|
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: 663.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 4 RYSRPEMANIWTEENKYKAWLEVEILADEAWAELGEIPKEDVALIREKAGFDIDRILEIEQETRHDVVAFTRAVSETLGE 83
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 84 ERKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKR 163
Cdd:cd01360 81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 164 NIERFEIAAAGVEAGKISGAVGNFANIPPFVESYVCEKLGIRPQEISTQVLPRDLHAEYFSTLALIATSIERMATEIRGL 243
Cdd:cd01360 161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 244 QKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAERIIAPDTTILIDYM 323
Cdd:cd01360 241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 324 LNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKtahswdnqvdfkplleadpevtsrl 403
Cdd:cd01360 321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQRE------------------------- 375
|
410 420
....*....|....*....|....
gi 332364906 404 tqeeideifnpvYYTKRVDEIFKR 427
Cdd:cd01360 376 ------------YYLKHVDEIFKR 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: 639.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 1 MI-NRYSRPEMANIWTEENKYKAWLEVEILADEAWAELGEIPKEDVALIREKA---GFDIDRILEIEQETRHDVVAFTRA 76
Cdd:COG0015 1 LIsPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAAddfEIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 77 VSETLG-EERKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLA 155
Cdd:COG0015 81 LKEKVGaEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 156 TWYSEMKRNIERFEIAAAGVEAGKISGAVGNFANIP---PFVESYVCEKLGIRPQEISTQVLPRDLHAEYFSTLALIATS 232
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 233 IERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAERII 312
Cdd:COG0015 241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 313 APDTTILIDYMLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKTAHSWDNQVDFKPL 392
Cdd:COG0015 321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 332364906 393 LEADPEVTSRLTQEEIDEIFNPVYYTKRVDEIFKRV 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: 564.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 1 MINRYSRPEMANIWTEENKYKAWLEVEILADEAWAELGEIPKEDVALIREKAGF---DIDRILEIEQETRHDVVAFTRAV 77
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFtevDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 78 SETLGEERKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATW 157
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 158 YSEMKRNIERFEIAAAGVEAGKISGAVGNFANIPP---FVESYVCEKLGIRPQEISTQVLPRDLHAEYFSTLALIATSIE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 235 RMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAERIIAP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 315 DTTILIDYMLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKTAHSWDNQV-DFKPLL 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEpDLLEFL 400
|
410 420 430
....*....|....*....|....*....|....*
gi 332364906 394 EADPEVTSRLTQEEIDEIFNPVYYTKRVDEIFKRV 428
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
10-379 |
0e+00 |
|
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: 522.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 10 MANIWTEENKYKAWLEVEILADEAWAELGEIPKEDVALIREKA---GFDIDRILEIEQETRHDVVAFTRAVSETLGEE-R 85
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAAdvfEIDAERIAEIEKETGHDVIAFVYALAEKCGEDaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 86 KWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNI 165
Cdd:cd01595 81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 166 ERFEIAAAGVEAGKISGAVGNFANI---PPFVESYVCEKLGIRPQEISTQVLPRDLHAEYFSTLALIATSIERMATEIRG 242
Cdd:cd01595 161 ERLEEARERVLVGGISGAVGTHASLgpkGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 243 LQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAERIIAPDTTILIDY 322
Cdd:cd01595 241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 332364906 323 MLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKT 379
Cdd:cd01595 321 ALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKEEN 377
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
20-336 |
1.66e-114 |
|
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: 338.32 E-value: 1.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 20 YKAWLEVEILADEAWAELGEIPKEDVALIREKAGFDIDRIL----EIEQETRHDVVAFTRAVSETLGEE-RKWVHYGLTS 94
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAadqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 95 TDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEIAAAG 174
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 175 VEAGKI-SGAVGNFANIPPFVESYVCEKLGI-RPQEISTQ-VLPRDLHAEYFSTLALIATSIERMATEIRGLQKSEQREV 251
Cdd:cd01334 161 LNVLPLgGGAVGTGANAPPIDRERVAELLGFfGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 252 EEFFAKgQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAERIIAPDTTILIDYMLNRFGNIV 331
Cdd:cd01334 241 ELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319
|
....*
gi 332364906 332 KNLTV 336
Cdd:cd01334 320 EGLEV 324
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
5-418 |
2.26e-113 |
|
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: 339.60 E-value: 2.26e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 5 YSRPEMANIWTEENKYKAWLEVEI-LAdEAWAELGEIPKEDVALIREKAG---FDIDRILEIEQETRHDVVAFTRAVSET 80
Cdd:cd01597 6 FGTPAMREIFSDENRVQAMLDVEAaLA-RAQAELGVIPKEAAAEIAAAADverLDLEALAEATARTGHPAIPLVKQLTAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 81 LGEE-RKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYS 159
Cdd:cd01597 85 CGDAaGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 160 EMKRNIERFEIAAAGVEAGKISGAVGNFA---NIPPFVESYVCEKLGIRPQEISTQVLpRDLHAEYFSTLALIATSIERM 236
Cdd:cd01597 165 ELLRHRERLDELRPRVLVVQFGGAAGTLAslgDQGLAVQEALAAELGLGVPAIPWHTA-RDRIAELASFLALLTGTLGKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 237 ATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAERIIAPDT 316
Cdd:cd01597 244 ARDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 317 TILIDYMLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKgMTREQAYDLVQPKTAHSWDNQVDFKPLLEAD 396
Cdd:cd01597 324 FLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRAVEEGRPLREVLLED 402
|
410 420
....*....|....*....|..
gi 332364906 397 PEVTSRLTQEEIDEIFNPVYYT 418
Cdd:cd01597 403 PEVAAYLSDEELDALLDPANYL 424
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
200-419 |
5.45e-93 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 279.22 E-value: 5.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 200 EKLGIRPQEIStqvlprdlhAEYfsTLALIATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTG 279
Cdd:PRK08937 8 AELGVIPKEDI---------AEI--VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 280 LARVIRGHMVTAFENVSLWHERDISHSSAERIIAPDTTILIDYMLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAML 359
Cdd:PRK08937 77 LARVLRSYLVTALENVPLWHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 360 TLIEKGMTREQAYDLVQPKTAHSWDNQVDFKPLLEADPEVTSRLTQEEIDEIFNPVYYTK 419
Cdd:PRK08937 157 ELVEKGMGREEAHELIREKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
4-286 |
4.23e-83 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 257.68 E-value: 4.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 4 RYS--RPEMANIWTEENKYKAWLEVE-----ILADEAWAELGEIPKEDVALIREKA-----GFDIDRILEIEQETRHDVV 71
Cdd:pfam00206 2 RFTvpADALMGIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKALdevaeEGKLDDQFPLKVWQEGSGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 72 AFTRAVSETLGE-------ERKWVHYGLTSTDVVDTAYGYLYKQAN-DIIREDLRRFTDIIAERAREHKFTIMMGRTHGV 143
Cdd:pfam00206 82 AVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 144 HAEPTTFGLKLATWYSEMKRNIERFEIAAAGVEAGKISG--AVGNFANIPPFVESYVCEKLG------IRPQEISTQVLP 215
Cdd:pfam00206 162 DATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATSD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332364906 216 RDLHAEYFSTLALIATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRG 286
Cdd:pfam00206 242 RDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
4-420 |
2.39e-66 |
|
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: 218.34 E-value: 2.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 4 RYSRPEMANIWTEENKYKAWLEVEILADEAWAELG-EIPKEDVA-LIREKAGFDIDRILEIEQETRHDVVAFTRAVSETL 81
Cdd:cd03302 4 RYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGlDISDEQIEeMKANVENIDFEIAAAEEKKLRHDVMAHVHAFGLLC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 82 GEERKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEM 161
Cdd:cd03302 84 PAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 162 KRNIERFEIAAAGVEAGKISGAVGNFANIPPFVESY----------VCEKLGI-RPQEISTQVLPRDLHAEYFSTLALIA 230
Cdd:cd03302 164 LMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDhdkvealdelVTKKAGFkKVYPVTGQTYSRKVDIDVLNALSSLG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 231 TSIERMATEIRGLQKSEqrEVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSL-WHERDISHSSAE 309
Cdd:cd03302 244 ATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTqWFERTLDDSANR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 310 RIIAPDTTILIDYMLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQpKTAHSWDNQV-- 387
Cdd:cd03302 322 RIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIR-VLSHQAAAVVkq 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 332364906 388 -----DFKPLLEADPEVtsRLTQEEIDEIFNPVYYTKR 420
Cdd:cd03302 401 eggdnDLIERIKNDAYF--KPIWDELDALLDPKTFIGR 436
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
72-327 |
2.75e-59 |
|
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: 193.21 E-value: 2.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 72 AFTRAVSETLGEER--KWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTT 149
Cdd:cd01594 19 VLAGRAGELAGGLHgsALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 150 FGLKLATWYSEMKRNIERFEIAAagveagkisgavgnfanippfvesyvceklgirpqeistqvlprdlHAEYFSTLALI 229
Cdd:cd01594 99 LGYELRAWAQVLGRDLERLEEAA----------------------------------------------VAEALDALALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 230 ATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSSAE 309
Cdd:cd01594 133 AAHLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSM 212
|
250
....*....|....*...
gi 332364906 310 RIIAPDTTILIDYMLNRF 327
Cdd:cd01594 213 REILADSLLLLIDALRLL 230
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
5-417 |
1.17e-57 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 196.00 E-value: 1.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 5 YSRPEMANIWTEENKYKAWLEVEILADEAWAELGEIPKEDVALIRE---KAGFDIDRI---------LEIEQetrhdVVA 72
Cdd:PRK09053 12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAacdAERLDLDALaqaaalagnLAIPL-----VKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 73 FTRAVSETLGEERKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGL 152
Cdd:PRK09053 87 LTAQVAARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 153 KLATWYSEMKRNIERFEIAAAGVEAGKISGAVGNFANI----PPFVESYVCE-KLGIRPQEISTQvlpRDLHAEYFSTLA 227
Cdd:PRK09053 167 KFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqaLPVAQALAAElQLALPALPWHTQ---RDRIAEFASALG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 228 LIATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHERDISHSS 307
Cdd:PRK09053 244 LLAGTLGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 308 AERIIAPDTTILIDYMLNRFGNIVKNLTVFPENMKRNMNSTFGLIFSQRAMLTLIEKgMTREQAYDLVQPKTAHSWDNQV 387
Cdd:PRK09053 324 AEWDTLPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADR-IGRLDAHHLVEQASKRAVAEGR 402
|
410 420 430
....*....|....*....|....*....|
gi 332364906 388 DFKPLLEADPEVTSRLTQEEIDEIFNPVYY 417
Cdd:PRK09053 403 HLRDVLAEDPQVSAHLSPAALDRLLDPAHY 432
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
5-301 |
3.42e-46 |
|
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: 162.61 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 5 YSRPEMANIWTEENKYKAWLEVEILADEAWAELGEIPKE---DVALIREKAGFDIDrilEIEQETRHD---VVAFTRAVS 78
Cdd:TIGR02426 6 FGDPAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEaaaAIEAACAAAAPDLE---ALAHAAATAgnpVIPLVKALR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 79 ETLGEE-RKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATW 157
Cdd:TIGR02426 83 KAVAGEaARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 158 YSEMKRNIERFEIAAAGVEAGKISGAVGNFANIPPF---VESYVCEKLGIRPQEISTQVLpRDLHAEYFSTLALIATSIE 234
Cdd:TIGR02426 163 LAAVLRARDRLAALRTRALPLQFGGAAGTLAALGTRggaVAAALAARLGLPLPALPWHTQ-RDRIAEFGSALALVAGALG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332364906 235 RMATEIRGLQKSEqreVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFENVSLWHER 301
Cdd:TIGR02426 242 KIAGDIALLSQTE---VGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHER 305
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
18-276 |
2.91e-41 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 152.21 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 18 NKYKAWLEVE---ILADEAwaELGEIP---KEDVALIRE-KAGF---DIDRILEIEQETRHDVVA---FTRAVSETLGEE 84
Cdd:PRK09285 33 IRYRVQVEVEwliALAAHP--GIPEVPpfsAEANAFLRAiVENFseeDAARIKEIERTTNHDVKAveyFLKEKLAGLPEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 85 RK---WVHYGLTSTDVVDTAYGYLYKQA-NDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSE 160
Cdd:PRK09285 111 EAvseFIHFACTSEDINNLSHALMLKEArEEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 161 MKRNIERFEiaaaGVE-AGKISGAVGNFA---------NIPPFVESYVcEKLGIRPQEISTQVLPRDLHAEYFSTLALIA 230
Cdd:PRK09285 191 LERQLKQLE----AVEiLGKINGAVGNYNahlaaypevDWHAFSREFV-ESLGLTWNPYTTQIEPHDYIAELFDAVARFN 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 332364906 231 TSIERMATEIRGL-------QKSEQREVeeffakgqkGSSAMPHKRNPIGSEN 276
Cdd:PRK09285 266 TILIDLDRDVWGYislgyfkQKTKAGEI---------GSSTMPHKVNPIDFEN 309
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
18-310 |
3.28e-39 |
|
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: 145.84 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 18 NKYKAWLEVEIL----ADEAWAELGEIPKEDVALIREKA-GF---DIDRILEIEQETRHDVVA---FTRAVSETLGEERK 86
Cdd:cd01598 11 IKYRVQVEVEWLialsNLEEIPEVPPLTKEELKFLRAIIeNFseeDALRIKEIEATTNHDVKAveyFLKEKFETLGLLKK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 87 ---WVHYGLTSTDVVDTAYGYLYKQA-NDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMK 162
Cdd:cd01598 91 ikeFIHFACTSEDINNLAYALMIKEArNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 163 R---NIERFEIaaagveAGKISGAVGNFA---------NIPPFVESYVcEKLGIRPQEISTQVLPRDLHAEYFSTLALIA 230
Cdd:cd01598 171 RqykQLKQIEI------LGKFNGAVGNFNahlvaypdvDWRKFSEFFV-TSLGLTWNPYTTQIEPHDYIAELFDALARIN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 231 TSIERMATEIRGL-------QKSEQREVeeffakgqkGSSAMPHKRNPIGSENMTG---LARVIRGHMVTAFEnVSLWhE 300
Cdd:cd01598 244 TILIDLCRDIWGYislgyfkQKVKKGEV---------GSSTMPHKVNPIDFENAEGnlgLSNALLNHLSAKLP-ISRL-Q 312
|
330
....*....|
gi 332364906 301 RDISHSSAER 310
Cdd:cd01598 313 RDLTDSTVLR 322
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
350-429 |
6.31e-34 |
|
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: 121.79 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 350 GLIFSQRAMLTLIEKGMTREQAYDLVQPKTAHSWDNQVDFKPLLEADPEVTSRLTQEEIDEIFNPVYYTKRVDEIFKRVG 429
Cdd:smart00998 2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
8-282 |
7.10e-28 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 113.23 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 8 PEMANIWTEENKYKAWLEVEILADEAWAELGEIPKEDVALIREK-AGFDIDrILEIEQETRHD---VVAFTRAVSETLGE 83
Cdd:PRK05975 18 DEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIAAAcETFEPD-LAALRHATARDgvvVPALVRQLRAAVGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 84 E-RKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMK 162
Cdd:PRK05975 97 EaAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 163 RNIERFEIAAAGVEAGKISGAVGNFANI---PPFVESYVCEKLGI--RPQEISTqvlpRDLHAEYFSTLALIATSIERMA 237
Cdd:PRK05975 177 RHRDRLEALRADVFPLQFGGAAGTLEKLggkAAAVRARLAKRLGLedAPQWHSQ----RDFIADFAHLLSLVTGSLGKFG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 332364906 238 TEIrGLQKSEQREVEeffAKGQKGSSAMPHKRNPIGSENMTGLAR 282
Cdd:PRK05975 253 QDI-ALMAQAGDEIS---LSGGGGSSAMPHKQNPVAAETLVTLAR 293
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
350-428 |
1.32e-25 |
|
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: 99.03 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 350 GLIFSQRAMLTLIeKGMTREQAYDLVQPKTAHSWD-NQVDFKPLLEADPEVTsRLTQEEIDEIFNPVYYTKRVDEIFKRV 428
Cdd:pfam10397 1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEeGKNDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADEIVDRV 78
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
25-310 |
1.93e-22 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 99.04 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 25 EVEILADEAWAELGEIpkedvalireKAGFDIDRILE---IEQETRHDVVA---FTRAVSETLGEERK---WVHYGLTST 95
Cdd:PLN02848 58 EVPPFSDEANSFLEGI----------IAGFSVDDALEvkkIERVTNHDVKAveyFLKQKCKSHPELAKvleFFHFACTSE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 96 DVVDTAYGYLYKQA-NDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRniERFEIAAAG 174
Cdd:PLN02848 128 DINNLSHALMLKEGvNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSR--QRKQLSEVK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 175 VEaGKISGAVGNF---------ANIPPFVESYVcEKLGIRPQEISTQVLPRDLHAEYFSTLALIATSIERMATEIRG--- 242
Cdd:PLN02848 206 IK-GKFAGAVGNYnahmsaypeVDWPAVAEEFV-TSLGLTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWSyis 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332364906 243 LQKSEQREVeeffaKGQKGSSAMPHKRNPIGSENMTG---LARVIRGHMVTAFEnVSLWhERDISHSSAER 310
Cdd:PLN02848 284 LGYFKQITK-----AGEVGSSTMPHKVNPIDFENSEGnlgLANAELSHLSMKLP-ISRM-QRDLTDSTVLR 347
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
24-415 |
5.27e-22 |
|
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: 97.62 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 24 LEVEILADEAWA----ELGEIPKEDVALIR----------EKAGFDIDrileIEQEtrhDVV-AFTRAVSETLGEERKWV 88
Cdd:cd01359 9 FEEDIAGSIAHAvmlaEQGILTEEEAAKILaglakiraeiEAGAFELD----PEDE---DIHmAIERRLIERIGDVGGKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 89 HYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERF 168
Cdd:cd01359 82 HTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 169 EIAAAGVE---AGkiSGA-VGNFANIPPfveSYVCEKLG---IRPQEISTqVLPRDLHAEYFSTLALIATSIERMATEIR 241
Cdd:cd01359 162 ADAYKRVNvspLG--AGAlAGTTFPIDR---ERTAELLGfdgPTENSLDA-VSDRDFVLEFLSAAALLMVHLSRLAEDLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 242 gLQKSEQR---EVEEFFAkgqKGSSAMPHKRNPIGSENMTGLA-RVIrGH---MVTAFENVSLWHERDISHSSAERIIAP 314
Cdd:cd01359 236 -LWSTQEFgfvELPDAYS---TGSSIMPQKKNPDVLELIRGKAgRVI-GAlagLLTTLKGLPLAYNKDLQEDKEPLFDAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 315 DTTILidyMLNRFGNIVKNLTVFPENMKRNMNSTFGLIfSQRAMLTLIEKGMTREQAYDLVQPKTAHSWDNQVDFKPLLE 394
Cdd:cd01359 311 DTLIA---SLRLLTGVISTLTVNPERMREAAEAGFSTA-TDLADYLVREKGVPFREAHHIVGRAVRLAEEKGKDLSDLTL 386
|
410 420
....*....|....*....|.
gi 332364906 395 ADPEVTSRLTQEEIDEIFNPV 415
Cdd:cd01359 387 AELQAISPLFEEDVREALDPE 407
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
28-271 |
1.19e-16 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 81.74 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 28 ILADEAWA-ELGE---IPKEDVALIR----------EKAGFDIDRILE-----IEqetrhdvvaftRAVSETLGEERKWV 88
Cdd:PRK00855 37 IAGSIAHArMLAKqgiLSEEEAEKILagldeileeiEAGKFEFSPELEdihmaIE-----------ARLTERIGDVGGKL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 89 HYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERF 168
Cdd:PRK00855 106 HTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 169 EI-----------AAAGveAGKisgavgNFaNIPPFvesYVCEKLGI-RPQEISTQ-VLPRDLHAEYFSTLALIATSIER 235
Cdd:PRK00855 186 RDarkrvnrsplgSAAL--AGT------TF-PIDRE---RTAELLGFdGVTENSLDaVSDRDFALEFLSAASLLMVHLSR 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 332364906 236 MATEIrglqkseqreV----EEF--------FAkgqKGSSAMPHKRNP 271
Cdd:PRK00855 254 LAEEL----------IlwssQEFgfvelpdaFS---TGSSIMPQKKNP 288
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
117-284 |
4.59e-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: 58.28 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 117 LRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEIAAAGVEAGKISG-AVGNFANIPP-FV 194
Cdd:cd01362 160 LKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGtAVGTGLNAHPgFA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 195 ESyVCEKL----GIRPQE-------ISTQvlprDLHAEYFSTLALIATSIERMATEIR--------GLQkseqrevEEFF 255
Cdd:cd01362 240 EK-VAAELaeltGLPFVTapnkfeaLAAH----DALVEASGALKTLAVSLMKIANDIRwlgsgprcGLG-------ELSL 307
|
170 180 190
....*....|....*....|....*....|
gi 332364906 256 AKGQKGSSAMPHKRNPIGSENMTGL-ARVI 284
Cdd:cd01362 308 PENEPGSSIMPGKVNPTQCEALTMVaAQVM 337
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
105-278 |
1.26e-08 |
|
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: 56.76 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 105 LYKQANDIIREdLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEIAAAGVEAGKISG-A 183
Cdd:cd01357 148 LILLLRKLLDA-LAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGtA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 184 VGNFANIPPFVESYVCEKLgirpQEISTQVLPR-----------DLHAEYFSTLALIATSIERMATEIRgLQKSEQR--- 249
Cdd:cd01357 227 IGTGINAPPGYIELVVEKL----SEITGLPLKRaenlidatqntDAFVEVSGALKRLAVKLSKIANDLR-LLSSGPRagl 301
|
170 180 190
....*....|....*....|....*....|....*..
gi 332364906 250 ------EVeeffakgQKGSSAMPHKRNPIGSE--NMT 278
Cdd:cd01357 302 geinlpAV-------QPGSSIMPGKVNPVIPEvvNQV 331
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
117-284 |
1.46e-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: 56.66 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 117 LRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEIAAAGVEAGKISG-AVGNFANIPPFVE 195
Cdd:cd01596 159 LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGtAVGTGLNAPPGYA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 196 SYVCEKLgirpQEISTqvLP-------------RDLHAEYFSTLALIATSIERMATEIR--------GLQKSEQREVeef 254
Cdd:cd01596 239 EKVAAEL----AELTG--LPfvtapnlfeataaHDALVEVSGALKTLAVSLSKIANDLRllssgpraGLGEINLPAN--- 309
|
170 180 190
....*....|....*....|....*....|.
gi 332364906 255 fakgQKGSSAMPHKRNPIGSENMTGLA-RVI 284
Cdd:cd01596 310 ----QPGSSIMPGKVNPVIPEAVNMVAaQVI 336
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
35-284 |
1.39e-07 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 53.56 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 35 AELGEIPKEDVALIREKAgfdiDRILEieqeTRHD----------------------VVAfTRAvSETLGEER---KWVH 89
Cdd:PRK00485 60 AELGLLDAEKADAIVAAA----DEVIA----GKHDdhfpldvwqtgsgtqsnmnvneVIA-NRA-SELLGGELgskKPVH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 90 ------YGLTSTDVVDTAygyLYKQANDIIREDL----RRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYS 159
Cdd:PRK00485 130 pndhvnMSQSSNDTFPTA---MHIAAVLAIVERLlpalEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 160 EMKRNIERFEIAAAGVEAGKISG-AVGNFANIPP-FVESyVCEklgirpqEISTQV-LP-------------RD----LH 219
Cdd:PRK00485 207 QLEHGIERIEAALPHLYELALGGtAVGTGLNAHPgFAER-VAE-------ELAELTgLPfvtapnkfealaaHDalveAS 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332364906 220 AeyfsTLALIATSIERMATEIRglqkseqreveeFFAKG-------------QKGSSAMPHKRNPIGSENMTGL-ARVI 284
Cdd:PRK00485 279 G----ALKTLAVSLMKIANDIR------------WLASGprcglgeislpenEPGSSIMPGKVNPTQCEALTMVcAQVM 341
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
67-290 |
1.94e-07 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 53.19 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 67 RHDV-VAFTRAVSETLGEERKWVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHA 145
Cdd:PLN02646 95 REDVhMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 146 EPTTFGLKLATWYSEMKRNIERFEIAAAGVEAGKI-SGAV-GNFANIPPFVESyvcEKLGI-RPQEISTQ-VLPRDLHAE 221
Cdd:PLN02646 175 QPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLgSCALaGTGLPIDRFMTA---KDLGFtAPMRNSIDaVSDRDFVLE 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332364906 222 YFSTLALIATSIERMATEIRgLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVT 290
Cdd:PLN02646 252 FLFANSITAIHLSRLGEEWV-LWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVT 319
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
94-284 |
1.92e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 49.98 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 94 ST-DVVDTAYGY-LYKQANDIIREdLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEIA 171
Cdd:PRK13353 140 STnDVFPTAIRIaALNLLEGLLAA-MGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 172 AAGVEAGKISG-AVGNFANIPPFVESYVCEKLgirpQEIS-------------TQVLprDLHAEYFSTLALIATSIERMA 237
Cdd:PRK13353 219 REHLYEVNLGGtAVGTGLNADPEYIERVVKHL----AAITglplvgaedlvdaTQNT--DAFVEVSGALKVCAVNLSKIA 292
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 332364906 238 TEIRgLQKSEQRE-VEEFF--AKgQKGSSAMPHKRNPIGSENMTGLA-RVI 284
Cdd:PRK13353 293 NDLR-LLSSGPRTgLGEINlpAV-QPGSSIMPGKVNPVMPEVVNQIAfQVI 341
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
21-286 |
2.73e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 49.78 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 21 KAWLEVEILADEAWAELGEIPKEDVALIREkagfDIDRILEIEQETRHDVVAftRAVSETLGEERKWVHYGLTSTDVVDT 100
Cdd:PRK12308 42 KALLSVGVLSEEEQQKLELALNELKLEVME----DPEQILLSDAEDIHSWVE--QQLIGKVGDLGKKLHTGRSRNDQVAT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 101 AYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHAEPTTFglklATW---YSEM-KRNIERFEIAAAGVE 176
Cdd:PRK12308 116 DLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTF----AHWclaYVEMfERDYSRLEDALTRLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 177 AGKI-SGAVGNFANipPFVESYVCEKLGIRPQEIST--QVLPRDLHAEYFSTLALIATSIERMATEIRGLQKSEQREVeE 253
Cdd:PRK12308 192 TCPLgSGALAGTAY--PIDREALAHNLGFRRATRNSldSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSGESGFI-E 268
|
250 260 270
....*....|....*....|....*....|...
gi 332364906 254 FFAKGQKGSSAMPHKRNPIGSEnmtglarVIRG 286
Cdd:PRK12308 269 LADTVTSGSSLMPQKKNPDALE-------LIRG 294
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
15-293 |
9.80e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 47.67 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 15 TEENKYKAWLEVEILadEAWAELGEIPKEDvaLIREKAGFDIDRILE--IEQETRHDVVAFtravsetlgeerkwVHYGL 92
Cdd:PRK06705 53 TEENLMKKEEAKFIL--HALKKVEEIPEEQ--LLYTEQHEDLFFLVEhlISQEAKSDFVSN--------------MHIGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 93 TSTDVVDTAYgylykqandiiREDLRRFT-----------DIIAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEM 161
Cdd:PRK06705 115 SRNDMGVTMY-----------RMSLRRYVlrlmehhlllqESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 162 KRNIERFEIAAAGVEAGKISGAVGNFANIPPFVESyVCEKLGIRP--QEISTQVLPRDLHAEYFSTLALIATSIERMATE 239
Cdd:PRK06705 184 QRDLERMKKTYKLLNQSPMGAAALSTTSFPIKRER-VADLLGFTNviENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHD 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 332364906 240 IRGLQKSEQREVEefFAKGQ-KGSSAMPHKRNPIGSENMTGLARVIRGHMVTAFE 293
Cdd:PRK06705 263 FLLLATKEYDGIT--VARPYvQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQ 315
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
68-281 |
5.07e-05 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 45.38 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 68 HDVVAfTRAVsETLGEERKWVHY---------GLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMG 138
Cdd:PRK14515 114 NEVIA-NRAL-ELLGMEKGDYHYispnshvnmAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 139 RTHGVHAEPTTFGLKLATWYSEMKRNIERFEIAAAGV-EAGKISGAVGNFANIPP-FVESYVCEKLGIRPQEI------- 209
Cdd:PRK14515 192 RTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLyEVNMGATAVGTGLNADPeYIEAVVKHLAAISELPLvgaedlv 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332364906 210 -STQvlPRDLHAEYFSTLALIATSIERMATEIRgLQKSEQRE--VEEFFAKGQKGSSAMPHKRNPIGSENMTGLA 281
Cdd:PRK14515 272 dATQ--NTDAYTEVSAALKVCMMNMSKIANDLR-LMASGPRVglAEIMLPARQPGSSIMPGKVNPVMPEVINQIA 343
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
124-290 |
1.14e-04 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 44.14 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 124 IAERAREHKFTIMMGRTHGVHAEPTTFGLKLATWYSEM---KRNIER-----FEIAAAGVeagkisgAVGNFANIPP-FV 194
Cdd:PRK12425 169 LAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLdyaERAIRAalpavCELAQGGT-------AVGTGLNAPHgFA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 195 ESYVCEKLGIRPqeistqvLPRDLHAEYFSTLA-------------LIATSIERMATEIRGLQKSEQREVEEF-FAKGQK 260
Cdd:PRK12425 242 EAIAAELAALSG-------LPFVTAPNKFAALAgheplvslsgalkTLAVALMKIANDLRLLGSGPRAGLAEVrLPANEP 314
|
170 180 190
....*....|....*....|....*....|
gi 332364906 261 GSSAMPHKRNPIGSENMTGLARVIRGHMVT 290
Cdd:PRK12425 315 GSSIMPGKVNPTQCEALSMLACQVMGNDAT 344
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
67-291 |
1.59e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.07 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 67 RHDVVAFTRAVSETLGEERK-WVHYGLTSTDVVDTAYGYLYKQANDIIREDLRRFTDIIAERAREHKFTIMMGRTHGVHA 145
Cdd:PRK02186 488 RGLYMLYEAYLIERLGEDVGgVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364906 146 EPTTFGLKLATWYSEMKRNIERF-----EIAAAGVEAGkiSGAVGNFANIPPFVesyvCEKLGI-RPQEIS-TQVLPRDL 218
Cdd:PRK02186 568 LPGSLGHYLLAVDGALARETHALfalfeHIDVCPLGAG--AGGGTTFPIDPEFV----ARLLGFeQPAPNSlDAVASRDG 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332364906 219 HAEYFSTLALIATSIERMATEirgLQKSEQREVE--EFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMVTA 291
Cdd:PRK02186 642 VLHFLSAMAAISTVLSRLAQD---LQLWTTREFAlvSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASA 713
|
|
| |
