|
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: 661.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 4 RYSRPEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIRKKADFDIDRILEIEQETRHDVVAFTRAVSETLGE 83
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 84 ERKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKR 163
Cdd:cd01360 81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 164 NIERFEHAAAGVEAGKISGAVGNFANIPPFVEEYVCDKLGIRAQEISTQVLPRDLHAEYFAVLASIATSIERMATEIRGL 243
Cdd:cd01360 161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 244 QKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAERIITPDTTILIDYM 323
Cdd:cd01360 241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 324 LNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKtayswdnqvdfkplleadsevtsrl 403
Cdd:cd01360 321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQRE------------------------- 375
|
410 420
....*....|....*....|....
gi 446533399 404 tqeeideifnpvYYTKRVDDIFER 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: 634.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 1 MI-NRYSRPEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIRKKAD---FDIDRILEIEQETRHDVVAFTRA 76
Cdd:COG0015 1 LIsPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADdfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 77 VSETLG-EERKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLA 155
Cdd:COG0015 81 LKEKVGaEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 156 TWYSEMKRNIERFEHAAAGVEAGKISGAVGNFANIP---PFVEEYVCDKLGIRAQEISTQVLPRDLHAEYFAVLASIATS 232
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 233 IERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAERII 312
Cdd:COG0015 241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 313 TPDTTILIDYMLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKTAYSWDNQVDFKPL 392
Cdd:COG0015 321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 446533399 393 LEADSEVTSRLTQEEIDEIFNPVYYTKRVDDIFERL 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: 562.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 1 MINRYSRPEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIRKKADF---DIDRILEIEQETRHDVVAFTRAV 77
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFtevDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 78 SETLGEERKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATW 157
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 158 YSEMKRNIERFEHAAAGVEAGKISGAVGNFANIPP---FVEEYVCDKLGIRAQEISTQVLPRDLHAEYFAVLASIATSIE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 235 RMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAERIITP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 315 DTTILIDYMLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKTAYSWDNQV-DFKPLL 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEpDLLEFL 400
|
410 420 430
....*....|....*....|....*....|....*
gi 446533399 394 EADSEVTSRLTQEEIDEIFNPVYYTKRVDDIFERL 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: 525.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 10 MANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIRKKAD---FDIDRILEIEQETRHDVVAFTRAVSETLGEE-R 85
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADvfeIDAERIAEIEKETGHDVIAFVYALAEKCGEDaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 86 KWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNI 165
Cdd:cd01595 81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 166 ERFEHAAAGVEAGKISGAVGNFANI---PPFVEEYVCDKLGIRAQEISTQVLPRDLHAEYFAVLASIATSIERMATEIRG 242
Cdd:cd01595 161 ERLEEARERVLVGGISGAVGTHASLgpkGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 243 LQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAERIITPDTTILIDY 322
Cdd:cd01595 241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446533399 323 MLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKT 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 |
3.69e-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: 337.55 E-value: 3.69e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 20 YRAWLEVEILSDEAWAELGEIPKEDVALIRKKADFDIDRIL----EIEQETRHDVVAFTRAVSETLGEE-RKWVHYGLTS 94
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAadqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 95 TDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAG 174
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 175 VEAGKI-SGAVGNFANIPPFVEEYVCDKLGI-RAQEISTQ-VLPRDLHAEYFAVLASIATSIERMATEIRGLQKSEQREV 251
Cdd:cd01334 161 LNVLPLgGGAVGTGANAPPIDRERVAELLGFfGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 252 EEFFAKgQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAERIITPDTTILIDYMLNRFGNIV 331
Cdd:cd01334 241 ELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319
|
....*
gi 446533399 332 KNLTV 336
Cdd:cd01334 320 EGLEV 324
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
5-427 |
1.94e-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: 1.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 5 YSRPEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIRKKAD---FDIDRILEIEQETRHDVVAFTRAVSETL 81
Cdd:cd01597 6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADverLDLEALAEATARTGHPAIPLVKQLTAAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 82 GEE-RKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSE 160
Cdd:cd01597 86 GDAaGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 161 MKRNIERFEHAAAGVEAGKISGAVGNFA---NIPPFVEEYVCDKLGIRAQEISTQVLpRDLHAEYFAVLASIATSIERMA 237
Cdd:cd01597 166 LLRHRERLDELRPRVLVVQFGGAAGTLAslgDQGLAVQEALAAELGLGVPAIPWHTA-RDRIAELASFLALLTGTLGKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 238 TEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAERIITPDTT 317
Cdd:cd01597 245 RDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 318 ILIDYMLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKgMTREQAYDLVQPKTAYSWDNQVDFKPLLEADS 397
Cdd:cd01597 325 LLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRAVEEGRPLREVLLEDP 403
|
410 420 430
....*....|....*....|....*....|....
gi 446533399 398 EVTSRLTQEEIDEIFNPVYYT----KRVDDIFER 427
Cdd:cd01597 404 EVAAYLSDEELDALLDPANYLgsapALVDRVLAR 437
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
225-419 |
6.73e-91 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 274.21 E-value: 6.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 225 VLASIATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDIS 304
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 305 HSSAERIITPDTTILIDYMLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLVQPKTAYSWD 384
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWK 181
|
170 180 190
....*....|....*....|....*....|....*
gi 446533399 385 NQVDFKPLLEADSEVTSRLTQEEIDEIFNPVYYTK 419
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
4-286 |
5.62e-85 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 262.30 E-value: 5.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 4 RYS--RPEMANIWSEENKYRAWLEVEILSDE-----AWAELGEIPKEDVALIRKKAD-----FDIDRILEIEQETRHDVV 71
Cdd:pfam00206 2 RFTvpADALMGIFTDRSRFNFRLGEEDIKGLaalkkAAAKANVILKEEAAAIIKALDevaeeGKLDDQFPLKVWQEGSGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 72 AFTRAVSETLGE-------ERKWVHYGLTSTDVVDTAYGYLYKQAN-DIIRRDLENFTNIIADKAKEHKFTIMMGRTHGV 143
Cdd:pfam00206 82 AVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 144 HAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG--AVGNFANIPPFVEEYVCDKLG------IRAQEISTQVLP 215
Cdd:pfam00206 162 DATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATSD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446533399 216 RDLHAEYFAVLASIATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRG 286
Cdd:pfam00206 242 RDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
4-375 |
8.29e-68 |
|
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: 222.19 E-value: 8.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 4 RYSRPEMANIWSEENKYRAWLEVEILSDEAWAELG-EIPKEDVALIRKKAD-FDIDRILEIEQETRHDVVAFTRAVSETL 81
Cdd:cd03302 4 RYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGlDISDEQIEEMKANVEnIDFEIAAAEEKKLRHDVMAHVHAFGLLC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 82 GEERKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEM 161
Cdd:cd03302 84 PAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 162 KRNIERFEHAAAGVEAGKISGAVGNFANippFVE-------------EYVCDKLGI-RAQEISTQVLPRDLHAEYFAVLA 227
Cdd:cd03302 164 LMDLRNLERLRDDLRFRGVKGTTGTQAS---FLDlfegdhdkvealdELVTKKAGFkKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 228 SIATSIERMATEIRGLQKSEqrEVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVAL-WHERDISHS 306
Cdd:cd03302 241 SLGATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTqWFERTLDDS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446533399 307 SAERIITPDTTILIDYMLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKGMTREQAYDLV 375
Cdd:cd03302 319 ANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERI 387
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
72-327 |
2.67e-58 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 190.90 E-value: 2.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 72 AFTRAVSETLGEER--KWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTT 149
Cdd:cd01594 19 VLAGRAGELAGGLHgsALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 150 FGLKLATWYSEMKRNIERFEHAAagveagkisgavgnfanippfveeyvcdklgiraqeistqvlprdlHAEYFAVLASI 229
Cdd:cd01594 99 LGYELRAWAQVLGRDLERLEEAA----------------------------------------------VAEALDALALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 230 ATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSSAE 309
Cdd:cd01594 133 AAHLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSM 212
|
250
....*....|....*...
gi 446533399 310 RIITPDTTILIDYMLNRF 327
Cdd:cd01594 213 REILADSLLLLIDALRLL 230
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
5-417 |
1.61e-54 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 187.53 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 5 YSRPEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIR---KKADFDIDRI---------LEIEQetrhdVVA 72
Cdd:PRK09053 12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEaacDAERLDLDALaqaaalagnLAIPL-----VKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 73 FTRAVSETLGEERKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGL 152
Cdd:PRK09053 87 LTAQVAARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 153 KLATWYSEMKRNIERFEHAAAGVEAGKISGAVGNFANI----PPFVEEYVCD-KLGIRAQEISTQvlpRDLHAEYFAVLA 227
Cdd:PRK09053 167 KFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqaLPVAQALAAElQLALPALPWHTQ---RDRIAEFASALG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 228 SIATSIERMATEIRGLQKSEQREVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHERDISHSS 307
Cdd:PRK09053 244 LLAGTLGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 308 AERIITPDTTILIDYMLNRFGNIVKNLTVFPENMIRNMNSTFGLIFSQRAMLTLIEKgMTREQAYDLVQPKTAYSWDNQV 387
Cdd:PRK09053 324 AEWDTLPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADR-IGRLDAHHLVEQASKRAVAEGR 402
|
410 420 430
....*....|....*....|....*....|
gi 446533399 388 DFKPLLEADSEVTSRLTQEEIDEIFNPVYY 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 |
2.22e-45 |
|
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: 160.30 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 5 YSRPEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKE---DVALIRKKADFDIDrilEIEQETRHD---VVAFTRAVS 78
Cdd:TIGR02426 6 FGDPAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEaaaAIEAACAAAAPDLE---ALAHAAATAgnpVIPLVKALR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 79 ETLGEE-RKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATW 157
Cdd:TIGR02426 83 KAVAGEaARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 158 YSEMKRNIERFEHAAAGVEAGKISGAVGNFANIPPF---VEEYVCDKLGIRAQEISTQVLpRDLHAEYFAVLASIATSIE 234
Cdd:TIGR02426 163 LAAVLRARDRLAALRTRALPLQFGGAAGTLAALGTRggaVAAALAARLGLPLPALPWHTQ-RDRIAEFGSALALVAGALG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446533399 235 RMATEIRGLQKSEqreVEEFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITAYENVALWHER 301
Cdd:TIGR02426 242 KIAGDIALLSQTE---VGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHER 305
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
4-276 |
2.21e-40 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 149.52 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 4 RYSR--PEMANIWSEE--NKYRAWLEVE---ILSDEAwaELGEIP---KEDVALIRK-KADF---DIDRILEIEQETRHD 69
Cdd:PRK09285 15 RYASktAALRPIFSEFglIRYRVQVEVEwliALAAHP--GIPEVPpfsAEANAFLRAiVENFseeDAARIKEIERTTNHD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 70 VVA---FTRAVSETLGEERK---WVHYGLTSTDVVDTAYGYLYKQA-NDIIRRDLENFTNIIADKAKEHKFTIMMGRTHG 142
Cdd:PRK09285 93 VKAveyFLKEKLAGLPELEAvseFIHFACTSEDINNLSHALMLKEArEEVLLPALRELIDALKELAHEYADVPMLSRTHG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 143 VHAEPTTFGLKLATWYSEMKRNIERFEHaaagVE-AGKISGAVGNFA---------NIPPFVEEYVCdKLGIRAQEISTQ 212
Cdd:PRK09285 173 QPATPTTLGKEMANVAYRLERQLKQLEA----VEiLGKINGAVGNYNahlaaypevDWHAFSREFVE-SLGLTWNPYTTQ 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446533399 213 VLPRDLHAEYFAVLASIATSIERMATEIRGL-------QKSEQREVeeffakgqkGSSAMPHKRNPIGSEN 276
Cdd:PRK09285 248 IEPHDYIAELFDAVARFNTILIDLDRDVWGYislgyfkQKTKAGEI---------GSSTMPHKVNPIDFEN 309
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
11-310 |
3.17e-40 |
|
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: 148.54 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 11 ANIWSEE--NKYRAWLEVE---ILSDEAwaELGEIP---KEDVALIRKKA-DF---DIDRILEIEQETRHDVVA---FTR 75
Cdd:cd01598 2 RPYFSEYalIKYRVQVEVEwliALSNLE--EIPEVPpltKEELKFLRAIIeNFseeDALRIKEIEATTNHDVKAveyFLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 76 AVSETLGEERK---WVHYGLTSTDVVDTAYGYLYKQA-NDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFG 151
Cdd:cd01598 80 EKFETLGLLKKikeFIHFACTSEDINNLAYALMIKEArNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 152 LKLATWYSEMKRNIERFEHAaagVEAGKISGAVGNFA---------NIPPFVEEYVcDKLGIRAQEISTQVLPRDLHAEY 222
Cdd:cd01598 160 KELAVFVYRLERQYKQLKQI---EILGKFNGAVGNFNahlvaypdvDWRKFSEFFV-TSLGLTWNPYTTQIEPHDYIAEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 223 FAVLASIATSIERMATEIRGL-------QKSEQREVeeffakgqkGSSAMPHKRNPIGSENMTG---LARVIRGHMITAY 292
Cdd:cd01598 236 FDALARINTILIDLCRDIWGYislgyfkQKVKKGEV---------GSSTMPHKVNPIDFENAEGnlgLSNALLNHLSAKL 306
|
330
....*....|....*...
gi 446533399 293 EnVALWhERDISHSSAER 310
Cdd:cd01598 307 P-ISRL-QRDLTDSTVLR 322
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
350-429 |
2.05e-32 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 117.55 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 350 GLIFSQRAMLTLIEKGMTREQAYDLVQPKTAYSWDNQVDFKPLLEADSEVTSRLTQEEIDEIFNPVYYTKRVDDIFERLG 429
Cdd:smart00998 2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
8-282 |
1.37e-24 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 103.98 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 8 PEMANIWSEENKYRAWLEVEILSDEAWAELGEIPKEDVALIRKK-ADFDIDrILEIEQETRHD---VVAFTRAVSETLGE 83
Cdd:PRK05975 18 DEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIAAAcETFEPD-LAALRHATARDgvvVPALVRQLRAAVGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 84 E-RKWVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMK 162
Cdd:PRK05975 97 EaAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 163 RNIERFEHAAAGVEAGKISGAVGNFANI---PPFVEEYVCDKLGI--RAQEISTqvlpRDLHAEYFAVLASIATSIERMA 237
Cdd:PRK05975 177 RHRDRLEALRADVFPLQFGGAAGTLEKLggkAAAVRARLAKRLGLedAPQWHSQ----RDFIADFAHLLSLVTGSLGKFG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446533399 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 |
1.30e-23 |
|
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: 93.63 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 350 GLIFSQRAMLTLIeKGMTREQAYDLVQPKTAYSWD-NQVDFKPLLEADSEVTsRLTQEEIDEIFNPVYYTKRVDDIFERL 428
Cdd:pfam10397 1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEeGKNDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADEIVDRV 78
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
25-310 |
3.03e-22 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 98.66 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 25 EVEILSDEAWAELGEIpkedvalirkKADFDIDRILE---IEQETRHDVVA---FTRAVSETLGEERK---WVHYGLTST 95
Cdd:PLN02848 58 EVPPFSDEANSFLEGI----------IAGFSVDDALEvkkIERVTNHDVKAveyFLKQKCKSHPELAKvleFFHFACTSE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 96 DVVDTAYGYLYKQA-NDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRniERFEHAAAG 174
Cdd:PLN02848 128 DINNLSHALMLKEGvNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSR--QRKQLSEVK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 175 VEaGKISGAVGNF---------ANIPPFVEEYVCDkLGIRAQEISTQVLPRDLHAEYFAVLASIATSIERMATEIRG--- 242
Cdd:PLN02848 206 IK-GKFAGAVGNYnahmsaypeVDWPAVAEEFVTS-LGLTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWSyis 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446533399 243 LQKSEQREVeeffaKGQKGSSAMPHKRNPIGSENMTG---LARVIRGHMITAYEnVALWhERDISHSSAER 310
Cdd:PLN02848 284 LGYFKQITK-----AGEVGSSTMPHKVNPIDFENSEGnlgLANAELSHLSMKLP-ISRM-QRDLTDSTVLR 347
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
24-415 |
1.75e-20 |
|
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: 92.99 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 24 LEVEILSDEAWA----ELGEIPKEDVALIrkkadfdIDRILEIEQETRHDVVAFT-----------RAVSETLGEERKWV 88
Cdd:cd01359 9 FEEDIAGSIAHAvmlaEQGILTEEEAAKI-------LAGLAKIRAEIEAGAFELDpededihmaieRRLIERIGDVGGKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 89 HYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERF 168
Cdd:cd01359 82 HTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 169 EHAAAGVE---AGkiSGA-VGNFANIPPfveEYVCDKLG---IRAQEISTqVLPRDLHAEYFAVLASIATSIERMATEIR 241
Cdd:cd01359 162 ADAYKRVNvspLG--AGAlAGTTFPIDR---ERTAELLGfdgPTENSLDA-VSDRDFVLEFLSAAALLMVHLSRLAEDLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 242 gLQKSEQR---EVEEFFAkgqKGSSAMPHKRNPIGSENMTGLA-RVIrGH---MITAYENVALWHERDISHSSAERIITP 314
Cdd:cd01359 236 -LWSTQEFgfvELPDAYS---TGSSIMPQKKNPDVLELIRGKAgRVI-GAlagLLTTLKGLPLAYNKDLQEDKEPLFDAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 315 DTTILidyMLNRFGNIVKNLTVFPENMIRNMNSTFGLIfSQRAMLTLIEKGMTREQAYDLVQPKTAYSWDNQVDFKPLLE 394
Cdd:cd01359 311 DTLIA---SLRLLTGVISTLTVNPERMREAAEAGFSTA-TDLADYLVREKGVPFREAHHIVGRAVRLAEEKGKDLSDLTL 386
|
410 420
....*....|....*....|.
gi 446533399 395 ADSEVTSRLTQEEIDEIFNPV 415
Cdd:cd01359 387 AELQAISPLFEEDVREALDPE 407
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
28-271 |
1.04e-15 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 78.65 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 28 ILSDEAWA-ELGE---IPKEDVALIRK-----KADFDIDRI-LEIEQETRHDVVAftRAVSETLGEERKWVHYGLTSTDV 97
Cdd:PRK00855 37 IAGSIAHArMLAKqgiLSEEEAEKILAgldeiLEEIEAGKFeFSPELEDIHMAIE--ARLTERIGDVGGKLHTGRSRNDQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 98 VDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEH------- 170
Cdd:PRK00855 115 VATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDarkrvnr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 171 ----AAAGveAGKisgavgNFaNIPPfveEYVCDKLGI-RAQEISTQ-VLPRDLHAEYFAVLASIATSIERMATEIrglq 244
Cdd:PRK00855 195 splgSAAL--AGT------TF-PIDR---ERTAELLGFdGVTENSLDaVSDRDFALEFLSAASLLMVHLSRLAEEL---- 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 446533399 245 kseqreV----EEF--------FAkgqKGSSAMPHKRNP 271
Cdd:PRK00855 259 ------IlwssQEFgfvelpdaFS---TGSSIMPQKKNP 288
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
117-284 |
1.00e-10 |
|
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: 63.29 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 117 LENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG-AVGNFANIPP-FV 194
Cdd:cd01362 160 LKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGtAVGTGLNAHPgFA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 195 EEyVCDklgiraqEISTQV-LPRDLHAEYFAVLAS-------------IATSIERMATEIR--------GLQkseqrevE 252
Cdd:cd01362 240 EK-VAA-------ELAELTgLPFVTAPNKFEALAAhdalveasgalktLAVSLMKIANDIRwlgsgprcGLG-------E 304
|
170 180 190
....*....|....*....|....*....|...
gi 446533399 253 EFFAKGQKGSSAMPHKRNPIGSENMTGL-ARVI 284
Cdd:cd01362 305 LSLPENEPGSSIMPGKVNPTQCEALTMVaAQVM 337
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
117-284 |
2.33e-10 |
|
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: 62.06 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 117 LENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG-AVGNFANIPPFVE 195
Cdd:cd01596 159 LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGtAVGTGLNAPPGYA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 196 EYVCDKLgiraQEISTqvLP-------------RDLHAEYFAVLASIATSIERMATEIR--------GLQKSEQREVeef 254
Cdd:cd01596 239 EKVAAEL----AELTG--LPfvtapnlfeataaHDALVEVSGALKTLAVSLSKIANDLRllssgpraGLGEINLPAN--- 309
|
170 180 190
....*....|....*....|....*....|.
gi 446533399 255 fakgQKGSSAMPHKRNPIGSENMTGLA-RVI 284
Cdd:cd01596 310 ----QPGSSIMPGKVNPVIPEAVNMVAaQVI 336
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
35-284 |
4.58e-10 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 61.26 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 35 AELGEIPKEDVALIRKKADfdidRILEieqeTRHD----------------------VVAfTRAvSETLGEER---KWVH 89
Cdd:PRK00485 60 AELGLLDAEKADAIVAAAD----EVIA----GKHDdhfpldvwqtgsgtqsnmnvneVIA-NRA-SELLGGELgskKPVH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 90 ------YGLTSTDVVDTAygyLYKQANDIIRRDL----ENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYS 159
Cdd:PRK00485 130 pndhvnMSQSSNDTFPTA---MHIAAVLAIVERLlpalEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 160 EMKRNIERFEHAAAGVEAGKISG-AVGNFANIPP-FVEEyVCDKLgirAQEISTQVLPRDLHaeyFAVLAS--------- 228
Cdd:PRK00485 207 QLEHGIERIEAALPHLYELALGGtAVGTGLNAHPgFAER-VAEEL---AELTGLPFVTAPNK---FEALAAhdalveasg 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446533399 229 ----IATSIERMATEIRglqkseqreveeFFAKG-------------QKGSSAMPHKRNPIGSENMTGL-ARVI 284
Cdd:PRK00485 280 alktLAVSLMKIANDIR------------WLASGprcglgeislpenEPGSSIMPGKVNPTQCEALTMVcAQVM 341
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
124-278 |
9.47e-10 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 60.23 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 124 IADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG-AVGNFANIPPFVEEYVCDKL 202
Cdd:cd01357 166 FQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGtAIGTGINAPPGYIELVVEKL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 203 giraQEISTQVLPR-----------DLHAEYFAVLASIATSIERMATEIRgLQKSEQR---------EVeeffakgQKGS 262
Cdd:cd01357 246 ----SEITGLPLKRaenlidatqntDAFVEVSGALKRLAVKLSKIANDLR-LLSSGPRaglgeinlpAV-------QPGS 313
|
170
....*....|....*...
gi 446533399 263 SAMPHKRNPIGSE--NMT 278
Cdd:cd01357 314 SIMPGKVNPVIPEvvNQV 331
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
127-284 |
1.40e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 56.53 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 127 KAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG-AVGNFANIPPFVEEYVCDKLG-- 203
Cdd:PRK13353 174 KAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGtAVGTGLNADPEYIERVVKHLAai 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 204 -----IRAQEI--STQVLprDLHAEYFAVLASIATSIERMATEIRgLQKSEQRE-VEEFF--AKgQKGSSAMPHKRNPIG 273
Cdd:PRK13353 254 tglplVGAEDLvdATQNT--DAFVEVSGALKVCAVNLSKIANDLR-LLSSGPRTgLGEINlpAV-QPGSSIMPGKVNPVM 329
|
170
....*....|..
gi 446533399 274 SENMTGLA-RVI 284
Cdd:PRK13353 330 PEVVNQIAfQVI 341
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
14-286 |
2.54e-07 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 52.86 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 14 WSeenkyRAWLEVEILSDE-------AWAELGEIPKEDVALIRKKADFDIDRILEieqetrhdvvaftRAVSETLGEERK 86
Cdd:PRK12308 40 WS-----KALLSVGVLSEEeqqklelALNELKLEVMEDPEQILLSDAEDIHSWVE-------------QQLIGKVGDLGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 87 WVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFglklATW---YSEM-K 162
Cdd:PRK12308 102 KLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTF----AHWclaYVEMfE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 163 RNIERFEHAAAGVEAGKI-SGAVGNFANipPFVEEYVCDKLGIRAQEIST--QVLPRDLHAEYFAVlASIAT-SIERMAT 238
Cdd:PRK12308 178 RDYSRLEDALTRLDTCPLgSGALAGTAY--PIDREALAHNLGFRRATRNSldSVSDRDHVMELMSV-ASISMlHLSRLAE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446533399 239 EIRGLQKSEQREVeEFFAKGQKGSSAMPHKRNPIGSEnmtglarVIRG 286
Cdd:PRK12308 255 DLIFYNSGESGFI-ELADTVTSGSSLMPQKKNPDALE-------LIRG 294
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
117-288 |
3.54e-06 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 48.92 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 117 LENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG-AVGNFANIPP-FV 194
Cdd:PLN00134 156 LKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGtAVGTGLNTKKgFD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 195 EEYvcdklgirAQEISTQV-LPRDLHAEYFAVLAS-------------IATSIERMATEIR--------GLQKSEQREVE 252
Cdd:PLN00134 236 EKI--------AAAVAEETgLPFVTAPNKFEALAAhdafvelsgalntVAVSLMKIANDIRllgsgprcGLGELNLPENE 307
|
170 180 190
....*....|....*....|....*....|....*..
gi 446533399 253 effakgqKGSSAMPHKRNPIGSENMTGL-ARVIRGHM 288
Cdd:PLN00134 308 -------PGSSIMPGKVNPTQCEALTMVcAQVMGNHV 337
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
68-281 |
3.65e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 49.23 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 68 HDVVAfTRAVsETLGEERKWVHY---------GLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMG 138
Cdd:PRK14515 114 NEVIA-NRAL-ELLGMEKGDYHYispnshvnmAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 139 RTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGV-EAGKISGAVGNFANIPPFVEEYVCDKLG-------IRAQEIS 210
Cdd:PRK14515 192 RTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLyEVNMGATAVGTGLNADPEYIEAVVKHLAaiselplVGAEDLV 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446533399 211 TQVLPRDLHAEYFAVLASIATSIERMATEIRgLQKSEQRE--VEEFFAKGQKGSSAMPHKRNPIGSENMTGLA 281
Cdd:PRK14515 272 DATQNTDAYTEVSAALKVCMMNMSKIANDLR-LMASGPRVglAEIMLPARQPGSSIMPGKVNPVMPEVINQIA 343
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
117-290 |
4.24e-06 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 48.76 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 117 LENFTNIIADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKrNIERFEHAA--AGVEAGKISGAVGNFANIPP-F 193
Cdd:PRK12425 162 IAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLD-YAERAIRAAlpAVCELAQGGTAVGTGLNAPHgF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 194 VEEyvcdklgIRAQEISTQVLPRDLHAEYFAVLA-------------SIATSIERMATEIRGLQKSEQREVEEF-FAKGQ 259
Cdd:PRK12425 241 AEA-------IAAELAALSGLPFVTAPNKFAALAgheplvslsgalkTLAVALMKIANDLRLLGSGPRAGLAEVrLPANE 313
|
170 180 190
....*....|....*....|....*....|.
gi 446533399 260 KGSSAMPHKRNPIGSENMTGLARVIRGHMIT 290
Cdd:PRK12425 314 PGSSIMPGKVNPTQCEALSMLACQVMGNDAT 344
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
128-293 |
2.40e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 46.52 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 128 AKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISGAVGNFANIpPFVEEYVCDKLGIRA- 206
Cdd:PRK06705 150 AADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTTSF-PIKRERVADLLGFTNv 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 207 -QEISTQVLPRDLHAEYFAVLASIATSIERMATEIRGLQKSEQREVEefFAKGQ-KGSSAMPHKRNPIGSENMTGLARVI 284
Cdd:PRK06705 229 iENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGIT--VARPYvQISSIMPQKRNPVSIEHARAITSSA 306
|
....*....
gi 446533399 285 RGHMITAYE 293
Cdd:PRK06705 307 LGEAFTVFQ 315
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
124-271 |
5.23e-05 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 45.50 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 124 IADKAKEHKFTIMMGRTHGVHAEPTTFGLKLATWYSEMKRNIERFEHAAAGVEAGKISG-AVGNFANIPPFVEEYVCDKL 202
Cdd:PRK12273 173 FEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGAtAIGTGLNAPPGYIELVVEKL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 203 giraQEISTQ--VLPRDL---------HAEYFAVLASIATSIERMATEIRgLQKSEQR---------EVeeffakgQKGS 262
Cdd:PRK12273 253 ----AEITGLplVPAEDLieatqdtgaFVEVSGALKRLAVKLSKICNDLR-LLSSGPRaglneinlpAV-------QAGS 320
|
....*....
gi 446533399 263 SAMPHKRNP 271
Cdd:PRK12273 321 SIMPGKVNP 329
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
67-291 |
1.99e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 43.68 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 67 RHDVVAFTRAVSETLGEERK-WVHYGLTSTDVVDTAYGYLYKQANDIIRRDLENFTNIIADKAKEHKFTIMMGRTHGVHA 145
Cdd:PRK02186 488 RGLYMLYEAYLIERLGEDVGgVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533399 146 EPTTFGLKLATWYSEMKRNIERFEHAAAGVEA---GKISGAVGNFanipPFVEEYVCDKLGIRAQEIST--QVLPRDLHA 220
Cdd:PRK02186 568 LPGSLGHYLLAVDGALARETHALFALFEHIDVcplGAGAGGGTTF----PIDPEFVARLLGFEQPAPNSldAVASRDGVL 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446533399 221 EYFAVLASIATSIERMATEirgLQKSEQREVE--EFFAKGQKGSSAMPHKRNPIGSENMTGLARVIRGHMITA 291
Cdd:PRK02186 644 HFLSAMAAISTVLSRLAQD---LQLWTTREFAlvSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASA 713
|
|
| |
