALKKVEEIPEE-QLLYTEQHEDLFFLVEHLISQEAKSDFVSNMHIGRSRNDMGVTMYRMSLRRYVLRL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 140 SKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGID 219
Cdd:PRK06705 136 MEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTTSFPIK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 220 REFLAKGLGFDGVIGNSLTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDS 299
Cdd:PRK06705 216 RERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQKRNPVS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 300 LELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDMQEDKEP-LFDALTTVEHSILIATGVISTLLIDKQNME-KALTMDMLA 377
Cdd:PRK06705 296 IEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKrRSYKHAITI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 378 TDLADYLVRK-GVPFRETHHISGECVRKAEEEKlSGIDQLSFEQFQQ-IDSRF-----EKDVMETFDFEASVERRDALGG 450
Cdd:PRK06705 376 TDFADVLTKNyGIPFRHAHHAASVIANMSLEQK-KELHELCFKDVNIyLQEKFkiqllEKEWEEIISPEAFIQKRNVYGG 454
|
410
....*....|....
gi 336287733 451 TAKSAVLKQLENLK 464
Cdd:PRK06705 455 PSKKEMERMINNRK 468
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
13-407 |
5.86e-36 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 138.10 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 13 KLWGGrftGA-----TDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELNLIHQGLEQIRQewhdNKFII 87
Cdd:PRK06389 2 KIWSG---GAgeeleNDFYDNIVKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIYK----NGIEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 88 KAGDEDIHTANERRLGEIIGKNISgKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEidvLMPGYTH 167
Cdd:PRK06389 75 DLDLEDVHTAIENFVIRRCGDMFK-NFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIPGFNLKG---RLPGYTH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 168 LQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVV 247
Cdd:PRK06389 151 FRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 248 E--SLFWSTLFMNhISRFSEDLIIYSSGefGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIP 325
Cdd:PRK06389 231 EniSYLISSLAVD-LSRICQDIIIYYEN--GIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 326 STYNKDMQEDKEPLFDALTTVEHSILIATGVISTLLIDKQNmEKALTMDMLATDLADYLVRKGVPFRETHHISGECVRKA 405
Cdd:PRK06389 308 TGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITN-EKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIREG 386
|
..
gi 336287733 406 EE 407
Cdd:PRK06389 387 EV 388
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
375-442 |
5.32e-30 |
|
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: 111.36 E-value: 5.32e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336287733 375 MLATDLADYLVRKGVPFRETHHISGECVRKAEEEKLSgIDQLSFEQFQQIDSRFEKDVMETFDFEASV 442
Cdd:pfam14698 2 STATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKD-LEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
51-397 |
3.81e-25 |
|
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: 106.43 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 51 YTQGLNKLGLITTEELNLIHQGLEQIRQEW-----------HDNKFIIKAgdedihtanerrLGEIIGKNISGKVHTGRS 119
Cdd:cd01595 21 LAEAQAELGLIPKEAAEEIRAAADVFEIDAeriaeieketgHDVIAFVYA------------LAEKCGEDAGEYVHFGAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 120 RNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIIT 199
Cdd:cd01595 89 SQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 200 R--VNQS--PLGSGALAGhPYGID-REFLAKGLGFDGVigNSLTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSSGE 274
Cdd:cd01595 169 RvlVGGIsgAVGTHASLG-PKGPEvEERVAEKLGLKVP--PITTQIEPRDRIAELLSALALIAGTLEKIATDIRLLQRTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 275 FGFIKL-ADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSipstynkDMQED-------KEPLFDALTTV 346
Cdd:cd01595 246 IGEVEEpFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQ-------WHERDlsdssveRNILPDAFLLL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 336287733 347 EHSILIATGVISTLLIDKQNMEKALTMD---MLATDLADYLVRKGVPFRETHHI 397
Cdd:cd01595 319 DAALSRLQGLLEGLVVNPERMRRNLDLTwglILSEAVMMALAKKGLGRQEAYEL 372
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
51-411 |
1.83e-24 |
|
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: 105.17 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 51 YTQGLNKLGLITTEELnlihqglEQIRQEWHDNKFIIKAGDEDIHTAN------ERRLGEIIGKNISGKVHTGRSRNDQV 124
Cdd:COG0015 31 LAEAQAELGLIPAEAA-------AAIRAAADDFEIDAERIKEIEKETRhdvkafVYALKEKVGAEAGEYIHFGATSQDIN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 125 ATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVnqs 204
Cdd:COG0015 104 DTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERV--- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 205 PLG--SGA---LAGHPYG---IDREFLAK-GLGFDGVIgnslTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEF 275
Cdd:COG0015 181 LVGkiGGAvgtYAAHGEAwpeVEERVAEKlGLKPNPVT----TQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 276 GFIK-LADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSipstynkDMQED-------KEPLFDALTTVE 347
Cdd:COG0015 257 GEVEePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALAS-------WHERDlsdssveRNILPDAFLLLD 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336287733 348 HSILIATGVISTLLIDKQNMEKALTM---DMLATDLADYLVRKGVPFRETHHISGECVRKAEEEKLS 411
Cdd:COG0015 330 GALERLLKLLEGLVVNPERMRANLDLtggLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGND 396
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
149-409 |
1.10e-15 |
|
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: 78.82 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 149 AILERAHKeiDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLG--SGALAG-HPYGID-REFLA 224
Cdd:cd01597 130 ARLAATHR--DTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGgaAGTLASlGDQGLAvQEALA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 225 KGLGFDgvignsLTAVS---DRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEFGfiKLADAYSTG---SSLMPQKKNPD 298
Cdd:cd01597 208 AELGLG------VPAIPwhtARDRIAELASFLALLTGTLGKIARDVYLLMQTEIG--EVAEPFAKGrggSSTMPHKRNPV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 299 SLELLRGKSGRVFGQLSGFLMSiksipstynkdMQEDKE-----------PLFDALTTVEHSILIATGVISTLLIDKQNM 367
Cdd:cd01597 280 GCELIVALARRVPGLAALLLDA-----------MVQEHErdagawhaewiALPEIFLLASGALEQAEFLLSGLEVNEDRM 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 336287733 368 EKALTMD---------MLAtdLADYLVRKgvpfrETHHISGECVRKAEEEK 409
Cdd:cd01597 349 RANLDLTgglilseavMMA--LAPKLGRQ-----EAHDLVYEACMRAVEEG 392
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
114-297 |
2.69e-12 |
|
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: 68.32 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 114 VHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKR 193
Cdd:cd01357 130 VNMSQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRAR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 194 LQEIITRVNQSPLGSGA----LAGHPYGIDR--EFLAKGLGFDGVI-GNSLTAVSDRDFVVEslFWSTL--FMNHISRFS 264
Cdd:cd01357 210 IYKARERLREVNLGGTAigtgINAPPGYIELvvEKLSEITGLPLKRaENLIDATQNTDAFVE--VSGALkrLAVKLSKIA 287
|
170 180 190
....*....|....*....|....*....|....*.
gi 336287733 265 EDLIIYSSGE---FGFIKLAdAYSTGSSLMPQKKNP 297
Cdd:cd01357 288 NDLRLLSSGPragLGEINLP-AVQPGSSIMPGKVNP 322
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
57-297 |
2.92e-12 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 68.47 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 57 KLGLITTEELNLIHQGLEQIRQEWHDNKFIIK-----AGDEDIHTANE---RRLGEIIGK--------NISGKVHTGRSR 120
Cdd:PRK13353 62 DLGLLPRRIAEAIVQACDEILAGKLHDQFIVDpiqggAGTSTNMNANEviaNRALELLGGekgdyhyvSPNDHVNMAQST 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 121 NDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITR 200
Cdd:PRK13353 142 NDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 201 VNQSPLGSGALaGHPYGIDREFLAKGLG-FDGVIGNSLT-------AVSDRDFVVE-SLFWSTLFMNhISRFSEDLIIYS 271
Cdd:PRK13353 222 LYEVNLGGTAV-GTGLNADPEYIERVVKhLAAITGLPLVgaedlvdATQNTDAFVEvSGALKVCAVN-LSKIANDLRLLS 299
|
250 260
....*....|....*....|....*....
gi 336287733 272 SGE---FGFIKLAdAYSTGSSLMPQKKNP 297
Cdd:PRK13353 300 SGPrtgLGEINLP-AVQPGSSIMPGKVNP 327
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
57-297 |
4.72e-09 |
|
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: 58.20 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 57 KLGLITTEELNLIHQGLEQIRQEWHDNKFIIK-----AGdedihT-----ANE---RRLGEIIGKNISGK--------VH 115
Cdd:cd01596 57 ELGLLDEEKADAIVQACDEVIAGKLDDQFPLDvwqtgSG-----TstnmnVNEviaNRALELLGGKKGKYpvhpnddvNN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 116 TGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQ 195
Cdd:cd01596 132 SQSSNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 196 EIITRVNQSPLGSGA----LAGHPYGIDR--EFLAK--GLGFDGViGNSLTAVSDRDFVVE---SLfwSTLFMNhISRFS 264
Cdd:cd01596 212 AALERLRELNLGGTAvgtgLNAPPGYAEKvaAELAEltGLPFVTA-PNLFEATAAHDALVEvsgAL--KTLAVS-LSKIA 287
|
250 260 270
....*....|....*....|....*....|....*.
gi 336287733 265 EDLIIYSSGE---FGFIKLaDAYSTGSSLMPQKKNP 297
Cdd:cd01596 288 NDLRLLSSGPragLGEINL-PANQPGSSIMPGKVNP 322
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
74-312 |
6.99e-09 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 57.70 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 74 EQIRQEWHDNkFIIK-----AGDEDIHTANE---RRLGEIIGK------NISGKVHT--GRSRNDQVATDMRIFVRESLL 137
Cdd:PRK14515 86 EILDGKWHDH-FIVDpiqggAGTSMNMNANEviaNRALELLGMekgdyhYISPNSHVnmAQSTNDAFPTAIHIATLNALE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 138 NLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGA----LAG 213
Cdd:PRK14515 165 GLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAvgtgLNA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 214 HPYGIDR--EFLAKGLGFDGVIGNSLT-AVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSSG-EFGFIKLA-DAYSTGS 288
Cdd:PRK14515 245 DPEYIEAvvKHLAAISELPLVGAEDLVdATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGpRVGLAEIMlPARQPGS 324
|
250 260
....*....|....*....|....
gi 336287733 289 SLMPQKKNPDSLELLRGKSGRVFG 312
Cdd:PRK14515 325 SIMPGKVNPVMPEVINQIAFQVIG 348
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
97-304 |
6.13e-08 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 54.70 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 97 ANE---RRLGEIIGKNISGK--------VHTGRSRNDQVATDMRI-FVRESLLNLSKILHQFITAILERAHKEIDVLMPG 164
Cdd:PLN00134 98 ANEviaNRAAEILGGPVGEKspvhpndhVNRSQSSNDTFPTAMHIaAATEIHSRLIPALKELHESLRAKSFEFKDIVKIG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 165 YTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGA----LAGHPyGIDREFLAK-----GLGFDGViGN 235
Cdd:PLN00134 178 RTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAvgtgLNTKK-GFDEKIAAAvaeetGLPFVTA-PN 255
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336287733 236 SLTAVSDRD-FVVESLFWSTLFMNhISRFSEDLIIYSSGE---FGFIKLAdAYSTGSSLMPQKKNPDSLELLR 304
Cdd:PLN00134 256 KFEALAAHDaFVELSGALNTVAVS-LMKIANDIRLLGSGPrcgLGELNLP-ENEPGSSIMPGKVNPTQCEALT 326
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
119-297 |
8.65e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 54.36 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 119 SRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEII 198
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 199 TRVNQSPLGSGA----LAGHPYGIDR--EFLAKGLGFDGVI-GNSLTAVSDRD-FVVESlfwSTL--FMNHISRFSEDLI 268
Cdd:PRK12273 222 ELLREVNLGATAigtgLNAPPGYIELvvEKLAEITGLPLVPaEDLIEATQDTGaFVEVS---GALkrLAVKLSKICNDLR 298
|
170 180 190
....*....|....*....|....*....|..
gi 336287733 269 IYSSGE---FGFIKLAdAYSTGSSLMPQKKNP 297
Cdd:PRK12273 299 LLSSGPragLNEINLP-AVQAGSSIMPGKVNP 329
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
114-396 |
1.17e-07 |
|
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: 53.71 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 114 VHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKR 193
Cdd:cd01360 85 IHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLER 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 194 LQEIITRVNQS----PLGSGALAGhPYgiDREFLAKGLGFdGVIGNSlTAVSDRDfvveslfwstlfmNHISRFSEDLII 269
Cdd:cd01360 165 LKEARERILVGkisgAVGTYANLG-PE--VEERVAEKLGL-KPEPIS-TQVIQRD-------------RHAEYLSTLALI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 270 YSSGEfgfiKLA------------------DAYSTGSSLMPQKKNPDSLELLRGksgrvfgqLSGFLMSIkSIPSTYN-- 329
Cdd:cd01360 227 ASTLE----KIAteirhlqrtevleveepfSKGQKGSSAMPHKRNPILSENICG--------LARVIRSN-VIPALENva 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 330 ----KDMQE---DKEPLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMD---------MLAtdladyLVRKGVPfRE 393
Cdd:cd01360 294 lwheRDISHssvERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTkglifsqrvLLA------LVEKGMS-RE 366
|
...
gi 336287733 394 THH 396
Cdd:cd01360 367 EAY 369
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-303 |
1.87e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 52.75 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 100 RRLGEIIGKNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAI--LERAHKEIDvLMpGYTHLQKAQPIRWA 177
Cdd:PRK05975 88 RQLRAAVGEEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLdaLEATFGQNA-LM-GHTRMQAAIPITVA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 178 HWLSSYATYFTEDYKRLQEIITRVNQSPLGSGA-----LAGHPYGIdREFLAKGLGfdgvIGNSLTAVSDRDFVVESLFW 252
Cdd:PRK05975 166 DRLASWRAPLLRHRDRLEALRADVFPLQFGGAAgtlekLGGKAAAV-RARLAKRLG----LEDAPQWHSQRDFIADFAHL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 336287733 253 STLFMNHISRFSEDLIIYSSGEfGFIKLADaySTGSSLMPQKKNPDSLELL 303
Cdd:PRK05975 241 LSLVTGSLGKFGQDIALMAQAG-DEISLSG--GGGSSAMPHKQNPVAAETL 288
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
57-297 |
1.11e-06 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 50.96 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 57 KLGLITTEELNLIHQGLEQIRQEWHDNKFIIkagdeDI-------HT---ANE---RRLGEIIGKNISGK--------VH 115
Cdd:cd01362 57 ELGLLDEEKADAIVQAADEVIAGKLDDHFPL-----VVwqtgsgtQTnmnVNEviaNRAIELLGGVLGSKkpvhpndhVN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 116 TGRSRNDQVATDMRIFVRESLLN-LSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRL 194
Cdd:cd01362 132 MSQSSNDTFPTAMHIAAALALQErLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 195 QEIITRVNQSPLGSGA----LAGHPyGIDREFLAK-----GLGFDgVIGNSLTAVSDRDFVVE----------SLFwstl 255
Cdd:cd01362 212 EAALPRLYELALGGTAvgtgLNAHP-GFAEKVAAElaeltGLPFV-TAPNKFEALAAHDALVEasgalktlavSLM---- 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 336287733 256 fmnHISRfseDLIIYSSGE---FGFIKLaDAYSTGSSLMPQKKNP 297
Cdd:cd01362 286 ---KIAN---DIRWLGSGPrcgLGELSL-PENEPGSSIMPGKVNP 323
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
126-327 |
1.20e-05 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 47.31 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 126 TDMrIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPI----RWAHWLSSyatyFTEDYKRLQEIITRV 201
Cdd:cd03302 103 TDL-IQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTtvgkRACLWIQD----LLMDLRNLERLRDDL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 202 N----QSPLGSGA-----LAGHPYGIDR--EFLAKGLGFDGVIgNSLTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIY 270
Cdd:cd03302 178 RfrgvKGTTGTQAsfldlFEGDHDKVEAldELVTKKAGFKKVY-PVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 271 SS---GEFGFIKladaYSTGSSLMPQKKNPDSLEllrgksgRVFGqLSGFLMSIKSIPST 327
Cdd:cd03302 257 ANlkeVEEPFEK----GQIGSSAMPYKRNPMRSE-------RCCS-LARHLMNLASNAAQ 304
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
56-312 |
1.75e-05 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 47.22 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 56 NKLGLITTEELNLIHQGLEQIRQEWHDNKFII-----KAGDEDIHTANE---RRLGEIIGKNISGK--------VHTGRS 119
Cdd:PRK12425 58 DRNGDLPADIARLIEQAADEVLDGQHDDQFPLvvwqtGSGTQSNMNVNEviaGRANELAGNGRGGKspvhpndhVNRSQS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 120 RNDQVATDMRIF----VRESLLnlsKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQ 195
Cdd:PRK12425 138 SNDCFPTAMHIAaaqaVHEQLL---PAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 196 EIITRVNQ-----SPLGSGALAGHPYG--IDREFLA-KGLGFDGViGNSLTAVSDRD-FVVESLFWSTLFMNhISRFSED 266
Cdd:PRK12425 215 AALPAVCElaqggTAVGTGLNAPHGFAeaIAAELAAlSGLPFVTA-PNKFAALAGHEpLVSLSGALKTLAVA-LMKIAND 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 336287733 267 LIIYSSGE---FGFIKLAdAYSTGSSLMPQKKNPDSLELLRGKSGRVFG 312
Cdd:PRK12425 293 LRLLGSGPragLAEVRLP-ANEPGSSIMPGKVNPTQCEALSMLACQVMG 340
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
57-297 |
2.89e-04 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 43.16 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 57 KLGLITTEELNLIHQGLEQIRQEWHDNKFIIkagdeDI-HT---------ANE---RRLGEIIGKNISGK--VH------ 115
Cdd:PRK00485 61 ELGLLDAEKADAIVAAADEVIAGKHDDHFPL-----DVwQTgsgtqsnmnVNEviaNRASELLGGELGSKkpVHpndhvn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 116 TGRSRNDQVATDMRI----FVRESLLnlsKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDY 191
Cdd:PRK00485 136 MSQSSNDTFPTAMHIaavlAIVERLL---PALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 192 KRLQEIITRVNQSPLGSGA----LAGHPyGIDREFLAK-----GLGFDGViGNSLTAVSDRDFVVE----------SLFw 252
Cdd:PRK00485 213 ERIEAALPHLYELALGGTAvgtgLNAHP-GFAERVAEElaeltGLPFVTA-PNKFEALAAHDALVEasgalktlavSLM- 289
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 336287733 253 stlfmnhisRFSEDLIIYSSGE---FGFIKLADAySTGSSLMPQKKNP 297
Cdd:PRK00485 290 ---------KIANDIRWLASGPrcgLGEISLPEN-EPGSSIMPGKVNP 327
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
260-440 |
8.35e-04 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 40.78 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 260 ISRFSEDLIIYSSGEFGFIKLADAYS-TGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSI-----KSIPSTYNKDMQ 333
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGqKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVplwheRDLSHSSAERIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 334 edkepLFDALTTVEHSILIATGVISTLLIDKQNMEKALTMD---MLATDLADYLVRKGVPFRETHHISGECVRKAEEEKL 410
Cdd:PRK08937 110 -----LPDAFLALDYILNRFVNILENLVVFPENIERNLDKTlgfIATERVLLELVEKGMGREEAHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|.
gi 336287733 411 SGIDQLSF-EQFQQIDSRFEKDVMetFDFEA 440
Cdd:PRK08937 185 DLRELLEAdERFTKQLTKEELDEL--FDPEA 213
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
147-390 |
2.62e-03 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 40.11 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 147 ITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATyftedykRLQEIITRVNQSPLgSGALAG-----------HP 215
Cdd:PLN02848 154 IKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAY-------RLSRQRKQLSEVKI-KGKFAGavgnynahmsaYP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 216 yGIDREFLAK------GLGFDGVIgnslTAVSDRDFVVEslfwstLFmNHISRFSEDLIIYSSGEFGFIKLA------DA 283
Cdd:PLN02848 226 -EVDWPAVAEefvtslGLTFNPYV----TQIEPHDYMAE------LF-NAVSRFNNILIDFDRDIWSYISLGyfkqitKA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336287733 284 YSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGflMSIKSIPSTYNKDMQeDKEPLFDALTTVEHSILIATGV---ISTL 360
Cdd:PLN02848 294 GEVGSSTMPHKVNPIDFENSEGNLGLANAELSH--LSMKLPISRMQRDLT-DSTVLRNMGVGLGHSLLAYKSTlrgIGKL 370
|
250 260 270
....*....|....*....|....*....|..
gi 336287733 361 LIDKQNMEKAL--TMDMLATDLADYLVRKGVP 390
Cdd:PLN02848 371 QVNEARLAEDLdqTWEVLAEPIQTVMRRYGVP 402
|
|
| |
