|
Name |
Accession |
Description |
Interval |
E-value |
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
42-478 |
0e+00 |
|
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: 560.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 42 THGGGYAGPVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGA 121
Cdd:cd01597 1 LLGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATARTGHPAIPLVKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 122 LQRNCSPSAREYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVA 201
Cdd:cd01597 81 LTAACGDAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 202 GWIDELLRHRERLGEARKRILVVQLFGGVGTMAAFGDEAMLLLESFARRLSLDVPLAGWHVSRDRVTEFVSTLAMVTASL 281
Cdd:cd01597 161 VWLSELLRHRERLDELRPRVLVVQFGGAAGTLASLGDQGLAVQEALAAELGLGVPAIPWHTARDRIAELASFLALLTGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 282 ARIADEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAV 361
Cdd:cd01597 241 GKIARDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 362 ADVSHYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMAKQLGKSSAYEIIFEITQACQRKRIPMRQALE 441
Cdd:cd01597 321 PEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLL 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 15598712 442 SDPRVGAVMPKETLARLFEPRTHLGMAGTIVDKVLDK 478
Cdd:cd01597 401 EDPEVAAYLSDEELDALLDPANYLGSAPALVDRVLAR 437
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
47-475 |
1.16e-155 |
|
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: 449.15 E-value: 1.16e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 47 YAGPVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGALQRNC 126
Cdd:COG0015 6 YASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKETRHDVKAFVYALKEKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 127 SPSAREYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDE 206
Cdd:COG0015 86 GAEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 207 LLRHRERLGEARKRILVVQLFGGVGTMAAFGDEAMLLLESFARRLSLDV-PLAGWHVSRDRVTEFVSTLAMVTASLARIA 285
Cdd:COG0015 166 LLRQLERLEEARERVLVGKIGGAVGTYAAHGEAWPEVEERVAEKLGLKPnPVTTQIEPRDRHAELFSALALIAGSLEKIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 286 DEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAVADVS 365
Cdd:COG0015 246 RDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNILPDAF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 366 HYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMA-KQLGKSSAYEIIFEITQACQRKRIPMRQALESDP 444
Cdd:COG0015 326 LLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVrRGLGREEAYELVKELARGAWEEGNDLRELLAADP 405
|
410 420 430
....*....|....*....|....*....|.
gi 15598712 445 RVGAVMPKETLARLFEPRTHLGMAGTIVDKV 475
Cdd:COG0015 406 EIPAELSKEELEALFDPANYLGAADEIVDRV 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
53-424 |
2.44e-150 |
|
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: 433.47 E-value: 2.44e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 53 RRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGALQRNCSPSARE 132
Cdd:cd01595 2 RAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVFEIDAERIAEIEKETGHDVIAFVYALAEKCGEDAGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 133 YVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRE 212
Cdd:cd01595 82 YVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 213 RLGEARKRILVVQLFGGVGTMAAFGDEAMLLLESFARRLSLDVPLAGWHV-SRDRVTEFVSTLAMVTASLARIADEIRTL 291
Cdd:cd01595 162 RLEEARERVLVGGISGAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQIePRDRIAELLSALALIAGTLEKIATDIRLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 292 NRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAVADVSHYALMA 371
Cdd:cd01595 242 QRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15598712 372 LSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMAKQ-LGKSSAYEIIFE 424
Cdd:cd01595 322 LSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKgLGRQEAYELVKE 375
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
47-422 |
2.18e-103 |
|
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: 314.10 E-value: 2.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 47 YAGPVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARlsaVDLQQIADGVASTGHSLMPLLGALQRNC 126
Cdd:cd01360 2 YGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAK---FDVERVKEIEAETKHDVIAFVTAIAEYC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 127 SPSAReYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDE 206
Cdd:cd01360 79 GEAGR-YIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 207 LLRHRERLGEARKRILVVQLFGGVGTMAAFGDEamlLLESFARRLSLDV-PLAGWHVSRDRVTEFVSTLAMVTASLARIA 285
Cdd:cd01360 158 FKRHLERLKEARERILVGKISGAVGTYANLGPE---VEERVAEKLGLKPePISTQVIQRDRHAEYLSTLALIASTLEKIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 286 DEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAVADVS 365
Cdd:cd01360 235 TEIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDAT 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598712 366 HYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMA-KQLGKSSAYEII 422
Cdd:cd01360 315 ILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVeKGMSREEAYEIV 372
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
47-475 |
9.77e-103 |
|
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: 313.90 E-value: 9.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 47 YAGPVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGALQRNC 126
Cdd:TIGR00928 5 YGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYALKEKC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 127 sPSAREYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDE 206
Cdd:TIGR00928 85 -GAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 207 LLRHRERLGEARKRILVVQLFGGVGTMAAFGDEAMLLLESFARRLSLD-VPLAGWHVSRDRVTEFVSTLAMVTASLARIA 285
Cdd:TIGR00928 164 MLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVEEVEERVTEFLGLKpVPISTQIEPRDRHAELLDALALLATTLEKFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 286 DEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAVADVS 365
Cdd:TIGR00928 244 VDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILPDAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 366 HYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMAKQ-LGKSSAYEIIFEITQACQRKRIP-MRQALESD 443
Cdd:TIGR00928 324 ILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERgMGREEAYEIVRELAMGAAEVDEPdLLEFLLED 403
|
410 420 430
....*....|....*....|....*....|..
gi 15598712 444 PRVGAVMPKETLARLFEPRTHLGMAGTIVDKV 475
Cdd:TIGR00928 404 ERITKYLKEEELAELLDPETYIGNAGEIVERV 435
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
50-483 |
2.69e-101 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 310.79 E-value: 2.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 50 PVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGALQRNCS-- 127
Cdd:PRK09053 15 PAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALAGNLAIPLVKQLTAQVAar 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 128 -PSAREYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDE 206
Cdd:PRK09053 95 dAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 207 LLRHRERLGEARKRILVVQLFGGVGTMAAFGDEAMLLLESFARRLSLDVPLAGWHVSRDRVTEFVSTLAMVTASLARIAD 286
Cdd:PRK09053 175 LLRHRQRLAALRPRALVLQFGGAAGTLASLGEQALPVAQALAAELQLALPALPWHTQRDRIAEFASALGLLAGTLGKIAR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 287 EIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCeqVVVLARLAKAQVLLA--LDAMILEHERDYRGTRLEWCAVADV 364
Cdd:PRK09053 255 DVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGC--AAVLTAATRAPGLVAtlFAAMPQEHERALGGWHAEWDTLPEL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 365 SHYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMAKQLGKSSAYEIIFEITQACQRKRIPMRQALESDP 444
Cdd:PRK09053 333 ACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADRIGRLDAHHLVEQASKRAVAEGRHLRDVLAEDP 412
|
410 420 430
....*....|....*....|....*....|....*....
gi 15598712 445 RVGAVMPKETLARLFEPRTHLGMAGTIVDKVLDKVASHH 483
Cdd:PRK09053 413 QVSAHLSPAALDRLLDPAHYLGQAHAWVDRVLAEHASRH 451
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
62-385 |
1.93e-90 |
|
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: 278.62 E-value: 1.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 62 LQRWLDVEAALALAQADVGVIPPEAALEIAKAAR-LSAVDLQQIADGVASTGHSLMPLLGALQRNCSPSAREYVHFGATT 140
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDeILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 141 QDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKR 220
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 221 ILVVQLFGG-VGTMAAFGDEamlLLESFARRLSLDVPLA---GWHVSRDRVTEFVSTLAMVTASLARIADEIRTLNRWEI 296
Cdd:cd01334 161 LNVLPLGGGaVGTGANAPPI---DRERVAELLGFFGPAPnstQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 297 GELEVGWTQQqIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAVADVSHYALMALSLLT 376
Cdd:cd01334 238 GEVELPDAKQ-PGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLT 316
|
....*....
gi 15598712 377 DTIDGLTVH 385
Cdd:cd01334 317 GVLEGLEVN 325
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
45-382 |
1.51e-79 |
|
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: 251.20 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 45 GGYAG-PVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGALQ 123
Cdd:TIGR02426 3 DGLFGdPAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAAAAPDLEALAHAAATAGNPVIPLVKALR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 124 RNCSPSAREYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGW 203
Cdd:TIGR02426 83 KAVAGEAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 204 IDELLRHRERLGEARKRILVVQLFGGVGTMAAFGDEAMLLLESFARRLSLDVPLAGWHVSRDRVTEFVSTLAMVTASLAR 283
Cdd:TIGR02426 163 LAAVLRARDRLAALRTRALPLQFGGAAGTLAALGTRGGAVAAALAARLGLPLPALPWHTQRDRIAEFGSALALVAGALGK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 284 IADEIRTLNRWEIGELEVGwtqQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEWCAVAD 363
Cdd:TIGR02426 243 IAGDIALLSQTEVGEVFEA---GGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPE 319
|
330
....*....|....*....
gi 15598712 364 VSHYALMALSLLTDTIDGL 382
Cdd:TIGR02426 320 LVRLTGGALRQAQVLAEGL 338
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
273-466 |
1.09e-55 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 184.85 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 273 TLAMVTASLARIADEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYR 352
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 353 GTRLEWCAVADVSHYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMA-KQLGKSSAYEIIFEITQACQR 431
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVeKGMGREEAHELIREKAMEAWK 181
|
170 180 190
....*....|....*....|....*....|....*
gi 15598712 432 KRIPMRQALESDPRVGAVMPKETLARLFEPRTHLG 466
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
66-358 |
7.71e-52 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 179.09 E-value: 7.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 66 LDVEAALALAQADVGVIPPEAALEIAKAARLSAVDLQQIADGVASTGHSLMPLLGALQRNCSPSAREYVHFGATTQDIQD 145
Cdd:PRK05975 34 LAFEAALAEAEAEHGIIPAEAAERIAAACETFEPDLAALRHATARDGVVVPALVRQLRAAVGEEAAAHVHFGATSQDVID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 146 TAQSLEMRDVLDETERALDILLDRLSVLASGT-RNALMvARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKRILVV 224
Cdd:PRK05975 114 TSLMLRLKAASEILAARLGALIARLDALEATFgQNALM-GHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRADVFPL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 225 QLFGGVGTMAAFGDEAMLLLESFARRLSLdVPLAGWHVSRDRVTEFVSTLAMVTASLARIADEIRTL--NRWEIGELEVG 302
Cdd:PRK05975 193 QFGGAAGTLEKLGGKAAAVRARLAKRLGL-EDAPQWHSQRDFIADFAHLLSLVTGSLGKFGQDIALMaqAGDEISLSGGG 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598712 303 wtqqqiGSSTMPHKRNPEGCEQVVVLARLAKAQVLLALDAMILEHERDYRGTRLEW 358
Cdd:PRK05975 272 ------GSSAMPHKQNPVAAETLVTLARFNATQVSGLHQALVHEQERSGAAWTLEW 321
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
45-337 |
6.48e-44 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 156.76 E-value: 6.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 45 GGYAGPVSRR--IFCSHCRLQRWLDVE-----AALALAQADVGVIPPEAALEIAKAAR-----LSAVDLQQIADGVASTG 112
Cdd:pfam00206 1 GRFTVPADALmgIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKALDevaeeGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 113 HS----LMPLLGALQrNCSPSAREYVHFGATTQDIQDTAQSLEMRDVLDET-ERALDILLDRLSVLASGTRNALMVARTH 187
Cdd:pfam00206 81 TAvnmnLNEVIGELL-GQLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVlLPALRQLIDALKEKAKEFADIVKPGRTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 188 SIPALPTTFGLKVAGWIDELLRHRERLGEARKRILVVQLFGGVGTMAAFG---DEAMLLLESFARRLSLDVPLAGWHV-- 262
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNadpEFAELVAKELGFFTGLPVKAPNSFEat 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598712 263 -SRDRVTEFVSTLAMVTASLARIADEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEqvvvLARLAKAQVL 337
Cdd:pfam00206 240 sDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLE----LLTGKAGRVM 311
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
105-376 |
2.09e-37 |
|
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: 136.97 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 105 ADGVASTGHSLMPLLGALQRNCSPSAREY-----VHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRN 179
Cdd:cd01594 3 ADLLVELAAALALVEEVLAGRAGELAGGLhgsalVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 180 ALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARkrilvvqlfggvgtmaafgdeamlllesfarrlsldvplag 259
Cdd:cd01594 83 TVMPGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA----------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 260 whvsrdrVTEFVSTLAMVTASLARIADEIRTLNRWEIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARLAKAQVLLA 339
Cdd:cd01594 122 -------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAV 194
|
250 260 270
....*....|....*....|....*....|....*..
gi 15598712 340 LDAMILEHERDYRGTRLEWCAVADVSHYALMALSLLT 376
Cdd:cd01594 195 LTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
47-428 |
1.17e-32 |
|
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: 128.97 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 47 YAGPVSRRIFCSHCRLQRWLDVEAALALAQADVGVIPPEAALEIAKAaRLSAVDLQQIADGVASTGHSLMPLLGALQRNC 126
Cdd:cd03302 5 YASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKA-NVENIDFEIAAAEEKKLRHDVMAHVHAFGLLC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 127 sPSAREYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDE 206
Cdd:cd03302 84 -PAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 207 LLRHRERLGEARKRILVVQLFGGVGTMAAF-----GDEAML--LLESFARRLSLD--VPLAGWHVSRDRVTEFVSTLAMV 277
Cdd:cd03302 163 LLMDLRNLERLRDDLRFRGVKGTTGTQASFldlfeGDHDKVeaLDELVTKKAGFKkvYPVTGQTYSRKVDIDVLNALSSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 278 TASLARIADEIRTLNRWEigELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLARlakaqVLLALDAMILE------HER-- 349
Cdd:cd03302 243 GATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLAR-----HLMNLASNAAQtastqwFERtl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 350 -DYRGTRLewcAVADVSHYALMALSLLTDTIDGLTVHDETMARTANAYSDAICTEAFVFEMAKQ-LGKSSAYEIIFEITQ 427
Cdd:cd03302 316 dDSANRRI---AIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAgGDRQDAHERIRVLSH 392
|
.
gi 15598712 428 A 428
Cdd:cd03302 393 Q 393
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
71-463 |
1.88e-19 |
|
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: 90.30 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 71 ALALAQAdvGVIPPEAALEIAKAarlsavdLQQIADGVASTGHSL--------MPLLGALQRNCSPSAReYVHFGATTQD 142
Cdd:cd01359 20 AVMLAEQ--GILTEEEAAKILAG-------LAKIRAEIEAGAFELdpededihMAIERRLIERIGDVGG-KLHTGRSRND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 143 IQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKRIL 222
Cdd:cd01359 90 QVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 223 VVQLFGGVGTMAAFG-DEAML--LLEsFAR--RLSLDvplAGWhvSRDRVTEFVSTLAMVTASLARIADEIRTLNRWEIG 297
Cdd:cd01359 170 VSPLGAGALAGTTFPiDRERTaeLLG-FDGptENSLD---AVS--DRDFVLEFLSAAALLMVHLSRLAEDLILWSTQEFG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 298 ELEV--GWTQqqiGSSTMPHKRNPEGCEqvvvLARLAKAQV---LLALDAMILEHERDYRGTRLE-WCAVADVSHYALMA 371
Cdd:cd01359 244 FVELpdAYST---GSSIMPQKKNPDVLE----LIRGKAGRVigaLAGLLTTLKGLPLAYNKDLQEdKEPLFDAVDTLIAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 372 LSLLTDTIDGLTVHDETMARTANA-YSDAicTE-AFVFEMAKQLGKSSAYEIIFEITQACQRKRIPMRQALESDPRVGAV 449
Cdd:cd01359 317 LRLLTGVISTLTVNPERMREAAEAgFSTA--TDlADYLVREKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISP 394
|
410
....*....|....
gi 15598712 450 MPKETLARLFEPRT 463
Cdd:cd01359 395 LFEEDVREALDPEN 408
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
45-319 |
1.61e-17 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 84.80 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 45 GGYAGPVS--RRIFcS-----HCRLQ---RWLdveAALAlAQADVGVIPPEAALEIAK----AARLSAVDLQQIADGVAS 110
Cdd:PRK09285 14 GRYASKTAalRPIF-SefgliRYRVQvevEWL---IALA-AHPGIPEVPPFSAEANAFlraiVENFSEEDAARIKEIERT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 111 TGHSL----------MPLLGALQRncspsAREYVHFGATTQDIQDTAQSLEMRDVLDETER-ALDILLDRLSVLASGTRN 179
Cdd:PRK09285 89 TNHDVkaveyflkekLAGLPELEA-----VSEFIHFACTSEDINNLSHALMLKEAREEVLLpALRELIDALKELAHEYAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 180 ALMVARTHSIPALPTTFGlKvagwidELLRHRERLGEARKRILVVQL---FGG-VGTMAAfgdeamlllESFArrlsldV 255
Cdd:PRK09285 164 VPMLSRTHGQPATPTTLG-K------EMANVAYRLERQLKQLEAVEIlgkINGaVGNYNA---------HLAA------Y 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 256 PLAGWH-VSRdrvtEFVSTL-----------------AMVTASLARIADEIRTLNR--WeiGELEVGWTQQQ-----IGS 310
Cdd:PRK09285 222 PEVDWHaFSR----EFVESLgltwnpyttqiephdyiAELFDAVARFNTILIDLDRdvW--GYISLGYFKQKtkageIGS 295
|
....*....
gi 15598712 311 STMPHKRNP 319
Cdd:PRK09285 296 STMPHKVNP 304
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
64-319 |
9.26e-17 |
|
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: 82.28 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 64 RWLdveaaLALAQAD-VGVIPPEAALEIAKAARL----SAVDLQQIADGVASTGH-------------SLMPLLGALqrn 125
Cdd:cd01598 20 EWL-----IALSNLEeIPEVPPLTKEELKFLRAIienfSEEDALRIKEIEATTNHdvkaveyflkekfETLGLLKKI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 126 cspsaREYVHFGATTQDIQDTAQSLEMRDVLDET-ERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWI 204
Cdd:cd01598 92 -----KEFIHFACTSEDINNLAYALMIKEARNEViLPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 205 dellrhrERLGEARKRILVVQL---FGG-VGTMAA------------FGDEamlllesFARRLSLDV-PLAGWHVSRDRV 267
Cdd:cd01598 167 -------YRLERQYKQLKQIEIlgkFNGaVGNFNAhlvaypdvdwrkFSEF-------FVTSLGLTWnPYTTQIEPHDYI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598712 268 TEFVSTlamvtasLARIADEIRTLNR--WeiGELEVGWTQQ-----QIGSSTMPHKRNP 319
Cdd:cd01598 233 AELFDA-------LARINTILIDLCRdiW--GYISLGYFKQkvkkgEVGSSTMPHKVNP 282
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
71-399 |
9.88e-16 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 79.37 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 71 ALALAQADVGVIPPEAALEIAKAarlsavdLQQIADGVAStghslmpllGALQRNcspSAREYVHF----------GAT- 139
Cdd:COG0165 41 AHARMLAEQGIISAEEAAAILAG-------LDEIEAEIEA---------GAFEFD---PELEDIHMnierrlieriGDVg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 140 ----T----QDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHR 211
Cdd:COG0165 102 gklhTgrsrNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLRDR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 212 ERLGEARKRILVVQLfgGVGTMA--AFG-DEAMLllesfARRL--------SLDVplagwhVS-RDRVTEFVSTLAMVTA 279
Cdd:COG0165 182 ERLADAYKRLNVSPL--GAAALAgtTFPiDRERT-----AELLgfdgptenSLDA------VSdRDFALEFLSAASLIMV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 280 SLARIADEIRTLNRWEIG--ELEVGWTQqqiGSSTMPHKRNPEGCEqvvvLARlAKA-QVLLALDAMI-------LEH-- 347
Cdd:COG0165 249 HLSRLAEELILWSSSEFGfvELPDAFST---GSSIMPQKKNPDVAE----LIR-GKTgRVIGNLTGLLttmkglpLAYnk 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15598712 348 --ERDYRGtrlewcaVADVSHYALMALSLLTDTIDGLTVHDETMARTANA-YSDA 399
Cdd:COG0165 321 dlQEDKEP-------LFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAgFSTA 368
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
400-476 |
2.25e-14 |
|
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: 68.25 E-value: 2.25e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598712 400 ICTEAFVFEMA-KQLGKSSAYEIIFEITQACQRKRIPMRQALESDPRVGAVMPKETLARLFEPRTHLGMAGTIVDKVL 476
Cdd:smart00998 4 IFSERVLLALVeKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
150-334 |
1.10e-12 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 69.80 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 150 LEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKRILVVQLfgg 229
Cdd:PRK00855 121 LYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPL--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 230 vGTMAAFG-----DEAMLllesfARRL--------SLDVplagwhVS-RDRVTEFVSTLAMVTASLARIADEIrtlnrwe 295
Cdd:PRK00855 198 -GSAALAGttfpiDRERT-----AELLgfdgvtenSLDA------VSdRDFALEFLSAASLLMVHLSRLAEEL------- 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598712 296 igeleVGWTQQQI-----------GSSTMPHKRNPEGCEqvvvLARlAKA 334
Cdd:PRK00855 259 -----ILWSSQEFgfvelpdafstGSSIMPQKKNPDVAE----LIR-GKT 298
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
68-325 |
2.94e-12 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 68.47 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 68 VEAALALAQADVGVIPPEAALEIAKAAR-LSAVDL--QQIAD---GVASTGHSL----------MPLLGAlqrncSPSAR 131
Cdd:PRK13353 52 VKKAAALANADLGLLPRRIAEAIVQACDeILAGKLhdQFIVDpiqGGAGTSTNMnanevianraLELLGG-----EKGDY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 132 EYVH------FGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWID 205
Cdd:PRK13353 127 HYVSpndhvnMAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYAR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 206 ELLRHRERLGEARKRILVVQLfGG--VGTMAAFGDEAMLLLESFARRLSlDVPLAG--------WHVsrDRVTEFVSTLA 275
Cdd:PRK13353 207 ALKRDRKRIQQAREHLYEVNL-GGtaVGTGLNADPEYIERVVKHLAAIT-GLPLVGaedlvdatQNT--DAFVEVSGALK 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15598712 276 MVTASLARIADEIRTLN---RWEIGELEVgwTQQQIGSSTMPHKRNPEGCEQV 325
Cdd:PRK13353 283 VCAVNLSKIANDLRLLSsgpRTGLGEINL--PAVQPGSSIMPGKVNPVMPEVV 333
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
132-319 |
4.25e-12 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 67.84 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 132 EYVHFGATTQDIQDTAQSLEMRDVLDE-TERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIdellrh 210
Cdd:PLN02848 118 EFFHFACTSEDINNLSHALMLKEGVNSvVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFA------ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 211 rERLGEARKRILVVQLF----GGVGT----MAAFgdeamlllesfarrlsldvPLAGW-HVSRdrvtEFVSTLAM----- 276
Cdd:PLN02848 192 -YRLSRQRKQLSEVKIKgkfaGAVGNynahMSAY-------------------PEVDWpAVAE----EFVTSLGLtfnpy 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598712 277 VTA-----SLARIADEIRTLNR---------WeiGELEVGWTQQ-----QIGSSTMPHKRNP 319
Cdd:PLN02848 248 VTQiephdYMAELFNAVSRFNNilidfdrdiW--SYISLGYFKQitkagEVGSSTMPHKVNP 307
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
400-475 |
1.88e-11 |
|
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: 59.74 E-value: 1.88e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598712 400 ICTEAFVFEMAKQLGKSSAYEIIFEITQACQRK-RIPMRQALESDPRVgAVMPKETLARLFEPRTHLGMAGTIVDKV 475
Cdd:pfam10397 3 IFSERVLLALVKGLGREEAHELVQEAAMKAWEEgKNDLRELLAADPEV-TYLSEEELDALFDPAYYLGRADEIVDRV 78
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
67-436 |
1.69e-10 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 63.26 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 67 DVEAALALAQA--DVGVIPPE------AALEIAKAARLSavDLQQIADGVASTGHS-----LMPLLGALQRNcspsarey 133
Cdd:PRK12308 33 DIVGSIAWSKAllSVGVLSEEeqqkleLALNELKLEVME--DPEQILLSDAEDIHSwveqqLIGKVGDLGKK-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 134 VHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRER 213
Cdd:PRK12308 103 LHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 214 LGEARKRILVVQLFGG--VGTMAAFGDEAMLLLESFAR--RLSLDvplagwHVS-RDRVTEFVSTLAMVTASLARIADEI 288
Cdd:PRK12308 183 LEDALTRLDTCPLGSGalAGTAYPIDREALAHNLGFRRatRNSLD------SVSdRDHVMELMSVASISMLHLSRLAEDL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 289 RTLNRWEIGELEVGWTQQQiGSSTMPHKRNPEGCEqvvvLARLAKAQVLLALDAMI-------LEHERDYRGTRlEWCAV 361
Cdd:PRK12308 257 IFYNSGESGFIELADTVTS-GSSLMPQKKNPDALE----LIRGKTGRVYGALAGMMmtvkalpLAYNKDMQEDK-EGLFD 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598712 362 ADVSHYALMALSLLtdTIDGLTV-HDETMARTANAYSDAicTEAFVFEMAKQLGKSSAYEIIFEITQACQRKRIPM 436
Cdd:PRK12308 331 ALDTWNDCMEMAAL--CFDGIKVnGERTLEAAKQGYANA--TELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
68-336 |
3.95e-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: 61.67 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 68 VEAALALAQADVGVIPPEAALEIAKAArlsavdlQQIADG---------VASTG---HSLM-----------PLLGAlqr 124
Cdd:cd01596 47 VKKAAALANAELGLLDEEKADAIVQAC-------DEVIAGklddqfpldVWQTGsgtSTNMnvnevianralELLGG--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 125 ncSPSAREYVH------FGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGL 198
Cdd:cd01596 117 --KKGKYPVHPnddvnnSQSSNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 199 KVAGWIDELLRHRERLGEARKRILVVQLfGG--VGTM----AAFGdeamlllESFARRLS----LDVPLAGWHV----SR 264
Cdd:cd01596 195 EFSGYAAQLARDIARIEAALERLRELNL-GGtaVGTGlnapPGYA-------EKVAAELAeltgLPFVTAPNLFeataAH 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598712 265 DRVTEFVSTLAMVTASLARIADEIRTLN---RWEIGELEVgwTQQQIGSSTMPHKRNPEGCEQVVVLArlakAQV 336
Cdd:cd01596 267 DALVEVSGALKTLAVSLSKIANDLRLLSsgpRAGLGEINL--PANQPGSSIMPGKVNPVIPEAVNMVA----AQV 335
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
162-344 |
1.03e-09 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 60.49 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 162 ALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKRILVVQLfGG--VGT----MAA 235
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELAL-GGtaVGTglnaHPG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 236 FGDEamlllesFARRLS--LDVP----------LAgwhvSRDRVTEFVSTLAMVTASLARIADEIRTLN---RWEIGELE 300
Cdd:PRK00485 242 FAER-------VAEELAelTGLPfvtapnkfeaLA----AHDALVEASGALKTLAVSLMKIANDIRWLAsgpRCGLGEIS 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598712 301 VgwTQQQIGSSTMPHKRNPEGCEQVVVLArlakAQVlLALDAMI 344
Cdd:PRK00485 311 L--PENEPGSSIMPGKVNPTQCEALTMVC----AQV-MGNDAAV 347
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
68-336 |
3.71e-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: 58.67 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 68 VEAALALAQADVGVIPPEAALEIAKAArlsavdlQQIADG---------VASTG---HSLM-----------PLLGALQR 124
Cdd:cd01362 47 LKKAAAQANAELGLLDEEKADAIVQAA-------DEVIAGklddhfplvVWQTGsgtQTNMnvnevianraiELLGGVLG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 125 NCSP-SAREYVHFGATTQDIQDTA----QSLEMRDVLdetERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLK 199
Cdd:cd01362 120 SKKPvHPNDHVNMSQSSNDTFPTAmhiaAALALQERL---LPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 200 VAGWIDELLRHRERLGEARKRILVVQLFG-----GVGTMAAFGdeamlllESFARRLS---------LDVPLAGwHVSRD 265
Cdd:cd01362 197 FSGYAAQLEHAIARIEAALPRLYELALGGtavgtGLNAHPGFA-------EKVAAELAeltglpfvtAPNKFEA-LAAHD 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598712 266 RVTEFVSTLAMVTASLARIADEIRTLN---RWEIGELEVgwTQQQIGSSTMPHKRNPEGCEQVVVLArlakAQV 336
Cdd:cd01362 269 ALVEASGALKTLAVSLMKIANDIRWLGsgpRCGLGELSL--PENEPGSSIMPGKVNPTQCEALTMVA----AQV 336
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
62-458 |
8.12e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 58.32 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 62 LQRWLDVEAALALAQADVGVIPPEAALEIAKA-ARLSAVDLQQIADGVASTGhSLMPLLGALQRNCSPSAREYVHFGATT 140
Cdd:PRK02186 438 LDHLAAIDEAHLVMLGDTGIVAPERARPLLDAhRRLRDAGFAPLLARPAPRG-LYMLYEAYLIERLGEDVGGVLQTARSR 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 141 QDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKR 220
Cdd:PRK02186 517 NDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEH 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 221 ILVVQLFGGVGTMAAF----GDEAMLLleSFARRL--SLDVPlagwhVSRDRVTEFVSTLAMVTASLARIADEirtLNRW 294
Cdd:PRK02186 597 IDVCPLGAGAGGGTTFpidpEFVARLL--GFEQPApnSLDAV-----ASRDGVLHFLSAMAAISTVLSRLAQD---LQLW 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 295 EIGELEVGWTQQQI--GSSTMPHKRNPEGCEQVVV-LARLAKAQVLLALDAMILEHERDYRGTRLEWCAVADVSHYALMA 371
Cdd:PRK02186 667 TTREFALVSLPDALtgGSSMLPQKKNPFLLEFVKGrAGVVAGALASASAALGKTPFSNSFEAGSPMNGPIAQACAAIEDA 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 372 LSLLTDTIDGLTVHDETM---ARTANAYSDAICTEAFVFEMAKqlGKSSAYEIIFEITQACQRKRIPMRQALESDPRVGA 448
Cdd:PRK02186 747 AAVLVLLIDGLEADQARMrahLEDGGVSATAVAESLVVRRSIS--FRSAHTQVGQAIRQSLDQGRSSADALAALDPQFVS 824
|
410
....*....|
gi 15598712 449 VMPKETLARL 458
Cdd:PRK02186 825 RAPLEWARSH 834
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
68-325 |
1.03e-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: 57.15 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 68 VEAALALAQADVGVIPPEAALEIAKAARLSA---------VDLQQiadGVAST------------------GHSLmpllG 120
Cdd:cd01357 47 VKKAAALANAELGLLDEEKAEAIVKACDEIIagklhdqfvVDVIQ---GGAGTstnmnanevianralellGHEK----G 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 121 ALQRnCSPSarEYVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKV 200
Cdd:cd01357 120 EYQY-VHPN--DHVNMSQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 201 AGWIDELLRHRERLGEARKRILVVQLfGG--VGTMAAFGDEAMLLLESFARRLSlDVPLAGwhvSRDRV--TEFVSTLAM 276
Cdd:cd01357 197 GAYATALKRDRARIYKARERLREVNL-GGtaIGTGINAPPGYIELVVEKLSEIT-GLPLKR---AENLIdaTQNTDAFVE 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598712 277 VTASLAR-------IADEIRTLN---RWEIGELEVgwTQQQIGSSTMPHKRNPEGCEQV 325
Cdd:cd01357 272 VSGALKRlavklskIANDLRLLSsgpRAGLGEINL--PAVQPGSSIMPGKVNPVIPEVV 328
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
170-323 |
5.15e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 51.91 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 170 LSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKRILVVQLFGGV--GTMAAFGDEAMLLLESF 247
Cdd:PRK04833 139 LVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGAlaGTAYEIDREQLAGWLGF 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598712 248 AR--RLSLDVplagwhVS-RDRVTEFVSTLAMVTASLARIADEIRTLNRWEIGELEVGWTQQQiGSSTMPHKRNPEGCE 323
Cdd:PRK04833 219 ASatRNSLDS------VSdRDHVLELLSDASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTS-GSSLMPQKKNPDALE 290
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
68-319 |
9.55e-06 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 48.07 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 68 VEAALALAQADVGVIPPEAALEIAKAArlsavdlQQIADGVASTGHSLMPLLGALQRNCSPSARE--------------- 132
Cdd:PRK14515 58 VKKAAALANTDVGRLELNKGGAIAEAA-------QEILDGKWHDHFIVDPIQGGAGTSMNMNANEvianralellgmekg 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 133 ---------YVHFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGW 203
Cdd:PRK14515 131 dyhyispnsHVNMAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 204 IDELLRHRERLGEARKRILVVQLFG-GVGTMAAFGDEamlLLESFARRLS--LDVPLAGW-HV-----SRDRVTEFVSTL 274
Cdd:PRK14515 211 SRVLERDMKRIQQSRQHLYEVNMGAtAVGTGLNADPE---YIEAVVKHLAaiSELPLVGAeDLvdatqNTDAYTEVSAAL 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15598712 275 AMVTASLARIADEIRTLNRW-EIGELEVGWTQQQIGSSTMPHKRNP 319
Cdd:PRK14515 288 KVCMMNMSKIANDLRLMASGpRVGLAEIMLPARQPGSSIMPGKVNP 333
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
156-319 |
1.06e-05 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 47.81 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 156 LDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERLGEARKRILVVQLFG-----GV 230
Cdd:PRK12273 159 LRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGAtaigtGL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 231 GTMAAFGDEAMLLLesfaRRLSlDVPLAGwhvSRDRV--TEFVSTLAMVTASLAR-------IADEIRTLN---RWEIGE 298
Cdd:PRK12273 239 NAPPGYIELVVEKL----AEIT-GLPLVP---AEDLIeaTQDTGAFVEVSGALKRlavklskICNDLRLLSsgpRAGLNE 310
|
170 180
....*....|....*....|.
gi 15598712 299 LEVgwTQQQIGSSTMPHKRNP 319
Cdd:PRK12273 311 INL--PAVQAGSSIMPGKVNP 329
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
135-325 |
3.41e-05 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 46.26 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 135 HFGATTQDIQDTAQSLEMRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRERL 214
Cdd:PLN02646 118 HTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 215 GEARKRILVVQLfgGVGTMA--AFG-DEAMLllesfARRLSLDVPLAGW--HVS-RDRVTEFVSTLAMVTASLARIADEI 288
Cdd:PLN02646 198 VDCRPRVNFCPL--GSCALAgtGLPiDRFMT-----AKDLGFTAPMRNSidAVSdRDFVLEFLFANSITAIHLSRLGEEW 270
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598712 289 RTLNRWEIGELEVGwTQQQIGSSTMPHKRNPEGCEQV 325
Cdd:PLN02646 271 VLWASEEFGFVTPS-DAVSTGSSIMPQKKNPDPMELV 306
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
134-324 |
1.59e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 44.20 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 134 VHFGATTQDIQDTAQSLEMRD-VLDETERALdILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELLRHRE 212
Cdd:PRK06705 110 MHIGRSRNDMGVTMYRMSLRRyVLRLMEHHL-LLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 213 RLGEARKrilvvqlFGGVGTMAAfgdeAMLLLESFARRLSLDVPLAGW----HVSRDRVTEF-----VSTLAMVT-ASLA 282
Cdd:PRK06705 189 RMKKTYK-------LLNQSPMGA----AALSTTSFPIKRERVADLLGFtnviENSYDAVAGAdylleVSSLLMVMmTNTS 257
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598712 283 RIADEIRTLNRWEIGELEVGWTQQQIgSSTMPHKRNPEGCEQ 324
Cdd:PRK06705 258 RWIHDFLLLATKEYDGITVARPYVQI-SSIMPQKRNPVSIEH 298
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
132-329 |
5.30e-04 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 42.22 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 132 EYVHFGATTQDIQDTAQSLE-MRDVLDETERALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELlRH 210
Cdd:PRK12425 130 DHVNRSQSSNDCFPTAMHIAaAQAVHEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQL-DY 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 211 RERlgeARKRIL--VVQLFGG---VGT----MAAFGDEAMLLLESFARRLSLDVP-----LAGwhvsRDRVTEFVSTLAM 276
Cdd:PRK12425 209 AER---AIRAALpaVCELAQGgtaVGTglnaPHGFAEAIAAELAALSGLPFVTAPnkfaaLAG----HEPLVSLSGALKT 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598712 277 VTASLARIADEIRTLNRW-EIGELEVGWTQQQIGSSTMPHKRNPEGCEQVVVLA 329
Cdd:PRK12425 282 LAVALMKIANDLRLLGSGpRAGLAEVRLPANEPGSSIMPGKVNPTQCEALSMLA 335
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
132-323 |
9.56e-04 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 41.60 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 132 EYVHFGATTQDIQDTAQSLEMrdVLDETER---ALDILLDRLSVLASGTRNALMVARTHSIPALPTTFGLKVAGWIDELL 208
Cdd:PLN00134 124 DHVNRSQSSNDTFPTAMHIAA--ATEIHSRlipALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598712 209 RHRERLGEARKRILVVQLFG-----GVGTMAAFgDEAMLLLESFARRLSLDVP------LAgwhvSRDRVTEFVSTLAMV 277
Cdd:PLN00134 202 YGLNRVQCTLPRLYELAQGGtavgtGLNTKKGF-DEKIAAAVAEETGLPFVTApnkfeaLA----AHDAFVELSGALNTV 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598712 278 TASLARIADEIRTLN---RWEIGELEVgwTQQQIGSSTMPHKRNPEGCE 323
Cdd:PLN00134 277 AVSLMKIANDIRLLGsgpRCGLGELNL--PENEPGSSIMPGKVNPTQCE 323
|
|
| |
