|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
12-447 |
0e+00 |
|
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: 803.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 12 LSTRYASKEMQFLFSDQNKFSTWRRLWVWLAKAESRLGLEISDAQIAEMELQISNIDFEAAAAEERLTRHDVMAHVHVFA 91
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 92 KQCPSAAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWI 171
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 172 QDLIMDERALSRCLEDLRFRGVKGTTGTQASFLQLFNGDGEKVKQLDQLVTELAGFKKAYAVTGQTYSRKVDVEIVAALA 251
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 252 SLGTTIHKMCSDLRILASRKELEEPFESTQIGSSAMPYKRNPMRSERCCALARHLITLFSSAANTHATQWLERTLDDSAN 331
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 332 RRLTLSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGDRQVCHEKIRVLSQEAGAQVKQ 411
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 201065703 412 HGKDNDLVVRVRKDPYFSPILEQLDTILDAKTFTGR 447
Cdd:cd03302 401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
21-400 |
5.81e-154 |
|
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: 442.71 E-value: 5.81e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 21 MQFLFSDQNKFSTWRRLWVWLAKAESRLGLeISDAQIAEME--LQISNIDFEAAAAEERLTRHDVMAHVHVFAKQCP-SA 97
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRaaADVFEIDAERIAEIEKETGHDVIAFVYALAEKCGeDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 98 APVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMD 177
Cdd:cd01595 80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 178 ERALSRCLEDLRFRGVKGTTGTQASFlqlfngdGEKVKQLDQLVTELAGFkKAYAVTGQTYSRKVDVEIVAALASLGTTI 257
Cdd:cd01595 160 LERLEEARERVLVGGISGAVGTHASL-------GPKGPEVEERVAEKLGL-KVPPITTQIEPRDRIAELLSALALIAGTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 258 HKMCSDLRILAS--RKELEEPFESTQIGSSAMPYKRNPMRSERCCALARHLITLFSSAANThATQWLERTLDDSANRRLT 335
Cdd:cd01595 232 EKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALEN-LVQWHERDLSDSSVERNI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 201065703 336 LSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGDRQVCHEKIRV 400
Cdd:cd01595 311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
12-455 |
3.29e-149 |
|
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: 432.59 E-value: 3.29e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 12 LSTRYASKEMQFLFSDQNKFSTWRRLWVWLAKAESRLGLeISDAQIAEMELQISN--IDFEAAAAEERLTRHDVMAHVHV 89
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 90 FAKQCPS-AAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRAC 168
Cdd:COG0015 81 LKEKVGAeAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 169 LWIQDLIMDERALSRCLEDLRFRGVKGTTGTQASFlqlfngdGEKVKQLDQLVTELAGFkKAYAVTGQTYSRKVDVEIVA 248
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAH-------GEAWPEVEERVAEKLGL-KPNPVTTQIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 249 ALASLGTTIHKMCSDLRILASR--KELEEPFESTQIGSSAMPYKRNPMRSERCCALARHLITLFSSAANThATQWLERTL 326
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRTevGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEA-LASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 327 DDSANRRLTLSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGDRQVCHEKIRVLSQEAG 406
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 201065703 407 AQvkqhgkDNDLVVRVRKDPYFSPIL--EQLDTILDAKTFTGRASDQVGEF 455
Cdd:COG0015 392 EE------GNDLRELLAADPEIPAELskEELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
12-455 |
2.20e-129 |
|
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: 382.08 E-value: 2.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 12 LSTRYASKEMQFLFSDQNKFSTWRRLWVWLAKAESRLGLeISDAQIAEME--LQISNIDFEAAAAEERLTRHDVMAHVHV 89
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGV-IPAEAVKEIRekANFTEVDLERIKEIEAVTRHDVKAVVYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 90 FAKQCPSAAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACL 169
Cdd:TIGR00928 80 LKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 170 WIQDLIMDERALSRCLEDLRFRGVKGTTGTQASFlqlfngdGEKVKQLDQLVTELAGFKKAYAVTgQTYSRKVDVEIVAA 249
Cdd:TIGR00928 160 WAEEMLRQLERLLQAKERIKVGGISGAVGTHAAA-------YPLVEEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 250 LASLGTTIHKMCSDLRILASR--KELEEPFESTQIGSSAMPYKRNPMRSERCCALARHLITLFSSAANThATQWLERTLD 327
Cdd:TIGR00928 232 LALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALEN-APLWHERDLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 328 DSANRRLTLSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGDRQVCHEKIRVLSQEAga 407
Cdd:TIGR00928 311 DSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGA-- 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 201065703 408 qvkQHGKDNDLVVRVRKDPYFSPILEQLD--TILDAKTFTGRASDQVGEF 455
Cdd:TIGR00928 389 ---AEVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
31-360 |
1.77e-86 |
|
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: 268.22 E-value: 1.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 31 FSTWRRLWVWLAKAESRLGLeISDAQIAEMELQISNIDFEAAAAE---ERLTRHDVMAHVHVFAKQC-PSAAPVIHLGAT 106
Cdd:cd01334 1 IRADLQVEKAHAKALAELGL-LPKEAAEAILAALDEILEGIAADQveqEGSGTHDVMAVEEVLAERAgELNGGYVHTGRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 107 SCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLE 186
Cdd:cd01334 80 SNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 187 DLRFRGVKGTT-GTQASFlqlfngdgekVKQLDQLVTELAGFKKAYAVTGQ-TYSRKVDVEIVAALASLGTTIHKMCSDL 264
Cdd:cd01334 160 RLNVLPLGGGAvGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 265 RILASR--KELEEPFEStQIGSSAMPYKRNPMRSERCCALARHLITLFSSAANTHATQWlERTLDDSANRRLTLSEAFLA 342
Cdd:cd01334 230 RLLSSGefGEVELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGP-LEDNVDSPVEREALPDSFDL 307
|
330
....*....|....*...
gi 201065703 343 ADAALLTLLNISQGLVVY 360
Cdd:cd01334 308 LDAALRLLTGVLEGLEVN 325
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
15-399 |
1.88e-62 |
|
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: 208.18 E-value: 1.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 15 RYASKEMQFLFSDQNKFSTWRRLWVWLAKAESRLGlEISDAQIAEMElQISNIDFEAAAAEERLTRHDVMAHVHVFAKQC 94
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLG-VIPAEAAEEIR-KKAKFDVERVKEIEAETKHDVIAFVTAIAEYC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 95 PSAAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDL 174
Cdd:cd01360 79 GEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 175 IMDERALSRCLEDLRFRGVKGTTGTQASFlqlfngdGEKVkqlDQLVTELAGFKKAYAVTgQTYSRKVDVEIVAALASLG 254
Cdd:cd01360 159 KRHLERLKEARERILVGKISGAVGTYANL-------GPEV---EERVAEKLGLKPEPIST-QVIQRDRHAEYLSTLALIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 255 TTIHKMCSDLRILaSR---KELEEPFESTQIGSSAMPYKRNPMRSERCCALARhLITLFSSAANTHATQWLERTLDDSAN 331
Cdd:cd01360 228 STLEKIATEIRHL-QRtevLEVEEPFSKGQKGSSAMPHKRNPILSENICGLAR-VIRSNVIPALENVALWHERDISHSSV 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 201065703 332 RRLTLSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGDRQVCHEKIR 399
Cdd:cd01360 306 ERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQ 373
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-446 |
2.66e-58 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 191.78 E-value: 2.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 249 ALASLGTTIHKMCSDLRILASRK--ELEEPFESTQIGSSAMPYKRNPMRSERCCALARHLITLFSSAANTHaTQWLERTL 326
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PLWHERDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 327 DDSANRRLTLSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGDRQVCHEKIRVLSQEAG 406
Cdd:PRK08937 101 SHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAW 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 201065703 407 AQVkqhgkdNDLVVRVRKDPYFSPIL--EQLDTILDAKTFTG 446
Cdd:PRK08937 181 KNQ------KDLRELLEADERFTKQLtkEELDELFDPEAFVG 216
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
16-458 |
2.18e-48 |
|
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: 172.04 E-value: 2.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 16 YASKEMQFLFSDQNKFSTWRRLWVWLAKAESRLGLEISDA--QIAEmELQISNIDFEAAAAEERLTRHDVMAHVHVFAKQ 93
Cdd:cd01597 6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAaaEIAA-AADVERLDLEALAEATARTGHPAIPLVKQLTAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 94 CP-SAAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQ 172
Cdd:cd01597 85 CGdAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 173 DLImdeRALSRcLEDLRFRGV----KGTTGTQASFlqlfngdGEKVKQLDQLVTELAGFKKAyAVTGQTySRKVDVEIVA 248
Cdd:cd01597 165 ELL---RHRER-LDELRPRVLvvqfGGAAGTLASL-------GDQGLAVQEALAAELGLGVP-AIPWHT-ARDRIAELAS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 249 ALASLGTTIHKMCSDLRILASRK--ELEEPFESTQIGSSAMPYKRNPMRSERCCALAR----HLITLFSSAANTHatqwl 322
Cdd:cd01597 232 FLALLTGTLGKIARDVYLLMQTEigEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARrvpgLAALLLDAMVQEH----- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 323 ERtldDSANRRL---TLSEAFLAADAALLTLLNISQGLVVYPKVIERHISQELPFMSTENIIMAMVKAGGdRQVCHEKIR 399
Cdd:cd01597 307 ER---DAGAWHAewiALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLG-RQEAHDLVY 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 201065703 400 VLSQEAGAQVKqhgkdnDLVVRVRKDP----YFSPilEQLDTILDAKTFTGRASDQVGEFVKE 458
Cdd:cd01597 383 EACMRAVEEGR------PLREVLLEDPevaaYLSD--EELDALLDPANYLGSAPALVDRVLAR 437
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
67-338 |
2.28e-38 |
|
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: 139.67 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 67 IDFEAAAAEerltrhdvMAHVHVFAKQCPSAA------PVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQF 140
Cdd:cd01594 5 LLVELAAAL--------ALVEEVLAGRAGELAgglhgsALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 141 AQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLimdERALSRcLEDLRFrgvkgttgtqasflqlfngdgekvkqldql 220
Cdd:cd01594 77 AEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVL---GRDLER-LEEAAV------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 221 vtelagfkkayavtgqtysrkvdVEIVAALASLGTTIHKMCSDLRILAS--RKELEEPFESTQIGSSAMPYKRNPMRSER 298
Cdd:cd01594 123 -----------------------AEALDALALAAAHLSKIAEDLRLLLSgeFGELGEPFLPGQPGSSIMPQKVNPVAAEL 179
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 201065703 299 CCALARHLITLFSSAANThATQWLERTLDDSANRRLTLSE 338
Cdd:cd01594 180 VRGLAGLVIGNLVAVLTA-LKGGPERDNEDSPSMREILAD 218
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
12-321 |
6.68e-31 |
|
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: 122.16 E-value: 6.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 12 LSTRYASK-EMQFLFSDQNKFSTWRRLWVWLAKAESRLGLEISDAQIAeMELQISNIDFEAAAAEERlTRHD---VMAHV 87
Cdd:TIGR02426 1 LLDGLFGDpAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAA-IEAACAAAAPDLEALAHA-AATAgnpVIPLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 88 HVFAKQCPS-AAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKR 166
Cdd:TIGR02426 79 KALRKAVAGeAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 167 ACLWIQDLimdERALSRcLEDLRFRGVK----GTTGTQASFlqlfNGDGEKVKQldqlvtELAGFKKAYAVTGQTYS-RK 241
Cdd:TIGR02426 159 AAGWLAAV---LRARDR-LAALRTRALPlqfgGAAGTLAAL----GTRGGAVAA------ALAARLGLPLPALPWHTqRD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 242 VDVEIVAALASLGTTIHKMCSDLrILASRKELEEPFESTQIGSSAMPYKRNPMRSERCCALAR---HLI-TLFSSAANTH 317
Cdd:TIGR02426 225 RIAEFGSALALVAGALGKIAGDI-ALLSQTEVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARrvpGLAaTLHAALPQEH 303
|
....*..
gi 201065703 318 ---ATQW 321
Cdd:TIGR02426 304 ersLGGW 310
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
101-297 |
1.49e-19 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 88.97 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 101 IHLGATScyvGD--NTDL-IVLRDALK-LLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLim 176
Cdd:pfam00206 105 VHTGQSS---NDqvPTALrLALKDALSeVLLPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVAL-- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 177 dERALSRcLEDLRFRGVKGTTGTQASFLQLFNGDGEKVKQLDQLVTELAGFK-KAYAVTGQTYSRKVDVEIVAALASLGT 255
Cdd:pfam00206 180 -TRDRER-LQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFFTGLPvKAPNSFEATSDRDAVVELSGALALLAT 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 201065703 256 TIHKMCSDLRILASRK--ELEEPFESTQIGSSAMPYKRNPMRSE 297
Cdd:pfam00206 258 SLSKFAEDLRLLSSGPagLVELSLAEGEPGSSIMPGKVNPDQLE 301
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
373-455 |
1.53e-19 |
|
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: 82.46 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 373 PFMSTENIIMAMVKaGGDRQVCHEKIRVLSQEAGAQVKqhgkdNDLVVRVRKDPYFS-PILEQLDTILDAKTFTGRASDQ 451
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 201065703 452 VGEF 455
Cdd:pfam10397 75 VDRV 78
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
41-293 |
3.16e-16 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 80.83 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 41 LAKAESRLGLeISDAQIAEMEL--QISNIDF----EAAAAEERLTRHDVMAHVHVFAKQCPSAAPVIHLGATSCYVGDNT 114
Cdd:PRK09053 37 LARAEAACGV-IPAAAVAPIEAacDAERLDLdalaQAAALAGNLAIPLVKQLTAQVAARDAEAARYVHWGATSQDIIDTG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 115 DLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVK 194
Cdd:PRK09053 116 LVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 195 GTTGTQASFlqlfngdGEKVKQLDQ-LVTELagfkkAYAVTGQTYSRKVD--VEIVAALASLGTTIHKMCSDLRILASRK 271
Cdd:PRK09053 196 GAAGTLASL-------GEQALPVAQaLAAEL-----QLALPALPWHTQRDriAEFASALGLLAGTLGKIARDVSLLMQTE 263
|
250 260
....*....|....*....|....
gi 201065703 272 --ELEEPFESTQIGSSAMPYKRNP 293
Cdd:PRK09053 264 vgEVFEPAAAGKGGSSTMPHKRNP 287
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
51-329 |
6.41e-16 |
|
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: 79.59 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 51 EISDAQIAEMELQISNIDFEAA---AAEERLTRHDVMAhVHVFAK----QCPSAAPV---IHLGATSCYVGDNTDLIVLR 120
Cdd:cd01598 36 PLTKEELKFLRAIIENFSEEDAlriKEIEATTNHDVKA-VEYFLKekfeTLGLLKKIkefIHFACTSEDINNLAYALMIK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 121 DAL-KLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLimdERALSRcLEDLRFRG-VKGTTG 198
Cdd:cd01598 115 EARnEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRL---ERQYKQ-LKQIEILGkFNGAVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 199 TQASFLQLF-NGDGEKVKQldQLVTELAGFKKAYavTGQTYSRKVDVEIVAALASLGTTIHKMCSDLRILASRKELEEPF 277
Cdd:cd01598 191 NFNAHLVAYpDVDWRKFSE--FFVTSLGLTWNPY--TTQIEPHDYIAELFDALARINTILIDLCRDIWGYISLGYFKQKV 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 201065703 278 ESTQIGSSAMPYKRNPMR---SERCCALARHLITLFSsaaNTHATQWLERTLDDS 329
Cdd:cd01598 267 KKGEVGSSTMPHKVNPIDfenAEGNLGLSNALLNHLS---AKLPISRLQRDLTDS 318
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
372-456 |
1.27e-15 |
|
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: 71.71 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 372 LPFMSTENIIMAMVKAGGDRQVCHEKIRVLSQEAGAQVKqhgkdnDLVVRVRKDPYFSPIL--EQLDTILDAKTFTGRAS 449
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLseEELEELFDPEYYLGHAD 74
|
....*..
gi 201065703 450 DQVGEFV 456
Cdd:smart00998 75 AIVDRVL 81
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
12-304 |
1.08e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 75.09 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 12 LSTRYASKEMQFLFSDQNKFSTWRRLWVWLAKAESRLGleISDAQIAEMELQISNiDFEAAAAEER--LTRHDVMahVHV 89
Cdd:PRK05975 11 LSGLFGDDEIAALFSAEADIAAMLAFEAALAEAEAEHG--IIPAEAAERIAAACE-TFEPDLAALRhaTARDGVV--VPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 90 FAKQC-----PSAAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVG 164
Cdd:PRK05975 86 LVRQLraavgEEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 165 KRACLWIQDLiMDER----ALSRCLEDLRFRGVKGTtgtqasfLQLFNGDGEKVKqlDQLVTELagfkkAYAVTGQTYS- 239
Cdd:PRK05975 166 DRLASWRAPL-LRHRdrleALRADVFPLQFGGAAGT-------LEKLGGKAAAVR--ARLAKRL-----GLEDAPQWHSq 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 201065703 240 RKVDVEIVAALASLGTTIHKMCSDLRILAsrkELEEPFE-STQIGSSAMPYKRNPMRSERCCALAR 304
Cdd:PRK05975 231 RDFIADFAHLLSLVTGSLGKFGQDIALMA---QAGDEISlSGGGGSSAMPHKQNPVAAETLVTLAR 293
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
10-306 |
1.82e-12 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 69.01 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 10 SPLSTRYASK--EMQFLFSDQ--NKFstwrRLWV---WLAKAESRLGL----EISDAQIAEMELQISNIDfEAAAAE--- 75
Cdd:PRK09285 10 SPLDGRYASKtaALRPIFSEFglIRY----RVQVeveWLIALAAHPGIpevpPFSAEANAFLRAIVENFS-EEDAARike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 76 -ERLTRHDVMAhVHVFAK-------QCPSAAPVIHLGATScyvGDNTDL---IVLRDALK-LLLPRVASVIARLSQFAQS 143
Cdd:PRK09285 85 iERTTNHDVKA-VEYFLKeklaglpELEAVSEFIHFACTS---EDINNLshaLMLKEAREeVLLPALRELIDALKELAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 144 YKDQPTLGFTHLQPAQLTTVGK-------RAclwiqdlimdERALSRcLEDLRFRG-VKGTTGTqasflqlFNG------ 209
Cdd:PRK09285 161 YADVPMLSRTHGQPATPTTLGKemanvayRL----------ERQLKQ-LEAVEILGkINGAVGN-------YNAhlaayp 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 210 --DGEKVKQldQLVTELagfkkayAVTGQTYSRKVD-----VEIVAALASLGTTIHKMCSD------LRILASR-KELEe 275
Cdd:PRK09285 223 evDWHAFSR--EFVESL-------GLTWNPYTTQIEphdyiAELFDAVARFNTILIDLDRDvwgyisLGYFKQKtKAGE- 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 201065703 276 pfestqIGSSAMPYKRNPMRSERC-------CALARHL 306
Cdd:PRK09285 293 ------IGSSTMPHKVNPIDFENSegnlglaNALLEHL 324
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
114-293 |
1.92e-12 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 69.02 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 114 TDL-IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQdliMDERALSRcLEDLRFRg 192
Cdd:PRK00855 117 TDLrLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAE---MLARDLER-LRDARKR- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 193 VK----------GTTgtqasflqlFNgdgekvkqLD-QLVTELAGFKKA-----YAVTgqtySRKVDVEIVAALASLGTT 256
Cdd:PRK00855 192 VNrsplgsaalaGTT---------FP--------IDrERTAELLGFDGVtenslDAVS----DRDFALEFLSAASLLMVH 250
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 201065703 257 IHKMCSDLRILASRK----ELEEPFeSTqiGSSAMPYKRNP 293
Cdd:PRK00855 251 LSRLAEELILWSSQEfgfvELPDAF-ST--GSSIMPQKKNP 288
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
114-293 |
4.84e-10 |
|
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: 61.41 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 114 TDL-IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLimdERALSRcLEDLRFR- 191
Cdd:cd01359 93 TDLrLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEML---ERDLER-LADAYKRv 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 192 -----GVKGTTGTqaSFLqlfngdgekvkqLD-QLVTELAGFKKAY-----AVTgqtySRKVDVEIVAALASLGTTIHKM 260
Cdd:cd01359 169 nvsplGAGALAGT--TFP------------IDrERTAELLGFDGPTensldAVS----DRDFVLEFLSAAALLMVHLSRL 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 201065703 261 CSDLRILASRK----ELEEPFeSTqiGSSAMPYKRNP 293
Cdd:cd01359 231 AEDLILWSTQEfgfvELPDAY-ST--GSSIMPQKKNP 264
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
114-293 |
8.46e-10 |
|
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: 60.88 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 114 TDL-IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQdliMDERALSRcLEDLRFR- 191
Cdd:COG0165 116 TDFrLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAE---MLLRDRER-LADAYKRl 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 192 -----GVKGTTGTqaSFlqlfngdgekvkQLD-QLVTELAGFKKAY-----AVTgqtySRKVDVEIVAALASLGTTIHKM 260
Cdd:COG0165 192 nvsplGAAALAGT--TF------------PIDrERTAELLGFDGPTensldAVS----DRDFALEFLSAASLIMVHLSRL 253
|
170 180 190
....*....|....*....|....*....|....*..
gi 201065703 261 CSDLRILASRK----ELEEPFeSTqiGSSAMPYKRNP 293
Cdd:COG0165 254 AEELILWSSSEfgfvELPDAF-ST--GSSIMPQKKNP 287
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
10-165 |
2.41e-09 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 59.37 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 10 SPLSTRYASKeMQFLFSDQNKFSTWR-RLWV---WLAKAESRLGLE----ISDAQIAEMELQISNIDFEAAAAE---ERL 78
Cdd:PLN02848 13 SPLDGRYWSK-VKDLRPIFSEFGLIRyRVLVevkWLLKLSQIPEVTevppFSDEANSFLEGIIAGFSVDDALEVkkiERV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 79 TRHDVMAHVHVFAKQC---PSAAPV---IHLGATSCYVGDNTDLIVLRDAL-KLLLPRVASVIARLSQFAQSYKDQPTLG 151
Cdd:PLN02848 92 TNHDVKAVEYFLKQKCkshPELAKVlefFHFACTSEDINNLSHALMLKEGVnSVVLPTMDEIIKAISSLAHEFAYVPMLS 171
|
170
....*....|....
gi 201065703 152 FTHLQPAQLTTVGK 165
Cdd:PLN02848 172 RTHGQPASPTTLGK 185
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
117-293 |
7.44e-08 |
|
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: 54.74 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 117 IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVKGT 196
Cdd:cd01596 146 AAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 197 ---TG--TQASFLQLFngdgekVKQLDQLvTELaGFKKA---YAVTGqtySRKVDVEIVAALASLGTTIHKMCSDLRILA 268
Cdd:cd01596 226 avgTGlnAPPGYAEKV------AAELAEL-TGL-PFVTApnlFEATA---AHDALVEVSGALKTLAVSLSKIANDLRLLS 294
|
170 180 190
....*....|....*....|....*....|
gi 201065703 269 S--R---KELEEPfeSTQIGSSAMPYKRNP 293
Cdd:cd01596 295 SgpRaglGEINLP--ANQPGSSIMPGKVNP 322
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
117-297 |
1.47e-07 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 53.83 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 117 IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVKGT 196
Cdd:PRK13353 151 IAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 197 T-GTqasflqlfnGDGEKVKQLDQLVTELAgfkkayAVTGQTYSRKVD-----------VEIVAALASLGTTIHKMCSDL 264
Cdd:PRK13353 231 AvGT---------GLNADPEYIERVVKHLA------AITGLPLVGAEDlvdatqntdafVEVSGALKVCAVNLSKIANDL 295
|
170 180 190
....*....|....*....|....*....|....*.
gi 201065703 265 RILAS--RKELEEPF-ESTQIGSSAMPYKRNPMRSE 297
Cdd:PRK13353 296 RLLSSgpRTGLGEINlPAVQPGSSIMPGKVNPVMPE 331
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
117-293 |
5.41e-07 |
|
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: 51.75 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 117 IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVKGT 196
Cdd:cd01357 146 LALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 197 ---TGTQASflqlfNGDGEKVKQLDQLVTELaGFKKAYAVTGQTYSRKVDVEIVAALASLGTTIHKMCSDLRILAS--RK 271
Cdd:cd01357 226 aigTGINAP-----PGYIELVVEKLSEITGL-PLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSgpRA 299
|
170 180
....*....|....*....|....*
gi 201065703 272 ELEE---PfeSTQIGSSAMPYKRNP 293
Cdd:cd01357 300 GLGEinlP--AVQPGSSIMPGKVNP 322
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
122-293 |
1.28e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 50.51 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 122 ALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVKGT---TG 198
Cdd:PRK12273 158 SLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATaigTG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 199 TQASflqlfNGDGEKV-KQLDQlVTELaGFKKAYAVTGQTYSRKVDVEIVAALASLGTTIHKMCSDLRILAS--R---KE 272
Cdd:PRK12273 238 LNAP-----PGYIELVvEKLAE-ITGL-PLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSgpRaglNE 310
|
170 180
....*....|....*....|.
gi 201065703 273 LEEPfeSTQIGSSAMPYKRNP 293
Cdd:PRK12273 311 INLP--AVQAGSSIMPGKVNP 329
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
124-297 |
2.15e-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: 49.81 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 124 KLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVKGT---TG-- 198
Cdd:cd01362 154 ERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTavgTGln 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 199 TQASFlqlfngdGEKV-KQLDQLvTELAgFKKA----YAVTGQtysrkvD--VEIVAALASLGTTIHKMCSDLRILAS-- 269
Cdd:cd01362 234 AHPGF-------AEKVaAELAEL-TGLP-FVTApnkfEALAAH------DalVEASGALKTLAVSLMKIANDIRWLGSgp 298
|
170 180 190
....*....|....*....|....*....|.
gi 201065703 270 R---KELEEPfeSTQIGSSAMPYKRNPMRSE 297
Cdd:cd01362 299 RcglGELSLP--ENEPGSSIMPGKVNPTQCE 327
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
72-314 |
1.15e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 47.92 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 72 AAAEERLT-RHDVMAHVHVFAKQC-PSAAPVIHLGATSCYVGDNTDLIVLRDALKLLLPRVASVIARLSQFAQSYKDQPT 149
Cdd:PRK02186 479 APLLARPApRGLYMLYEAYLIERLgEDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCAL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 150 LGFTHLQPAQLTTVGKRacLWIQDLIM--DERALSRCLEDLRFRGVKGTTGTQASFLQlfngDGEKVKQLdqLVTELAGF 227
Cdd:PRK02186 559 PIYSQYQPALPGSLGHY--LLAVDGALarETHALFALFEHIDVCPLGAGAGGGTTFPI----DPEFVARL--LGFEQPAP 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 228 KKAYAVTgqtySRKVDVEIVAALASLGTTIHKMCSDLRILASRKE--LEEPFESTQiGSSAMPYKRNPMRSERCCALARH 305
Cdd:PRK02186 631 NSLDAVA----SRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFalVSLPDALTG-GSSMLPQKKNPFLLEFVKGRAGV 705
|
....*....
gi 201065703 306 LITLFSSAA 314
Cdd:PRK02186 706 VAGALASAS 714
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
126-297 |
2.25e-05 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 46.62 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 126 LLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGKRACLWIQDLIMDERALSRCLEDLRFRGVKGT---TG--TQ 200
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTavgTGlnAH 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 201 ASFlqlfngdGEKV-KQLDQLvTELAgFKKA----YAVTGQtysrkvD--VEIVAALASLGTTIHKMCSDLRILAS--RK 271
Cdd:PRK00485 240 PGF-------AERVaEELAEL-TGLP-FVTApnkfEALAAH------DalVEASGALKTLAVSLMKIANDIRWLASgpRC 304
|
170 180
....*....|....*....|....*....
gi 201065703 272 ---ELEEPfeSTQIGSSAMPYKRNPMRSE 297
Cdd:PRK00485 305 glgEISLP--ENEPGSSIMPGKVNPTQCE 331
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
117-293 |
8.21e-05 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 45.04 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 117 IVLRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQLTTVGK--RAclWIQDLIMDERALSRCLEDLRFRGVK 194
Cdd:COG1027 148 LALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQefGA--YAVALARDRWRLYEAAELLREVNLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 195 GT---TGtqasflqlFNGD---GEKVkqldqlVTELAgfkkayAVTGQTYSRKVD-----------VEIVAALASLGTTI 257
Cdd:COG1027 226 GTaigTG--------LNAPpgyIELV------VEHLA------EITGLPLVRAENlieatqdtdafVEVSGALKRLAVKL 285
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 201065703 258 HKMCSDLRILAS--R---KELEEPfeSTQIGSSAMPYKRNP 293
Cdd:COG1027 286 SKICNDLRLLSSgpRaglGEINLP--AVQPGSSIMPGKVNP 324
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
119-293 |
2.60e-04 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 43.56 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 119 LRDALKLLLPRVASVIARLSQFAQSYKDQPTLGFTHLQPAQlttvgkrACLWiQDLIMD-----ERALSRcLEDLRFRgv 193
Cdd:PLN02646 135 CRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQ-------PVLL-SHWLLShveqlERDAGR-LVDCRPR-- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 194 kgttgtqASFLQL----FNGDGEKVKQldQLVTELAGFKKAYAVTGQTYS-RKVDVEIVAALASLGTTIHKMCSDLRILA 268
Cdd:PLN02646 204 -------VNFCPLgscaLAGTGLPIDR--FMTAKDLGFTAPMRNSIDAVSdRDFVLEFLFANSITAIHLSRLGEEWVLWA 274
|
170 180
....*....|....*....|....*.
gi 201065703 269 SRK-ELEEPFESTQIGSSAMPYKRNP 293
Cdd:PLN02646 275 SEEfGFVTPSDAVSTGSSIMPQKKNP 300
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
139-316 |
3.16e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 43.05 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 139 QFAQSYKDQPTLGFTHLQPAQLTTVGKRAcLWIQDLImdERALSRCLEDLRFRGvKGTTGTQASFLQLFNGDGEKvkqld 218
Cdd:PRK06705 148 QLAADHKETIMPAYTHTQPAQPTTFGHYT-LAIYDTM--QRDLERMKKTYKLLN-QSPMGAAALSTTSFPIKRER----- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 219 qlVTELAGF----KKAY-AVTGQTYSRKVDVEIVAALASLGTTIHkmcsDLRILASRK----ELEEPFesTQIgSSAMPY 289
Cdd:PRK06705 219 --VADLLGFtnviENSYdAVAGADYLLEVSSLLMVMMTNTSRWIH----DFLLLATKEydgiTVARPY--VQI-SSIMPQ 289
|
170 180 190
....*....|....*....|....*....|.
gi 201065703 290 KRNPMRSERCCALARHLI----TLFSSAANT 316
Cdd:PRK06705 290 KRNPVSIEHARAITSSALgeafTVFQMIHNT 320
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
245-314 |
2.45e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 40.26 E-value: 2.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201065703 245 EIVAALASLGTTIHKMCSDLRILASRKELEEPFESTQiGSSAMPYKRNPMRSERCCALARHLITLFSSAA 314
Cdd:PRK06389 232 NISYLISSLAVDLSRICQDIIIYYENGIITIPDEFTT-GSSLMPNKRNPDYLELFQGIAAESISVLSFIA 300
|
|
| |
