|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
4-427 |
0e+00 |
|
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: 649.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 4 RYTRPEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKLRRNARFDIRRIHELEKITRHDVVAFTRAVSESLGE 83
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 84 ERRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQR 163
Cdd:cd01360 81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 164 NRARFVAAAEEMRVGKLSGAVGTFAHIPPEVERITCEKLGLKPAPISTQVLARDRHAHYLSVLALIGATLEQLAVEVRHL 243
Cdd:cd01360 161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 244 QRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVILPDATTLVHYA 323
Cdd:cd01360 241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 324 LHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKGLSREAAYDLVQPaamqawdeerpfyeivrqhpaitkyl 403
Cdd:cd01360 321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQR-------------------------- 374
|
410 420
....*....|....*....|....
gi 2556435733 404 speeiaeafnpEYHLRHVDEIFRR 427
Cdd:cd01360 375 -----------EYYLKHVDEIFKR 387
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
1-428 |
0e+00 |
|
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: 623.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 1 MI-ARYTRPEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKLRRNAR---FDIRRIHELEKITRHDVVAFTRA 76
Cdd:COG0015 1 LIsPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADdfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 77 VSESLG-EERRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLA 155
Cdd:COG0015 81 LKEKVGaEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 156 LFYDMMQRNRARFVAAAEEMRVGKLSGAVGTFAHIP---PEVERITCEKLGLKPAPISTQVLARDRHAHYLSVLALIGAT 232
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 233 LEQLAVEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVI 312
Cdd:COG0015 241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 313 LPDATTLVHYALHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKGLSREAAYDLVQPAAMQAWDEERPFYEI 392
Cdd:COG0015 321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 2556435733 393 VRQHPAITKYLSPEEIAEAFNPEYHLRHVDEIFRRV 428
Cdd:COG0015 401 LAADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
1-428 |
0e+00 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 537.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 1 MIARYTRPEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKLRRNARF---DIRRIHELEKITRHDVVAFTRAV 77
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFtevDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 78 SESLGEERRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALF 157
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 158 YDMMQRNRARFVAAAEEMRVGKLSGAVGTFAHIPP---EVERITCEKLGLKPAPISTQVLARDRHAHYLSVLALIGATLE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 235 QLAVEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVILP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 315 DATTLVHYALHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKGLSREAAYDLVQPAAMQAWD-EERPFYEIV 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEvDEPDLLEFL 400
|
410 420 430
....*....|....*....|....*....|....*
gi 2556435733 394 RQHPAITKYLSPEEIAEAFNPEYHLRHVDEIFRRV 428
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
10-376 |
1.91e-180 |
|
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: 507.81 E-value: 1.91e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 10 MAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKLRRNA---RFDIRRIHELEKITRHDVVAFTRAVSESLGEE-R 85
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAAdvfEIDAERIAEIEKETGHDVIAFVYALAEKCGEDaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 86 RWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNR 165
Cdd:cd01595 81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 166 ARFVAAAEEMRVGKLSGAVGTFAHI---PPEVERITCEKLGLKPAPISTQVLARDRHAHYLSVLALIGATLEQLAVEVRH 242
Cdd:cd01595 161 ERLEEARERVLVGGISGAVGTHASLgpkGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 243 LQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVILPDATTLVHY 322
Cdd:cd01595 241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2556435733 323 ALHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKGLSREAAYDLVQ 376
Cdd:cd01595 321 ALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVK 374
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
5-428 |
4.34e-120 |
|
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: 356.55 E-value: 4.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 5 YTRPEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKLRRNA---RFDIRRIHELEKITRHDVVAFTRAVSESL 81
Cdd:cd01597 6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAAdveRLDLEALAEATARTGHPAIPLVKQLTAAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 82 GEE-RRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDM 160
Cdd:cd01597 86 GDAaGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 161 MQRNRARFVAAAEEMRVGKLSGAVGTFAHIP---PEVERITCEKLGLKPAPISTQVlARDRHAHYLSVLALIGATLEQLA 237
Cdd:cd01597 166 LLRHRERLDELRPRVLVVQFGGAAGTLASLGdqgLAVQEALAAELGLGVPAIPWHT-ARDRIAELASFLALLTGTLGKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 238 VEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVILPDAT 317
Cdd:cd01597 245 RDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 318 TLVHYALHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKgLSREAAYDLVQPAAMQAWDEERPFYEIVRQHP 397
Cdd:cd01597 325 LLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRAVEEGRPLREVLLEDP 403
|
410 420 430
....*....|....*....|....*....|.
gi 2556435733 398 AITKYLSPEEIAEAFNPEYHLRHVDEIFRRV 428
Cdd:cd01597 404 EVAAYLSDEELDALLDPANYLGSAPALVDRV 434
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
20-337 |
7.07e-120 |
|
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: 351.80 E-value: 7.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 20 YQSWLEVELAACEAWAEIGVIPKEDAEKLRRNARFDIRRIH----ELEKITRHDVVAFTRAVSESLGEE-RRWIHYGLTS 94
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAadqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 95 SDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEE 174
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 175 MRVGKL-SGAVGTFAHIPPEVERITCEKLGL-KPAPISTQVLA-RDRHAHYLSVLALIGATLEQLAVEVRHLQRSEVREV 251
Cdd:cd01334 161 LNVLPLgGGAVGTGANAPPIDRERVAELLGFfGPAPNSTQAVSdRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 252 EEAFGKgQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVILPDATTLVHYALHRYAGVI 331
Cdd:cd01334 241 ELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319
|
....*.
gi 2556435733 332 DTLKVY 337
Cdd:cd01334 320 EGLEVN 325
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
225-418 |
2.46e-79 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 244.55 E-value: 2.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 225 VLALIGATLEQLAVEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDIS 304
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 305 HSSVERVILPDATTLVHYALHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKGLSREAAYDLVQPAAMQAWD 384
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWK 181
|
170 180 190
....*....|....*....|....*....|....
gi 2556435733 385 EERPFYEIVRQHPAITKYLSPEEIAEAFNPEYHL 418
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
4-286 |
4.50e-72 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 229.18 E-value: 4.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 4 RYT--RPEMAQLWSEEAQYQSWLEVEL-----AACEAWAEIGVIPKEDAEKLRRNAR-----FDIRRIHELEKITRHDVV 71
Cdd:pfam00206 2 RFTvpADALMGIFTDRSRFNFRLGEEDikglaALKKAAAKANVILKEEAAAIIKALDevaeeGKLDDQFPLKVWQEGSGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 72 AFTRAVSESLGE-------ERRWIHYGLTSSDVVDTAWSYRLKKA-SELILEALDHFLEVLARRAHEHKYTLMIGRTHGV 143
Cdd:pfam00206 82 AVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 144 HAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLSG--AVGTFAHIPPEVERITCEKLG------LKPAPISTQVLA 215
Cdd:pfam00206 162 DATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATSD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2556435733 216 RDRHAHYLSVLALIGATLEQLAVEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRG 286
Cdd:pfam00206 242 RDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
1-382 |
1.13e-62 |
|
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: 208.71 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 1 MIARYTRPEMAQLWSEEAQYQSWLEVELAACEAWAEIGV-IPKEDAEKLRRNAR-FDIRRIHELEKITRHDVVAFTRAVS 78
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLdISDEQIEEMKANVEnIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 79 ESLGEERRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALF- 157
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWi 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 158 YDMMQRNRaRFVAAAEEMRVGKLSGAVGTFA----------HIPPEVERITCEKLGLKPA-PISTQVLARDRHAHYLSVL 226
Cdd:cd03302 161 QDLLMDLR-NLERLRDDLRFRGVKGTTGTQAsfldlfegdhDKVEALDELVTKKAGFKKVyPVTGQTYSRKVDIDVLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 227 ALIGATLEQLAVEVRHLQRSEvrEVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVAL-WHERDISH 305
Cdd:cd03302 240 SSLGATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTqWFERTLDD 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2556435733 306 SSVERVILPDATTLVHYALHRYAGVIDTLKVYPQRMRRNM--ELTFGLynSQRLLLMLIDKGLSREAAYDLVQPAAMQA 382
Cdd:cd03302 318 SANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIrqELPFMA--TENIIMAAVKAGGDRQDAHERIRVLSHQA 394
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
5-418 |
8.57e-62 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 206.79 E-value: 8.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 5 YTRPEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKLR---RNARFDIRRIHELEKITRHD----VVAFTRAV 77
Cdd:PRK09053 12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEaacDAERLDLDALAQAAALAGNLaiplVKQLTAQV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 78 SESLGEERRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALF 157
Cdd:PRK09053 92 AARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 158 YDMMQRNRARFVAAAEEMRVGKLSGAVGTFA----HIPPEVERITCE-KLGLKPAPISTQvlaRDRHAHYLSVLALIGAT 232
Cdd:PRK09053 172 LDALLRHRQRLAALRPRALVLQFGGAAGTLAslgeQALPVAQALAAElQLALPALPWHTQ---RDRIAEFASALGLLAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 233 LEQLAVEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVI 312
Cdd:PRK09053 249 LGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWHAEWDT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 313 LPDATTLVHYALHRYAGVIDTLKVYPQRMRRNMELTFGLYNSQRLLLMLIDKgLSREAAYDLVQPAAMQAWDEERPFYEI 392
Cdd:PRK09053 329 LPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADR-IGRLDAHHLVEQASKRAVAEGRHLRDV 407
|
410 420
....*....|....*....|....*.
gi 2556435733 393 VRQHPAITKYLSPEEIAEAFNPEYHL 418
Cdd:PRK09053 408 LAEDPQVSAHLSPAALDRLLDPAHYL 433
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
72-326 |
2.35e-53 |
|
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: 177.80 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 72 AFTRAVSESLGEERR--WIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTT 149
Cdd:cd01594 19 VLAGRAGELAGGLHGsaLVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 150 FGLKLALFYDMMQRNRARFVAAaeemrvgklsgavgtfahippeveritceklglkpapistqvlardRHAHYLSVLALI 229
Cdd:cd01594 99 LGYELRAWAQVLGRDLERLEEA----------------------------------------------AVAEALDALALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 230 GATLEQLAVEVRHLQRSEVREVEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVE 309
Cdd:cd01594 133 AAHLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSM 212
|
250
....*....|....*..
gi 2556435733 310 RVILPDATTLVHYALHR 326
Cdd:cd01594 213 REILADSLLLLIDALRL 229
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
8-334 |
7.93e-49 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
Pssm-ID: 274128 [Multi-domain] Cd Length: 338 Bit Score: 169.54 E-value: 7.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 8 PEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEKL---RRNARFDIRrihELEKITRHD---VVAFTRAVSESL 81
Cdd:TIGR02426 9 PAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAAIeaaCAAAAPDLE---ALAHAAATAgnpVIPLVKALRKAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 82 GEE-RRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDM 160
Cdd:TIGR02426 86 AGEaARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 161 MQRNRARFVAAAEEMRVGKLSGAVGTFAHIPP---EVERITCEKLGLkPAPISTQVLARDRHAHYLSVLALIGATLEQLA 237
Cdd:TIGR02426 166 VLRARDRLAALRTRALPLQFGGAAGTLAALGTrggAVAAALAARLGL-PLPALPWHTQRDRIAEFGSALALVAGALGKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 238 VEVRHLQRSEVrevEEAFGKGQKGSSAMPHKRNPIASENITGVARLLRGYMISAYENVALWHERDISHSSVERVILPDAT 317
Cdd:TIGR02426 245 GDIALLSQTEV---GEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPELV 321
|
330
....*....|....*..
gi 2556435733 318 TLVHYALHRYAGVIDTL 334
Cdd:TIGR02426 322 RLTGGALRQAQVLAEGL 338
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
23-346 |
4.38e-38 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 142.76 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 23 WLEvELAACEAWAEIGVIPKEDAEKLRRNAR-F---DIRRIHELEKITRHDVVA---FTR---AVSESLGEERRWIHYGL 92
Cdd:cd01598 21 WLI-ALSNLEEIPEVPPLTKEELKFLRAIIEnFseeDALRIKEIEATTNHDVKAveyFLKekfETLGLLKKIKEFIHFAC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 93 TSSDVVDTAWSYRLKKA-SELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFvaa 171
Cdd:cd01598 100 TSEDINNLAYALMIKEArNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQL--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 172 AEEMRVGKLSGAVGTF-AHIP--PEVERITCEK-----LGLKPAPISTQVLARDRHAHYLSVLALIGATLEQLAVEV--- 240
Cdd:cd01598 177 KQIEILGKFNGAVGNFnAHLVayPDVDWRKFSEffvtsLGLTWNPYTTQIEPHDYIAELFDALARINTILIDLCRDIwgy 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 241 ---RHLQrsevreveEAFGKGQKGSSAMPHKRNPIASENITG---VARLLRGYMiSAYENVALWhERDISHSSVERVI-L 313
Cdd:cd01598 257 islGYFK--------QKVKKGEVGSSTMPHKVNPIDFENAEGnlgLSNALLNHL-SAKLPISRL-QRDLTDSTVLRNIgV 326
|
330 340 350
....*....|....*....|....*....|...
gi 2556435733 314 PDATTLVhyALHRYAGVIDTLKVYPQRMRRNME 346
Cdd:cd01598 327 AFGHSLI--AYKSLLRGLDKLELNEARLLEDLD 357
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
25-346 |
3.42e-36 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 137.96 E-value: 3.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 25 EVE----LAACEAWAEIGVIPKEDAEKLRR-NARF---DIRRIHELEKITRHDVVA---FTRAVSESLGEERR---WIHY 90
Cdd:PRK09285 40 EVEwliaLAAHPGIPEVPPFSAEANAFLRAiVENFseeDAARIKEIERTTNHDVKAveyFLKEKLAGLPELEAvseFIHF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 91 GLTSSDVVDTAWSYRLKKA-SELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARfV 169
Cdd:PRK09285 120 ACTSEDINNLSHALMLKEArEEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQ-L 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 170 AAAEEMrvGKLSGAVGTF-AHIP--PEVERIT-----CEKLGLKPAPISTQVLARDRHAHYLSVLALIGATLEQLAVEV- 240
Cdd:PRK09285 199 EAVEIL--GKINGAVGNYnAHLAayPEVDWHAfsrefVESLGLTWNPYTTQIEPHDYIAELFDAVARFNTILIDLDRDVw 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 241 -----RHL-QRSEVREVeeafgkgqkGSSAMPHKRNPIASENITG---VAR-LLRgyMISAYENVALWhERDISHSSVER 310
Cdd:PRK09285 277 gyislGYFkQKTKAGEI---------GSSTMPHKVNPIDFENSEGnlgLANaLLE--HLAAKLPISRW-QRDLTDSTVLR 344
|
330 340 350
....*....|....*....|....*....|....*..
gi 2556435733 311 VI-LPDATTLVhyALHRYAGVIDTLKVYPQRMRRNME 346
Cdd:PRK09285 345 NLgVAFGYSLI--AYDSLLKGLGKLEVNEARLAEDLD 379
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
350-429 |
3.06e-32 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 117.17 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 350 GLYNSQRLLLMLIDKGLSREAAYDLVQPAAMQAWDEERPFYEIVRQHPAITKYLSPEEIAEAFNPEYHLRHVDEIFRRVG 429
Cdd:smart00998 2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
8-314 |
6.38e-27 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 110.53 E-value: 6.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 8 PEMAQLWSEEAQYQSWLEVELAACEAWAEIGVIPKEDAEK-LRRNARFDIRrIHELEKITRHD---VVAFTRAVSESLGE 83
Cdd:PRK05975 18 DEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERiAAACETFEPD-LAALRHATARDgvvVPALVRQLRAAVGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 84 E-RRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQ 162
Cdd:PRK05975 97 EaAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 163 RNRARFVAAAEEMRVGKLSGAVGTFAHIPPEVERIT---CEKLGLKPAPI--STqvlaRDRHAHYLSVLALIGATLEQLA 237
Cdd:PRK05975 177 RHRDRLEALRADVFPLQFGGAAGTLEKLGGKAAAVRarlAKRLGLEDAPQwhSQ----RDFIADFAHLLSLVTGSLGKFG 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2556435733 238 VEVRHLQRSEvREVEEAfgkGQKGSSAMPHKRNPIASENITGVARlLRGYMISAYENvALWHERDISHS--SVERVILP 314
Cdd:PRK05975 253 QDIALMAQAG-DEISLS---GGGGSSAMPHKQNPVAAETLVTLAR-FNATQVSGLHQ-ALVHEQERSGAawTLEWMILP 325
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
350-428 |
1.22e-24 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 96.33 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 350 GLYNSQRLLLMLIdKGLSREAAYDLVQPAAMQAWDEE-RPFYEIVRQHPAITkYLSPEEIAEAFNPEYHLRHVDEIFRRV 428
Cdd:pfam10397 1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEEGkNDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADEIVDRV 78
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
24-415 |
1.84e-24 |
|
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: 104.55 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 24 LEVELAACEAWAEIGVIPKEDAEKLRRNARfDIRRIHELEKITRH----DVV-AFTRAVSESLGEERRWIHYGLTSSDVV 98
Cdd:cd01359 13 IAGSIAHAVMLAEQGILTEEEAAKILAGLA-KIRAEIEAGAFELDpedeDIHmAIERRLIERIGDVGGKLHTGRSRNDQV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 99 DTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVG 178
Cdd:cd01359 92 ATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 179 KL-SGAVG--TFAhIPPEverITCEKLGLKPAPIST--QVLARDRHAHYLSVLALIGATLEQLAVEVrHLQRSEVR---E 250
Cdd:cd01359 172 PLgAGALAgtTFP-IDRE---RTAELLGFDGPTENSldAVSDRDFVLEFLSAAALLMVHLSRLAEDL-ILWSTQEFgfvE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 251 VEEAFGkgqKGSSAMPHKRNPIASENITG----VARLLRGyMISAYENVALWHERDISHSSVErviLPDATTLVHYALHR 326
Cdd:cd01359 247 LPDAYS---TGSSIMPQKKNPDVLELIRGkagrVIGALAG-LLTTLKGLPLAYNKDLQEDKEP---LFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 327 YAGVIDTLKVYPQRMRRnmELTFGLYNSQRLLLML-IDKGLS-REA---AYDLVQPAAMQAWD-EERPFYEIVRQHPAIT 400
Cdd:cd01359 320 LTGVISTLTVNPERMRE--AAEAGFSTATDLADYLvREKGVPfREAhhiVGRAVRLAEEKGKDlSDLTLAELQAISPLFE 397
|
410
....*....|....*
gi 2556435733 401 kylspEEIAEAFNPE 415
Cdd:cd01359 398 -----EDVREALDPE 407
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
35-415 |
4.38e-23 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 101.00 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 35 AEIGVIPKEDAEKLR----------RNARFDIRriHELEKItrHDVVAftRAVSESLGEERRWIHYGLTSSDVVDTAWSY 104
Cdd:PRK00855 48 AKQGILSEEEAEKILagldeileeiEAGKFEFS--PELEDI--HMAIE--ARLTERIGDVGGKLHTGRSRNDQVATDLRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 105 RLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKL-SGA 183
Cdd:PRK00855 122 YLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLgSAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 184 -VGTFAHIPPEverITCEKLGL-KPAPISTQ-VLARDRHAHYLSVLALIGATLEQLAVEVRHLQRSEVREVE--EAFgkg 258
Cdd:PRK00855 202 lAGTTFPIDRE---RTAELLGFdGVTENSLDaVSDRDFALEFLSAASLLMVHLSRLAEELILWSSQEFGFVElpDAF--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 259 QKGSSAMPHKRNPIASENITGVARLLRGYMIS----------AY------ENVALWHerdishsSVERVILpdattlvhy 322
Cdd:PRK00855 276 STGSSIMPQKKNPDVAELIRGKTGRVYGNLTGlltvmkglplAYnrdlqeDKEPLFD-------AVDTLKL--------- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 323 ALHRYAGVIDTLKVYPQRMRRNMELtfGLYNSQRLLLMLIDKGLS-REA---AYDLVQPAAMQAWD-EERPFYEIVRQHP 397
Cdd:PRK00855 340 SLEAMAGMLETLTVNKERMREAAGK--GFSTATDLADYLVRKGVPfREAheiVGKAVREAEERGVDlADLSLEELQAFSP 417
|
410
....*....|....*...
gi 2556435733 398 AITkylspEEIAEAFNPE 415
Cdd:PRK00855 418 LIT-----EDVYEVLTPE 430
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
55-310 |
1.20e-21 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 96.73 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 55 DIRRIHELEKITRHDVVA---FTRAVSES---LGEERRWIHYGLTSSDVVDTAWSYRLKKA-SELILEALDHFLEVLARR 127
Cdd:PLN02848 81 DALEVKKIERVTNHDVKAveyFLKQKCKShpeLAKVLEFFHFACTSEDINNLSHALMLKEGvNSVVLPTMDEIIKAISSL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 128 AHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFvaaAEEMRVGKLSGAVGTF-AHIP-------PEVERITC 199
Cdd:PLN02848 161 AHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQL---SEVKIKGKFAGAVGNYnAHMSaypevdwPAVAEEFV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 200 EKLGLKPAPISTQVLARDRHAHYLSVLALIGATLEQLAVEV-RHLQRSEVREVEEAfgkGQKGSSAMPHKRNPIASENIT 278
Cdd:PLN02848 238 TSLGLTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIwSYISLGYFKQITKA---GEVGSSTMPHKVNPIDFENSE 314
|
250 260 270
....*....|....*....|....*....|....
gi 2556435733 279 GVARLLRGYM--ISAYENVALWhERDISHSSVER 310
Cdd:PLN02848 315 GNLGLANAELshLSMKLPISRM-QRDLTDSTVLR 347
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
67-348 |
1.74e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 66.41 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 67 RHDVVAFTRAVSESLGEERR-WIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHA 145
Cdd:PRK02186 488 RGLYMLYEAYLIERLGEDVGgVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 146 EPTTFGLKLALFYDMMQRNRARFVAAAEEMRV---GKLSGAvGTFAHIPPEVeriTCEKLGL-KPAPISTQVLA-RDRHA 220
Cdd:PRK02186 568 LPGSLGHYLLAVDGALARETHALFALFEHIDVcplGAGAGG-GTTFPIDPEF---VARLLGFeQPAPNSLDAVAsRDGVL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 221 HYLSVLALIGATLEQLAVEvrhLQRSEVREV------EEAFGkgqkGSSAMPHKRNPIASENITGVARLLRGYMISAyeN 294
Cdd:PRK02186 644 HFLSAMAAISTVLSRLAQD---LQLWTTREFalvslpDALTG----GSSMLPQKKNPFLLEFVKGRAGVVAGALASA--S 714
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2556435733 295 VALWH---ERDISHSSVERVILPDATTLVHYALHRYAGVIDTLKVYPQRMRRNMELT 348
Cdd:PRK02186 715 AALGKtpfSNSFEAGSPMNGPIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLEDG 771
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
13-392 |
1.35e-10 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 63.26 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 13 LWSEEAQyqswlEVELAACEAWAEIgvipKEDAEKLRRNARFDIRRIHELEKItrhdvvaftravsESLGEERRWIHYGL 92
Cdd:PRK12308 50 LSEEEQQ-----KLELALNELKLEV----MEDPEQILLSDAEDIHSWVEQQLI-------------GKVGDLGKKLHTGR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 93 TSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAA 172
Cdd:PRK12308 108 SRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 173 EEMRVGKL-SGAVGTFAHiPPEVERITcEKLGLKPAPIST--QVLARDRHAHYLSVLALIGATLEQLAVEVRHLQRSEVR 249
Cdd:PRK12308 188 TRLDTCPLgSGALAGTAY-PIDREALA-HNLGFRRATRNSldSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSGESG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 250 EVEEAfGKGQKGSSAMPHKRNPIASENITG----VARLLRGYMISAyENVALWHERDISHssvERVILPDATTLVHYALH 325
Cdd:PRK12308 266 FIELA-DTVTSGSSLMPQKKNPDALELIRGktgrVYGALAGMMMTV-KALPLAYNKDMQE---DKEGLFDALDTWNDCME 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2556435733 326 RYAGVIDTLKVYPQRMRRNMELtfGLYNSQRLLLMLIDKGLSREAAYDLVQPAAMQAWDEERPFYEI 392
Cdd:PRK12308 341 MAALCFDGIKVNGERTLEAAKQ--GYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCALEEL 405
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-275 |
2.26e-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: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 106 LKKASELIlEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLSG-AV 184
Cdd:cd01357 149 ILLLRKLL-DALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGtAI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 185 GTFAHIPPE--------VERITceKLGLKPAP--I-STQVLarDRHAHYLSVLALIGATLEQLAVEVRhLQRS------- 246
Cdd:cd01357 228 GTGINAPPGyielvvekLSEIT--GLPLKRAEnlIdATQNT--DAFVEVSGALKRLAVKLSKIANDLR-LLSSgpraglg 302
|
170 180 190
....*....|....*....|....*....|.
gi 2556435733 247 EVR--EVeeafgkgQKGSSAMPHKRNPIASE 275
Cdd:cd01357 303 EINlpAV-------QPGSSIMPGKVNPVIPE 326
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
67-375 |
4.51e-10 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 61.28 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 67 RHDV-VAFTRAVSESLGEERRWIHYGLTSSDVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHA 145
Cdd:PLN02646 95 REDVhMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 146 EPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLsGAvGTFAHIPPEVER-ITCEKLGL-KPAPISTQ-VLARDRHAHY 222
Cdd:PLN02646 175 QPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPL-GS-CALAGTGLPIDRfMTAKDLGFtAPMRNSIDaVSDRDFVLEF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 223 LSVLALIGATLEQLAVEVrhlqrseVREVEEAFGKGQ------KGSSAMPHKRNPIASE-----------NITGVARLLR 285
Cdd:PLN02646 253 LFANSITAIHLSRLGEEW-------VLWASEEFGFVTpsdavsTGSSIMPQKKNPDPMElvrgksarvigDLVTVLALCK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 286 GyMISAYenvalwhERDISHssvERVILPDATTLVHYALHRYAGVIDTLKVYPQRMRRNmeLTFGLYNSQRLLLMLIDKG 365
Cdd:PLN02646 326 G-LPTAY-------NRDLQE---DKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKS--LPAGMLDATTLADYLVRKG 392
|
330
....*....|
gi 2556435733 366 LSREAAYDLV 375
Cdd:PLN02646 393 VPFRETHHIV 402
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
96-281 |
1.03e-09 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 60.00 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 96 DVVDTAWSYRLKKASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEM 175
Cdd:PRK13353 143 DVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 176 RVGKLSG-AVGTFAHIPPEVERITCEKL----GLKPAPISTQVLARDRHAHYLSVLALI---GATLEQLAVEVRhLQRSE 247
Cdd:PRK13353 223 YEVNLGGtAVGTGLNADPEYIERVVKHLaaitGLPLVGAEDLVDATQNTDAFVEVSGALkvcAVNLSKIANDLR-LLSSG 301
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2556435733 248 VREveeafGKG-------QKGSSAMPHKRNPIASENITGVA 281
Cdd:PRK13353 302 PRT-----GLGeinlpavQPGSSIMPGKVNPVMPEVVNQIA 337
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
110-281 |
7.21e-09 |
|
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: 57.51 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 110 SELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLSG-AVGTFA 188
Cdd:cd01362 153 QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGtAVGTGL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 189 HIPPEVERITCEKL----GL--KPAPISTQVLA-RDRHAHYLSVLALIGATLEQLAVEVRHLQ---RSEVREVEeaFGKG 258
Cdd:cd01362 233 NAHPGFAEKVAAELaeltGLpfVTAPNKFEALAaHDALVEASGALKTLAVSLMKIANDIRWLGsgpRCGLGELS--LPEN 310
|
170 180
....*....|....*....|...
gi 2556435733 259 QKGSSAMPHKRNPIASENITGVA 281
Cdd:cd01362 311 EPGSSIMPGKVNPTQCEALTMVA 333
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
70-281 |
1.95e-08 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 56.25 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 70 VVAfTRAvSESLGEER---RWIH------YGLTSSDVVDTA--------WSYRLkkaseliLEALDHFLEVLARRAHEHK 132
Cdd:PRK00485 109 VIA-NRA-SELLGGELgskKPVHpndhvnMSQSSNDTFPTAmhiaavlaIVERL-------LPALEHLRDTLAAKAEEFA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 133 YTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLSG-AVGTFAHIPPEVERITCEKL----GL--K 205
Cdd:PRK00485 180 DIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGtAVGTGLNAHPGFAERVAEELaeltGLpfV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 206 PAPISTQVLA-RDR--HAHylSVLALIGATLEQLAVEVRHLQ---RSEVREVEeaFGKGQKGSSAMPHKRNPIASENITG 279
Cdd:PRK00485 260 TAPNKFEALAaHDAlvEAS--GALKTLAVSLMKIANDIRWLAsgpRCGLGEIS--LPENEPGSSIMPGKVNPTQCEALTM 335
|
..
gi 2556435733 280 VA 281
Cdd:PRK00485 336 VC 337
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
88-276 |
3.01e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 52.68 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 88 IHYGLTSSDVVDTAWSYRLKKaseLILEALDHFL---EVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRN 164
Cdd:PRK06705 110 MHIGRSRNDMGVTMYRMSLRR---YVLRLMEHHLllqESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 165 RARFVAAAEEMRVGKLSGAVGTFAHIPPEVERITcEKLGLkpapisTQVLARDRHA-----HYLSVLALIGATLEQLAVE 239
Cdd:PRK06705 187 LERMKKTYKLLNQSPMGAAALSTTSFPIKRERVA-DLLGF------TNVIENSYDAvagadYLLEVSSLLMVMMTNTSRW 259
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2556435733 240 VRH---LQRSEVREVEEAFGKGQKgSSAMPHKRNPIASEN 276
Cdd:PRK06705 260 IHDfllLATKEYDGITVARPYVQI-SSIMPQKRNPVSIEH 298
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
106-208 |
6.00e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 48.20 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 106 LKKASELIlEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLSG-AV 184
Cdd:PRK12273 156 LLSLRKLL-DALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGAtAI 234
|
90 100 110
....*....|....*....|....*....|
gi 2556435733 185 GTFAHIPPEVERITCEKL------GLKPAP 208
Cdd:PRK12273 235 GTGLNAPPGYIELVVEKLaeitglPLVPAE 264
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
93-281 |
7.80e-06 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 47.99 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 93 TSSDVVDTAWSYRLKKA-SELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALF---YDMMQRN-RAR 167
Cdd:PRK12425 137 SSNDCFPTAMHIAAAQAvHEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFvaqLDYAERAiRAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 168 FVAAAEEMRVGKlsgAVGTFAHIPPEV-ERITCEKLGLKPAPISTQVLARDRHAHYLSVLALIGA------TLEQLAVEV 240
Cdd:PRK12425 217 LPAVCELAQGGT---AVGTGLNAPHGFaEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGAlktlavALMKIANDL 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2556435733 241 RHL---QRSEVREVEeaFGKGQKGSSAMPHKRNPIASENITGVA 281
Cdd:PRK12425 294 RLLgsgPRAGLAEVR--LPANEPGSSIMPGKVNPTQCEALSMLA 335
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
108-280 |
1.37e-03 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 40.83 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 108 KASELILEALDHFLEVLARRAHEHKYTLMIGRTHGVHAEPTTFGLKLALFYDMMQRNRARFVAAAEEMRVGKLSG-AVGT 186
Cdd:PLN00134 147 EIHSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGtAVGT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556435733 187 -------FAH-IPPEVERITceKLGLKPAPISTQVLA-RDRHAHYLSVLALIGATLEQLAVEVRHLQ---RSEVREVeeA 254
Cdd:PLN00134 227 glntkkgFDEkIAAAVAEET--GLPFVTAPNKFEALAaHDAFVELSGALNTVAVSLMKIANDIRLLGsgpRCGLGEL--N 302
|
170 180
....*....|....*....|....*.
gi 2556435733 255 FGKGQKGSSAMPHKRNPIASENITGV 280
Cdd:PLN00134 303 LPENEPGSSIMPGKVNPTQCEALTMV 328
|
|
| |
