|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
17-437 |
0e+00 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 861.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 97 HCCPKAAGIIHLGATSCYVGDNT---------------LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 161
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTdliqirdaldlilpkLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 162 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 241
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 242 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 321
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 322 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQ 401
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1034628421 402 EGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 437
Cdd:cd03302 401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
17-445 |
2.91e-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: 2.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 95 FGHCCPKAAG-IIHLGATSCYVGDNTLA---------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 158
Cdd:COG0015 81 LKEKVGAEAGeYIHFGATSQDINDTALAlqlrealelllpdldALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 159 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLS 238
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNPVTT-QIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 239 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 316
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 317 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 396
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034628421 397 SvvkqegGDNDLIERI----QVDAYFSPihSQLDHLLDPSSFTGRASQQVQRF 445
Cdd:COG0015 392 E------EGNDLRELLaadpEIPAELSK--EELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
17-445 |
2.44e-144 |
|
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: 421.37 E-value: 2.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 96 GHCCPKAAGIIHLGATSCYVGDNTLA---------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 160
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALAlllrdaleiilpklkQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 161 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEgddhkveQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 240
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVE-------EVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 241 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDD 318
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 319 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAsv 398
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAA-- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034628421 399 vkqEGGDNDLIERIQVDAYFSPIHSQLD--HLLDPSSFTGRASQQVQRF 445
Cdd:TIGR00928 390 ---EVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
233-436 |
7.46e-75 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 235.31 E-value: 7.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 233 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 310
Cdd:PRK08937 17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 311 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 390
Cdd:PRK08937 95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034628421 391 LSQQAASVVkqeggdNDLIERIQVDAYFSPIHSQ--LDHLLDPSSFTG 436
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
363-445 |
9.77e-25 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 97.49 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 363 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAASVVKqeggdNDLIERIQVDAYFS-PIHSQLDHLLDPSSFTGRASQQ 441
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 1034628421 442 VQRF 445
Cdd:pfam10397 75 VDRV 78
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
362-446 |
3.34e-20 |
|
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: 84.81 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 362 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKqeggdnDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRAS 439
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74
|
....*..
gi 1034628421 440 QQVQRFL 446
Cdd:smart00998 75 AIVDRVL 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
17-437 |
0e+00 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 861.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFG 96
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 97 HCCPKAAGIIHLGATSCYVGDNT---------------LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWI 161
Cdd:cd03302 81 LLCPAAAGIIHLGATSCFVTDNTdliqirdaldlilpkLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 162 QDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA 241
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 242 SLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN 321
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 322 RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQ 401
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1034628421 402 EGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGR 437
Cdd:cd03302 401 EGGDNDLIERIKNDAYFKPIWDELDALLDPKTFIGR 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
26-390 |
1.29e-163 |
|
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: 468.52 E-value: 1.29e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 26 MCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHTFGHCCPK-A 102
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADVfeIDAERIAEIEKETGHDVIAFVYALAEKCGEdA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 103 AGIIHLGATSCYVGDNT---------------LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMD 167
Cdd:cd01595 80 GEYVHFGATSQDINDTAlalqlrdaldiilpdLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 168 LQNLKRVRDDLRFRGVKGTTGTQASFLQlfegddhKVEQLDKMVTEKAGFKrAFIITGQTYTRKVDIEVLSVLASLGASV 247
Cdd:cd01595 160 LERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEERVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 248 HKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDDSANRRIC 325
Cdd:cd01595 232 EKIATDIRLLQRteIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-VQWHERDLSDSSVERNI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034628421 326 LAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 390
Cdd:cd01595 311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
17-445 |
2.91e-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: 2.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLEN--IDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 95 FGHCCPKAAG-IIHLGATSCYVGDNTLA---------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 158
Cdd:COG0015 81 LKEKVGAEAGeYIHFGATSQDINDTALAlqlrealelllpdldALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 159 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLfegddhkVEQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLS 238
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNPVTT-QIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 239 VLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMdPLQTASVQWFERTL 316
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAA-ALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 317 DDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAA 396
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034628421 397 SvvkqegGDNDLIERI----QVDAYFSPihSQLDHLLDPSSFTGRASQQVQRF 445
Cdd:COG0015 392 E------EGNDLRELLaadpEIPAELSK--EELEALFDPANYLGAADEIVDRV 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
17-445 |
2.44e-144 |
|
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: 421.37 E-value: 2.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTF 95
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGViPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 96 GHCCPKAAGIIHLGATSCYVGDNTLA---------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 160
Cdd:TIGR00928 81 KEKCGAEGEFIHFGATSNDIVDTALAlllrdaleiilpklkQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 161 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEgddhkveQLDKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 240
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVE-------EVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 241 ASLGASVHKICTDIRLLANL--KEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQWFERTLDD 318
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRTehFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENA-PLWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 319 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAsv 398
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAA-- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034628421 399 vkqEGGDNDLIERIQVDAYFSPIHSQLD--HLLDPSSFTGRASQQVQRF 445
Cdd:TIGR00928 390 ---EVDEPDLLEFLLEDERITKYLKEEElaELLDPETYIGNAGEIVERV 435
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
36-350 |
2.89e-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: 279.00 E-value: 2.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 36 FRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLENIDFKMAA---EEEKRLRHDVMAHVHTFGHCCPKA-AGIIHLGAT 111
Cdd:cd01334 1 IRADLQVEKAHAKALAELGL-LPKEAAEAILAALDEILEGIAAdqvEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 112 SCYVGDNT---------------LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRD 176
Cdd:cd01334 80 SNDIVDTAlrlalrdaldillpaLKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 177 DLRFRGVKGTT-GTQASFlqlfegddhkVEQLDKMVTEKAGFKRAFIITGQ-TYTRKVDIEVLSVLASLGASVHKICTDI 254
Cdd:cd01334 160 RLNVLPLGGGAvGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 255 RLLAN--LKEMEEPFEKQqIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASvQWFERTLDDSANRRICLAEAFLT 332
Cdd:cd01334 230 RLLSSgeFGEVELPDAKQ-PGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDL 307
|
330
....*....|....*...
gi 1034628421 333 ADTILNTLQNISEGLVVY 350
Cdd:cd01334 308 LDAALRLLTGVLEGLEVN 325
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
233-436 |
7.46e-75 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 235.31 E-value: 7.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 233 DIEVLsVLASLGASVHKICTDIRLLANLK--EMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAsVQ 310
Cdd:PRK08937 17 DIAEI-VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 311 WFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRV 390
Cdd:PRK08937 95 WHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIRE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034628421 391 LSQQAASVVkqeggdNDLIERIQVDAYFSPIHSQ--LDHLLDPSSFTG 436
Cdd:PRK08937 175 KAMEAWKNQ------KDLRELLEADERFTKQLTKeeLDELFDPEAFVG 216
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
20-389 |
2.45e-70 |
|
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: 229.36 E-value: 2.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 20 RYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQE----MKSNLENIDfkmaaEEEKRLRHDVMAHVHTF 95
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGV-IPAEAAEEirkkAKFDVERVK-----EIEAETKHDVIAFVTAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 96 GHCCPKAAGIIHLGATSCYVGDNTLA---------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLW 160
Cdd:cd01360 75 AEYCGEAGRYIHFGLTSSDVVDTALAlqlrealdiilkdlkELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 161 IQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfegdDHKVEqldKMVTEKAGFKRAFIITgQTYTRKVDIEVLSVL 240
Cdd:cd01360 155 YAEFKRHLERLKEARERILVGKISGAVGTYANL-------GPEVE---ERVAEKLGLKPEPIST-QVIQRDRHAEYLSTL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 241 ASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERTLDD 318
Cdd:cd01360 224 ALIASTLEKIATEIRHLqrTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNV-IPALENVALWHERDISH 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034628421 319 SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIR 389
Cdd:cd01360 303 SSVERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQ 373
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
17-448 |
1.34e-48 |
|
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.
Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 173.58 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL--PITDEQIQEmKSNLENIDFKMAAEEEKRLRHDVMAHVHT 94
Cdd:cd01597 2 LGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVipKEAAAEIAA-AADVERLDLEALAEATARTGHPAIPLVKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 95 FGHCCPKAAG-IIHLGATSCYVGD---------------NTLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCC 158
Cdd:cd01597 81 LTAACGDAAGeYVHWGATTQDIIDtalvlqlrdaldlleRDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 159 LWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFlqlfeGDDhkveqldKMVTEKAGFKR----AFIITGQTyTRKVDI 234
Cdd:cd01597 161 VWLSELLRHRERLDELRPRVLVVQFGGAAGTLASL-----GDQ-------GLAVQEALAAElglgVPAIPWHT-ARDRIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 235 EVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLAR---HLMTLVMDplqtASV 309
Cdd:cd01597 228 ELASFLALLTGTLGKIARDVYLLmqTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARrvpGLAALLLD----AMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 310 QWFERtlDDSANR--RICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGsRQDCHEK 387
Cdd:cd01597 304 QEHER--DAGAWHaeWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPKLG-RQEAHDL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034628421 388 IRVLSQQAAsvvkQEGGdnDLIERI----QVDAYFSPihSQLDHLLDPSSFTGRASQQVQRFLEE 448
Cdd:cd01597 381 VYEACMRAV----EEGR--PLREVLledpEVAAYLSD--EELDALLDPANYLGSAPALVDRVLAR 437
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
96-341 |
2.69e-36 |
|
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: 134.27 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 96 GHCCPKAAGII-----HLGATSCYVGDNT---------------LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGK 155
Cdd:cd01594 22 GRAGELAGGLHgsalvHKGRSSNDIGTTAlrlalrdalddllplLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 156 RCCLWIQDLCMDLQNLKRVRDdlrfrgvkgttgtqasflqlfegddhkveqldkmvtekagfkrafiitgqtytrkvdIE 235
Cdd:cd01594 102 ELRAWAQVLGRDLERLEEAAV---------------------------------------------------------AE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 236 VLSVLASLGASVHKICTDIRLLANLKEME--EPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLqTASVQWFE 313
Cdd:cd01594 125 ALDALALAAAHLSKIAEDLRLLLSGEFGElgEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVL-TALKGGPE 203
|
250 260
....*....|....*....|....*...
gi 1034628421 314 RTLDDSANRRICLAEAFLTADTILNTLQ 341
Cdd:cd01594 204 RDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
363-445 |
9.77e-25 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 97.49 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 363 PFMATENIIMAMVKaGGSRQDCHEKIRVLSQQAASVVKqeggdNDLIERIQVDAYFS-PIHSQLDHLLDPSSFTGRASQQ 441
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK-----NDLRELLAADPEVTyLSEEELDALFDPAYYLGRADEI 74
|
....
gi 1034628421 442 VQRF 445
Cdd:pfam10397 75 VDRV 78
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
362-446 |
3.34e-20 |
|
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: 84.81 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 362 LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKqeggdnDLIERIQVDAYFSPIHS--QLDHLLDPSSFTGRAS 439
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGK------DLRELLLADPEVTAYLSeeELEELFDPEYYLGHAD 74
|
....*..
gi 1034628421 440 QQVQRFL 446
Cdd:smart00998 75 AIVDRVL 81
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
17-316 |
4.81e-20 |
|
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: 91.35 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 17 LASRYAS-PEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLpITDEQIQEMKSNLENIDFKMAAEEE-------------K 82
Cdd:TIGR02426 1 LLDGLFGdPAALELFSDRAFLRAMLDFEAALARAQADAGL-IPAEAAAAIEAACAAAAPDLEALAHaaatagnpviplvK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 83 RLRHDVMAhvhtfghccpKAAGIIHLGATSCYVGDNTL---------------ARVISRLADFAKERASLPTLGFTHFQP 147
Cdd:TIGR02426 80 ALRKAVAG----------EAARYVHRGATSQDVIDTSLmlqlrdaldllladlGRLADALADLAARHRDTPMTGRTLLQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 148 AQLTTVGKRCCLWIQDLCMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDkMVTEKAGF--KR 219
Cdd:TIGR02426 150 AVPTTFGLKAAGWLAAVLRARDRLAALRTRalpLQFGGAAGTlaaLGTRGGAVA-----AALAARLG-LPLPALPWhtQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 220 AFIItgqtytrkvdiEVLSVLASLGASVHKICTDIRLLANLkEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTL 299
Cdd:TIGR02426 224 DRIA-----------EFGSALALVAGALGKIAGDIALLSQT-EVGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGL 291
|
330
....*....|....*..
gi 1034628421 300 VMdPLQTASVQWFERTL 316
Cdd:TIGR02426 292 AA-TLHAALPQEHERSL 307
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
22-287 |
4.25e-17 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 82.03 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 22 ASPEMCFVFSDR--YKFRTWRQLWLW---LAEAEQTLGLPIT----------DEQIQEMKSNLENI----------DFKM 76
Cdd:pfam00206 6 PADALMGIFTDRsrFNFRLGEEDIKGlaaLKKAAAKANVILKeeaaaiikalDEVAEEGKLDDQFPlkvwqegsgtAVNM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 77 AAEEekRLRHDVMAHVHTFGHccpkaagiIHLGATSCYVGDNTLA----------------RVISRLADFAKERASLPTL 140
Cdd:pfam00206 86 NLNE--VIGELLGQLVHPNDH--------VHTGQSSNDQVPTALRlalkdalsevllpalrQLIDALKEKAKEFADIVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 141 GFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMvtEKAGFKRA 220
Cdd:pfam00206 156 GRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAKELGFF--TGLPVKAP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034628421 221 FIITgQTYTRKVDIEVLSVLASLGASVHKICTDIRLLAN--LKEMEEPFEKQQIGSSAMPYKRNPMRSE 287
Cdd:pfam00206 234 NSFE-ATSDRDAVVELSGALALLATSLSKFAEDLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
43-362 |
3.20e-15 |
|
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: 77.66 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMA---AEEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:cd01598 21 WLiALSNLEEIPEVPpLTKEELKFLRAIIENFSEEDAlriKEIEATTNHDVKAveyflkeKFETLGLL-KKIKEFIHFAC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 111 TSCYVgDNT-----------------LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKR 173
Cdd:cd01598 100 TSEDI-NNLayalmikearnevilplLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 174 VRDDLRFrgvKGTTGTQASflqlfegddHKVE--QLDKMVTEKAgFKRAFIITGQTYTRKVD-----IEVLSVLASLGAS 246
Cdd:cd01598 179 IEILGKF---NGAVGNFNA---------HLVAypDVDWRKFSEF-FVTSLGLTWNPYTTQIEphdyiAELFDALARINTI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 247 VHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHL-MTLVMDPLQtasvqwfeRTLDD 318
Cdd:cd01598 246 LIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAegnlglsNALLNHLsAKLPISRLQ--------RDLTD 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034628421 319 SANRR---ICLAEAFLTADTILNTLQNISeglvvypkVIERRIRQEL 362
Cdd:cd01598 318 STVLRnigVAFGHSLIAYKSLLRGLDKLE--------LNEARLLEDL 356
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
15-448 |
6.02e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 73.90 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 15 SPLASRY-ASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGL-PITDEQIQEMKSNLENIDFKMAAEEE----------- 81
Cdd:PRK09053 5 ARLTDLYfGSPAMRAIFSDRATVQRMLDFEAALARAEAACGViPAAAVAPIEAACDAERLDLDALAQAAalagnlaiplv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 82 KRLRHDVMAHVhtfghccPKAAGIIHLGATSCYVGD---------------NTLARVISRLADFAKERASLPTLGFTHFQ 146
Cdd:PRK09053 85 KQLTAQVAARD-------AEAARYVHWGATSQDIIDtglvlqlrdaldllePDLDRLCDALATLAARHRATPMVGRTWLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 147 PAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASF----------------LQLFEGDDHKveQLDKM 210
Cdd:PRK09053 158 QALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqalpvaqalaaelqLALPALPWHT--QRDRI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 211 VtekagfkrafiitgqtytrkvdiEVLSVLASLGASVHKICTDIRLL--ANLKEMEEPFEKQQIGSSAMPYKRNPMRSER 288
Cdd:PRK09053 236 A-----------------------EFASALGLLAGTLGKIARDVSLLmqTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 289 CCSLARHLMTLVMDpLQTASVQWFERTLD------DSANRRICLAEAFLTAdtilntLQNISEGLVVYPKvierRIRQEL 362
Cdd:PRK09053 293 VLTAATRAPGLVAT-LFAAMPQEHERALGgwhaewDTLPELACLAAGALAQ------MAQIVEGLEVDAA----RMRANL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 363 PfmATENIIMA---MVKAGGS--RQDCHEKIRVLSQQAasVVKQEGGDNDLIERIQVDAYFSPihSQLDHLLDPSSFTGR 437
Cdd:PRK09053 362 D--LTHGLILAeavMLALADRigRLDAHHLVEQASKRA--VAEGRHLRDVLAEDPQVSAHLSP--AALDRLLDPAHYLGQ 435
|
490
....*....|.
gi 1034628421 438 ASQQVQRFLEE 448
Cdd:PRK09053 436 AHAWVDRVLAE 446
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-315 |
7.68e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 63.54 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 100 PKAAGIIHLGATSCYVGDNTLA---------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDL 164
Cdd:PRK05975 96 EEAAAHVHFGATSQDVIDTSLMlrlkaaseilaarlgALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 165 CMDLQNLKRVRDD---LRFRGVKGT---TGTQASFLQlfegdDHKVEQLDKMVTEKAGFKRAFIitgqtytrkVDIEVLs 238
Cdd:PRK05975 176 LRHRDRLEALRADvfpLQFGGAAGTlekLGGKAAAVR-----ARLAKRLGLEDAPQWHSQRDFI---------ADFAHL- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 239 vLASLGASVHKICTDIRLLAnlkEMEEpfEKQQIG---SSAMPYKRNPMRSERCCSLARHLMTLVmDPLQTASVQWFERT 315
Cdd:PRK05975 241 -LSLVTGSLGKFGQDIALMA---QAGD--EISLSGgggSSAMPHKQNPVAAETLVTLARFNATQV-SGLHQALVHEQERS 313
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
119-283 |
3.96e-07 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 52.53 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 119 TLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TGTQASFlq 195
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTaigTGINAPP-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 196 lfEGDDHKVEQLDKMVteKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLA----------NLKEMee 265
Cdd:cd01357 236 --GYIELVVEKLSEIT--GLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSsgpraglgeiNLPAV-- 309
|
170
....*....|....*...
gi 1034628421 266 pfekqQIGSSAMPYKRNP 283
Cdd:cd01357 310 -----QPGSSIMPGKVNP 322
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
43-296 |
7.72e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 51.68 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 43 WL-WLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMAA---EEEKRLRHDVMA-------HVHTFGHCcPKAAGIIHLGA 110
Cdd:PRK09285 43 WLiALAAHPGIPEVPpFSAEANAFLRAIVENFSEEDAArikEIERTTNHDVKAveyflkeKLAGLPEL-EAVSEFIHFAC 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 111 TScyvGD-NTLA------------------RVISRLADFAKERASLPTLGFTHFQPAQLTTVGKrcclwiqdlcmDLQN- 170
Cdd:PRK09285 122 TS---EDiNNLShalmlkeareevllpalrELIDALKELAHEYADVPMLSRTHGQPATPTTLGK-----------EMANv 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 171 ---LKRVRDdlRFRGVK------GTTGTQASFLQLF-EGDDHKveqldkmvtekagFKRAFI----ITGQTYTRKV---- 232
Cdd:PRK09285 188 ayrLERQLK--QLEAVEilgkinGAVGNYNAHLAAYpEVDWHA-------------FSREFVeslgLTWNPYTTQIephd 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034628421 233 DI-EVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERC-------CSLARHL 296
Cdd:PRK09285 253 YIaELFDAVARFNTILIDLDRDVWGYISLGYFKQKTKAGEIGSSTMPHKVNPIDFENSegnlglaNALLEHL 324
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
120-283 |
8.42e-06 |
|
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: 48.19 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 120 LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG--TQASFL 194
Cdd:cd01596 159 LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTavgTGlnAPPGYA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 195 QLFegddhkVEQLDKmvtekagfkrafiITGQTYTR---KVD--------IEVLSVLASLGASVHKICTDIRLLA----- 258
Cdd:cd01596 239 EKV------AAELAE-------------LTGLPFVTapnLFEataahdalVEVSGALKTLAVSLSKIANDLRLLSsgpra 299
|
170 180 190
....*....|....*....|....*....|
gi 1034628421 259 -----NLKEMeEPfekqqiGSSAMPYKRNP 283
Cdd:cd01596 300 glgeiNLPAN-QP------GSSIMPGKVNP 322
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
120-283 |
2.21e-05 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 47.04 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 120 LARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG--TQASFL 194
Cdd:PRK12273 166 LEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATaigTGlnAPPGYI 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 195 QLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRLL-----A 258
Cdd:PRK12273 246 ELV------VEKLAE-------------ITGLPLVPAEDlieatqdtgafVEVSGALKRLAVKLSKICNDLRLLssgprA 306
|
170 180
....*....|....*....|....*
gi 1034628421 259 NLKEMEEPfeKQQIGSSAMPYKRNP 283
Cdd:PRK12273 307 GLNEINLP--AVQAGSSIMPGKVNP 329
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
119-283 |
4.84e-05 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 45.81 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 119 TLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TG--TQASF 193
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTaigTGlnAPPGY 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 194 LQLFegddhkVEQLDKmvtekagfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRLLA---- 258
Cdd:COG1027 240 IELV------VEHLAE-------------ITGLPLVRAENlieatqdtdafVEVSGALKRLAVKLSKICNDLRLLSsgpr 300
|
170 180 190
....*....|....*....|....*....|.
gi 1034628421 259 ------NLKEMeepfekqQIGSSAMPYKRNP 283
Cdd:COG1027 301 aglgeiNLPAV-------QPGSSIMPGKVNP 324
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
131-287 |
3.66e-04 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 43.05 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 131 AKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGT---TGTQASflqlfegddhkVEQL 207
Cdd:PRK13353 175 AAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTavgTGLNAD-----------PEYI 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 208 DKMVTEKAGfkrafiITGQTYTRKVD-----------IEVLSVLASLGASVHKICTDIRLLAN-----LKEMEEPfeKQQ 271
Cdd:PRK13353 244 ERVVKHLAA------ITGLPLVGAEDlvdatqntdafVEVSGALKVCAVNLSKIANDLRLLSSgprtgLGEINLP--AVQ 315
|
170
....*....|....*.
gi 1034628421 272 IGSSAMPYKRNPMRSE 287
Cdd:PRK13353 316 PGSSIMPGKVNPVMPE 331
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
240-287 |
7.14e-04 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 42.00 E-value: 7.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034628421 240 LASLGASVHKICTDIRLLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 287
Cdd:PRK00485 281 LKTLAVSLMKIANDIRWLASgprcgLGEISLP--ENEPGSSIMPGKVNPTQCE 331
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
15-155 |
4.27e-03 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 39.72 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 15 SPLASRYAS--PEMCFVFSD----RYKFRTWRQLWLWLAEAEQTLGLP-ITDEQIQEMKSNLENIDFKMAAEE---EKRL 84
Cdd:PLN02848 13 SPLDGRYWSkvKDLRPIFSEfgliRYRVLVEVKWLLKLSQIPEVTEVPpFSDEANSFLEGIIAGFSVDDALEVkkiERVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034628421 85 RHDVMAhVHTF--GHCC--PKAAGI---IHLGATSCYVgdNTLA------------------RVISRLADFAKERASLPT 139
Cdd:PLN02848 93 NHDVKA-VEYFlkQKCKshPELAKVlefFHFACTSEDI--NNLShalmlkegvnsvvlptmdEIIKAISSLAHEFAYVPM 169
|
170
....*....|....*.
gi 1034628421 140 LGFTHFQPAQLTTVGK 155
Cdd:PLN02848 170 LSRTHGQPASPTTLGK 185
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
234-287 |
4.38e-03 |
|
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: 39.41 E-value: 4.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034628421 234 IEVLSVLASLGASVHKICTDIRLLAN-----LKEMEEPfeKQQIGSSAMPYKRNPMRSE 287
Cdd:cd01362 271 VEASGALKTLAVSLMKIANDIRWLGSgprcgLGELSLP--ENEPGSSIMPGKVNPTQCE 327
|
|
| |
