NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|262089311|gb|ACY24532|]
View 

adenylosuccinate lyase [uncultured crenarchaeote 57a5]

Protein Classification

adenylosuccinate lyase( domain architecture ID 10102158)

adenylosuccinate lyase catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 10-393 0e+00

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


:

Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 515.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  10 RYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVArsnKITINKIKELESISEHDTASIVQAISQH 89
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKA---KFDVERVKEIEAETKHDVIAFVTAIAEY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  90 CTPSTRpWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWAN 169
Cdd:cd01360   78 CGEAGR-YIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 170 ELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGsraLAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLDKI 249
Cdd:cd01360  157 EFKRHLERLKEARERILVGKISGAVGTYANLG---PEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 250 AIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMG 329
Cdd:cd01360  234 ATEIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDA 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089311 330 IILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAF 393
Cdd:cd01360  314 TILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQREYY 377
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 362-441 4.25e-17

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: 75.56  E-value: 4.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   362 KGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 10-393 0e+00

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 515.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  10 RYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVArsnKITINKIKELESISEHDTASIVQAISQH 89
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKA---KFDVERVKEIEAETKHDVIAFVTAIAEY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  90 CTPSTRpWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWAN 169
Cdd:cd01360   78 CGEAGR-YIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 170 ELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGsraLAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLDKI 249
Cdd:cd01360  157 EFKRHLERLKEARERILVGKISGAVGTYANLG---PEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 250 AIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMG 329
Cdd:cd01360  234 ATEIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDA 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089311 330 IILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAF 393
Cdd:cd01360  314 TILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQREYY 377
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 8-441 9.69e-180

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: 509.24  E-value: 9.69e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   8 SGRYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQAIS 87
Cdd:COG0015    3 SPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKETRHDVKAFVYALK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  88 QHCTPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVW 167
Cdd:COG0015   83 EKVGAEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 168 ANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLD 247
Cdd:COG0015  163 AAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEAWPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGSLE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 248 KIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIP 327
Cdd:COG0015  243 KIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNILP 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 328 MGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKNFKEAII 407
Cdd:COG0015  323 DAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLRELLA 402

                        410       420       430
                 ....*....|....*....|....*....|....
gi 262089311 408 QDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:COG0015  403 ADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 8-441 6.94e-137

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: 400.18  E-value: 6.94e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311    8 SGRYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQAIS 87
Cdd:TIGR00928   2 DERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   88 QHCtPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVW 167
Cdd:TIGR00928  82 EKC-GAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  168 ANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLD 247
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVEEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  248 KIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIP 327
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  328 MGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKN-FKEAI 406
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEPdLLEFL 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 262089311  407 IQDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 226-431 2.86e-66

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 211.43  E-value: 2.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 226 VIPRESLAEvqFIISLVGCTLDKIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQ 305
Cdd:PRK08937  12 VIPKEDIAE--IVLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 306 ENISLWHERDLSNSANERFTIPMGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAY 385
Cdd:PRK08937  90 ENVPLWHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAH 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 262089311 386 DNIQRVAFQTLAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHL 431
Cdd:PRK08937 170 ELIREKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
Lyase_1 pfam00206
Lyase;
9-288 7.85e-40

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 145.20  E-value: 7.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311    9 GRYG--SNEIRNIFEEERRLRYQLD-----FEAQVALSQGKLNIIPKNASREISLVARSN--KITINKIKELESISEHD- 78
Cdd:pfam00206   1 GRFTvpADALMGIFTDRSRFNFRLGeedikGLAALKKAAAKANVILKEEAAAIIKALDEVaeEGKLDDQFPLKVWQEGSg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   79 TAS-------IVQAISQHCTPSTrpWIHYGLTSNDVVDTSTSMQLRDA-FEIIEPKISKLISLILNKAKTYSTLPSVGRT 150
Cdd:pfam00206  81 TAVnmnlnevIGELLGQLVHPND--HVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  151 HGQHASIISFGLKFAVWANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSR---ALAVQKDVAKSLGLYSVEA--ATQ 225
Cdd:pfam00206 159 HLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADpefAELVAKELGFFTGLPVKAPnsFEA 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262089311  226 VIPRESLAEVQFIISLVGCTLDKIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSE 288
Cdd:pfam00206 239 TSDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 362-441 4.25e-17

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: 75.56  E-value: 4.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   362 KGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 363-441 1.50e-13

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: 65.51  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  363 GRIYAEFILEALVKkGIPRMKAYDNIQRVAFQTLAEDKN-FKEAIIQDTSIGSnLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:pfam10397   1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGKNdLRELLAADPEVTY-LSEEELDALFDPAYYLGRADEIVDRV 78
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 10-393 0e+00

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 515.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  10 RYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVArsnKITINKIKELESISEHDTASIVQAISQH 89
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKA---KFDVERVKEIEAETKHDVIAFVTAIAEY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  90 CTPSTRpWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWAN 169
Cdd:cd01360   78 CGEAGR-YIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 170 ELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGsraLAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLDKI 249
Cdd:cd01360  157 EFKRHLERLKEARERILVGKISGAVGTYANLG---PEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 250 AIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMG 329
Cdd:cd01360  234 ATEIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDA 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089311 330 IILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAF 393
Cdd:cd01360  314 TILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQREYY 377
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 8-441 9.69e-180

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: 509.24  E-value: 9.69e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   8 SGRYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQAIS 87
Cdd:COG0015    3 SPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKETRHDVKAFVYALK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  88 QHCTPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVW 167
Cdd:COG0015   83 EKVGAEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 168 ANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLD 247
Cdd:COG0015  163 AAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEAWPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGSLE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 248 KIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIP 327
Cdd:COG0015  243 KIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNILP 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 328 MGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKNFKEAII 407
Cdd:COG0015  323 DAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLRELLA 402

                        410       420       430
                 ....*....|....*....|....*....|....
gi 262089311 408 QDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:COG0015  403 ADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 16-393 7.26e-160

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: 456.58  E-value: 7.26e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  16 IRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQAISQHCTPSTR 95
Cdd:cd01595    1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVFEIDAERIAEIEKETGHDVIAFVYALAEKCGEDAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  96 PWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHI 175
Cdd:cd01595   81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 176 ERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLDKIAIEIRN 255
Cdd:cd01595  161 ERLEEARERVLVGGISGAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 256 LQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMGIILLDE 335
Cdd:cd01595  241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262089311 336 MVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAF 393
Cdd:cd01595  321 ALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKEENY 378
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 8-441 6.94e-137

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: 400.18  E-value: 6.94e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311    8 SGRYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQAIS 87
Cdd:TIGR00928   2 DERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   88 QHCtPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVW 167
Cdd:TIGR00928  82 EKC-GAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  168 ANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAATQVIPRESLAEVQFIISLVGCTLD 247
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVEEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  248 KIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIP 327
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  328 MGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKN-FKEAI 406
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEPdLLEFL 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 262089311  407 IQDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 11-444 1.25e-117

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: 351.16  E-value: 1.25e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  11 YGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQAISQHC 90
Cdd:cd01597    6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATARTGHPAIPLVKQLTAAC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  91 TPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANE 170
Cdd:cd01597   86 GDAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 171 LSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAATQVIpRESLAEVQFIISLVGCTLDKIA 250
Cdd:cd01597  166 LLRHRERLDELRPRVLVVQFGGAAGTLASLGDQGLAVQEALAAELGLGVPAIPWHTA-RDRIAELASFLALLTGTLGKIA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 251 IEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMGI 330
Cdd:cd01597  245 RDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIF 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 331 ILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKgIPRMKAYDNIQRVAFQTLAEDKNFKEAIIQDT 410
Cdd:cd01597  325 LLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRAVEEGRPLREVLLEDP 403

                        410       420       430
                 ....*....|....*....|....*....|....
gi 262089311 411 SIGSNLNMNELRKIFDPNNHLAASTKIIDNVAKK 444
Cdd:cd01597  404 EVAAYLSDEELDALLDPANYLGSAPALVDRVLAR 437
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 26-350 6.90e-92

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: 281.31  E-value: 6.90e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  26 LRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITI-NKIKELESISEHDTASIVQAISQHCTPSTRPWIHYGLTS 104
Cdd:cd01334    1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIaADQVEQEGSGTHDVMAVEEVLAERAGELNGGYVHTGRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 105 NDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKKR 184
Cdd:cd01334   81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 185 FLLCK-TLGVVGTGSLMGsraLAVQKDVAKSLGLYSVEAAT--QVIPRESLAEVQFIISLVGCTLDKIAIEIRNLQRTEI 261
Cdd:cd01334  161 LNVLPlGGGAVGTGANAP---PIDRERVAELLGFFGPAPNStqAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEF 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 262 GEVEEPFKKgQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMGIILLDEMVNSMI 341
Cdd:cd01334  238 GEVELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLT 316


                 ....*....
gi 262089311 342 KVIEGLTVN 350
Cdd:cd01334  317 GVLEGLEVN 325
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 226-431 2.86e-66

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 211.43  E-value: 2.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 226 VIPRESLAEvqFIISLVGCTLDKIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQ 305
Cdd:PRK08937  12 VIPKEDIAE--IVLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 306 ENISLWHERDLSNSANERFTIPMGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAY 385
Cdd:PRK08937  90 ENVPLWHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAH 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 262089311 386 DNIQRVAFQTLAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHL 431
Cdd:PRK08937 170 ELIREKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 8-401 1.11e-65

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: 217.19  E-value: 1.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   8 SGRYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNI-IPKNASREISlvARSNKITINKIKELESISEHDTASIVQAI 86
Cdd:cd03302    2 ASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLdISDEQIEEMK--ANVENIDFEIAAAEEKKLRHDVMAHVHAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  87 SQHCtPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAV 166
Cdd:cd03302   80 GLLC-PAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 167 WANELSLHIERIEEGKKRFLLCKTLGVVGTGSLM-------GSRALAVQKDVAKSLGLYSVEAAT-QVIPRESLAEVQFI 238
Cdd:cd03302  159 WIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFldlfegdHDKVEALDELVTKKAGFKKVYPVTgQTYSRKVDIDVLNA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 239 ISLVGCTLDKIAIEIRNLQRTEigEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRS-FSNIAQENISLWHERDLS 317
Cdd:cd03302  239 LSSLGATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNlASNAAQTASTQWFERTLD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 318 NSANERFTIPMGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLA 397
Cdd:cd03302  317 DSANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAA 396


                 ....
gi 262089311 398 EDKN 401
Cdd:cd03302  397 VVKQ 400
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 11-441 2.26e-59

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 201.01  E-value: 2.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  11 YGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREISLVARSNKITINKIKELESISEHDTASIVQA----I 86
Cdd:PRK09053  12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALAGNLAIPLVKQltaqV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  87 SQHCTPSTRpWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAV 166
Cdd:PRK09053  92 AARDAEAAR-YVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 167 WANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEAA--TQvipRESLAEVQFIISLVGC 244
Cdd:PRK09053 171 WLDALLRHRQRLAALRPRALVLQFGGAAGTLASLGEQALPVAQALAAELQLALPALPwhTQ---RDRIAEFASALGLLAG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 245 TLDKIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSE-------RVSSLARILrsFSNIAQEnislwHERDLS 317
Cdd:PRK09053 248 TLGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAavltaatRAPGLVATL--FAAMPQE-----HERALG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 318 NSANERFTIPMGIILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGRIYAEFILEALVKKgIPRMKAYDNIQRVAFQTLA 397
Cdd:PRK09053 321 GWHAEWDTLPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADR-IGRLDAHHLVEQASKRAVA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 262089311 398 EDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:PRK09053 400 EGRHLRDVLAEDPQVSAHLSPAALDRLLDPAHYLGQAHAWVDRV 443
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 96-341 2.09e-45

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: 157.77  E-value: 2.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  96 PWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHI 175
Cdd:cd01594   35 ALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVLGRDL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 176 ERIEEgkkrfllcktlgvvgtgslmgsralavqkdvakslglysveAAtqvipresLAEVQFIISLVGCTLDKIAIEIRN 255
Cdd:cd01594  115 ERLEE-----------------------------------------AA--------VAEALDALALAAAHLSKIAEDLRL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 256 LQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSERVSSLARILRSFSNIAQENISLWHERDLSNSANERFTIPMGIILLDE 335
Cdd:cd01594  146 LLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSMREILADSLLLLID 225


                 ....*.
gi 262089311 336 MVNSMI 341
Cdd:cd01594  226 ALRLLL 231
Lyase_1 pfam00206
Lyase;
9-288 7.85e-40

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 145.20  E-value: 7.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311    9 GRYG--SNEIRNIFEEERRLRYQLD-----FEAQVALSQGKLNIIPKNASREISLVARSN--KITINKIKELESISEHD- 78
Cdd:pfam00206   1 GRFTvpADALMGIFTDRSRFNFRLGeedikGLAALKKAAAKANVILKEEAAAIIKALDEVaeEGKLDDQFPLKVWQEGSg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   79 TAS-------IVQAISQHCTPSTrpWIHYGLTSNDVVDTSTSMQLRDA-FEIIEPKISKLISLILNKAKTYSTLPSVGRT 150
Cdd:pfam00206  81 TAVnmnlnevIGELLGQLVHPND--HVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  151 HGQHASIISFGLKFAVWANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSR---ALAVQKDVAKSLGLYSVEA--ATQ 225
Cdd:pfam00206 159 HLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADpefAELVAKELGFFTGLPVKAPnsFEA 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262089311  226 VIPRESLAEVQFIISLVGCTLDKIAIEIRNLQRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSE 288
Cdd:pfam00206 239 TSDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 1-320 4.13e-28

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 114.00  E-value: 4.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   1 MPILPID----SGRYGSNEIRNIFEEERRLRYQLDFEAQVALSQGKLNIIPKNASREIslVARSNKITINkIKELESISE 76
Cdd:PRK05975   1 MSISVFDhpflSGLFGDDEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERI--AAACETFEPD-LAALRHATA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  77 HDTASI---VQAISQHCTPSTRPWIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQ 153
Cdd:PRK05975  78 RDGVVVpalVRQLRAAVGEEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 154 HASIISFGLKFAVWANELSLHIERIEEGKKRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSV-EAATQvipRESL 232
Cdd:PRK05975 158 AAIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGGAAGTLEKLGGKAAAVRARLAKRLGLEDApQWHSQ---RDFI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 233 AEVQFIISLVGCTLDKIAIEIRNLQRTEiGEVEepfKKGQLGSSAVPVKRNPIKSERVSSLARilrsFSNIAQENI--SL 310
Cdd:PRK05975 235 ADFAHLLSLVTGSLGKFGQDIALMAQAG-DEIS---LSGGGGSSAMPHKQNPVAAETLVTLAR----FNATQVSGLhqAL 306

                        330
                 ....*....|
gi 262089311 311 WHERDLSNSA 320
Cdd:PRK05975 307 VHEQERSGAA 316
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 16-385 1.42e-23

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: 102.31  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  16 IRNIFEEERRLRYQLDFEAQ--VALSQ-GKLNIIPKNASREI----SLVARSNKITINKIKELESISEHDTASIVQAISQ 88
Cdd:cd01598    1 LRPYFSEYALIKYRVQVEVEwlIALSNlEEIPEVPPLTKEELkflrAIIENFSEEDALRIKEIEATTNHDVKAVEYFLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  89 HCTPSTR-----PWIHYGLTSNDVVDTSTSMQLRDAFE-IIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGL 162
Cdd:cd01598   81 KFETLGLlkkikEFIHFACTSEDINNLAYALMIKEARNeVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 163 KFAVWANELSLHIERIEEGKkrfLLCKTLGVVGTGSlmgsrALAV----------QKDVAKSLGLYSVEAATQVIPRESL 232
Cdd:cd01598  161 ELAVFVYRLERQYKQLKQIE---ILGKFNGAVGNFN-----AHLVaypdvdwrkfSEFFVTSLGLTWNPYTTQIEPHDYI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 233 AEVQFIISLVGCTLDKIAIEIrnLQRTEIGEVEEPFKKGQLGSSAVPVKRNPI---KSERVSSLAR-ILRSFSniAQENI 308
Cdd:cd01598  233 AELFDALARINTILIDLCRDI--WGYISLGYFKQKVKKGEVGSSTMPHKVNPIdfeNAEGNLGLSNaLLNHLS--AKLPI 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262089311 309 SLWhERDLSNSANER-FTIPMGIILLdeMVNSMIKVIEGLTVNRQKILDNINKTkGRIYAEFILEALVKKGIPrmKAY 385
Cdd:cd01598  309 SRL-QRDLTDSTVLRnIGVAFGHSLI--AYKSLLRGLDKLELNEARLLEDLDAN-WEVLAEPIQTVMRRYGIP--NPY 380
PLN02848 PLN02848
adenylosuccinate lyase
 1-398 2.04e-22

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 99.43  E-value: 2.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   1 MPILPIDsGRYGS--NEIRNIFEEERRLRYQLDFEAQVALsqgKLNIIP---------KNASREI-SLVARSNKITINKI 68
Cdd:PLN02848  10 TALSPLD-GRYWSkvKDLRPIFSEFGLIRYRVLVEVKWLL---KLSQIPevtevppfsDEANSFLeGIIAGFSVDDALEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  69 KELESISEHDTASIVQAISQHCtpSTRP-------WIHYGLTSNDVVDTSTSMQLRDAFE-IIEPKISKLISLILNKAKT 140
Cdd:PLN02848  86 KKIERVTNHDVKAVEYFLKQKC--KSHPelakvleFFHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 141 YSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKkrfLLCKTLGVVGTGSLMGSRA-----LAVQKDVAKSL 215
Cdd:PLN02848 164 FAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVK---IKGKFAGAVGNYNAHMSAYpevdwPAVAEEFVTSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 216 GLYSVEAATQVIPRESLAEVQFIISlvgcTLDKIAIEI-RNL-QRTEIGEVEEPFKKGQLGSSAVPVKRNPIKSErvssl 293
Cdd:PLN02848 241 GLTFNPYVTQIEPHDYMAELFNAVS----RFNNILIDFdRDIwSYISLGYFKQITKAGEVGSSTMPHKVNPIDFE----- 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 294 arilRSFSNIAQENISLWH----------ERDLSNSANERftiPMGIILLDEMV--NSMIKVIEGLTVNRQKILDNINKT 361
Cdd:PLN02848 312 ----NSEGNLGLANAELSHlsmklpisrmQRDLTDSTVLR---NMGVGLGHSLLayKSTLRGIGKLQVNEARLAEDLDQT 384

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 262089311 362 kGRIYAEFILEALVKKGIP----RMKAYDNIQRVAFQTLAE 398
Cdd:PLN02848 385 -WEVLAEPIQTVMRRYGVPepyeKLKELTRGRAVTKESMRE 424
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 5-361 7.57e-20

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 91.35  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   5 PIDsGRYGS--NEIRNIFEEERRLRYQLDFEAQ--VALSQG-KLNIIPKNASREI----SLVARSNKITINKIKELESIS 75
Cdd:PRK09285  11 PLD-GRYASktAALRPIFSEFGLIRYRVQVEVEwlIALAAHpGIPEVPPFSAEANaflrAIVENFSEEDAARIKEIERTT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  76 EHD-------------TASIVQAISqhctpstrPWIHYGLTSNDVVDTSTSMQLRDAFE-IIEPKISKLISLILNKAKTY 141
Cdd:PRK09285  90 NHDvkaveyflkeklaGLPELEAVS--------EFIHFACTSEDINNLSHALMLKEAREeVLLPALRELIDALKELAHEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 142 STLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKkrfLLCKTLGVVGTgslMGSRALA--------VQKDVAK 213
Cdd:PRK09285 162 ADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVE---ILGKINGAVGN---YNAHLAAypevdwhaFSREFVE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 214 SLGLYSVEAATQVIPRESLAEVqfiislvgctLDKIA----IEIrNL--------------QRTEIGEVeepfkkgqlGS 275
Cdd:PRK09285 236 SLGLTWNPYTTQIEPHDYIAEL----------FDAVArfntILI-DLdrdvwgyislgyfkQKTKAGEI---------GS 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 276 SAVPVKRNPI---KSERVSSLAR-ILRSFSNIAQenISLWhERDLSNSANER-FTIPMGIILLdeMVNSMIKVIEGLTVN 350
Cdd:PRK09285 296 STMPHKVNPIdfeNSEGNLGLANaLLEHLAAKLP--ISRW-QRDLTDSTVLRnLGVAFGYSLI--AYDSLLKGLGKLEVN 370

                        410
                 ....*....|.
gi 262089311 351 RQKILDNINKT 361
Cdd:PRK09285 371 EARLAEDLDAN 381
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 362-441 4.25e-17

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: 75.56  E-value: 4.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311   362 KGRIYAEFILEALVKKGIPRMKAYDNIQRVAFQTLAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 363-441 1.50e-13

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: 65.51  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  363 GRIYAEFILEALVKkGIPRMKAYDNIQRVAFQTLAEDKN-FKEAIIQDTSIGSnLNMNELRKIFDPNNHLAASTKIIDNV 441
Cdd:pfam10397   1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGKNdLRELLAADPEVTY-LSEEELDALFDPAYYLGRADEIVDRV 78
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 104-427 1.67e-12

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: 69.07  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 104 SNDVVdtSTSMQLRDAFEIIE---PKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEE 180
Cdd:cd01362  136 SNDTF--PTAMHIAAALALQErllPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEA 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 181 GKKRfLLCKTLG--VVGTGslMGSR---ALAVQKDVAKSLGLYSVEA-------ATQviprESLAEVQFIISLVGCTLDK 248
Cdd:cd01362  214 ALPR-LYELALGgtAVGTG--LNAHpgfAEKVAAELAELTGLPFVTApnkfealAAH----DALVEASGALKTLAVSLMK 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 249 IAIEIRNLQ---RTEIGEVEEPfkKGQLGSSAVPVKRNPIKSERVSSLAriLRSFSN-----IA--QENISLwherdlsN 318
Cdd:cd01362  287 IANDIRWLGsgpRCGLGELSLP--ENEPGSSIMPGKVNPTQCEALTMVA--AQVMGNdaaitIAgsSGNFEL-------N 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 319 SANerftiPMGI--------ILLDEMVNSMIKVIEGLTVNRQKILDNINKTkgriyaeFIL-EALVkkgiPRMkAYDNIQ 389
Cdd:cd01362  356 VFK-----PVIIynllqsirLLADACRSFADKCVAGIEPNRERIAELLERS-------LMLvTALN----PHI-GYDKAA 418

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262089311 390 RVAFQTLAEDKNFKEAIIQDTsigsNLNMNELRKIFDP 427
Cdd:cd01362  419 KIAKKAHKEGLTLKEAALELG----YLTEEEFDRLVDP 452
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 105-294 1.35e-11

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 66.16  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 105 NDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKKR 184
Cdd:PRK13353 142 NDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREH 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 185 fLLCKTLG--VVGTGSLMGSR-ALAVQKDVAKSLGLYSVEA-----ATQVIprESLAEVQFIISLVGCTLDKIAIEIRNL 256
Cdd:PRK13353 222 -LYEVNLGgtAVGTGLNADPEyIERVVKHLAAITGLPLVGAedlvdATQNT--DAFVEVSGALKVCAVNLSKIANDLRLL 298

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 262089311 257 Q---RTEIGEVEEPFKkgQLGSSAVPVKRNPIKSERVSSLA 294
Cdd:PRK13353 299 SsgpRTGLGEINLPAV--QPGSSIMPGKVNPVMPEVVNQIA 337
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 97-433 5.03e-11

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: 64.49  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  97 WIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIE 176
Cdd:cd01359   80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 177 RIEEGKKRFLLCktlgVVGTGSLMGSrALAVQKD-VAKSLGLYSVEA----ATQVipRESLAEVQFIISLVGCTLDKIAI 251
Cdd:cd01359  160 RLADAYKRVNVS----PLGAGALAGT-TFPIDRErTAELLGFDGPTEnsldAVSD--RDFVLEFLSAAALLMVHLSRLAE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 252 EIRNLQRTEIGEVEepfkkgqL------GSSAVPVKRNPIKSERVSSLA-RI---LRSFSNIAQeNISLWHERDLSNSAN 321
Cdd:cd01359  233 DLILWSTQEFGFVE-------LpdaystGSSIMPQKKNPDVLELIRGKAgRVigaLAGLLTTLK-GLPLAYNKDLQEDKE 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 322 ERFTipmGIILLDEMVNSMIKVIEGLTVNRQKILDninktkgRIYAEFIL-----EALVK-KGIPRMKAYDNIQRVAFQT 395
Cdd:cd01359  305 PLFD---AVDTLIASLRLLTGVISTLTVNPERMRE-------AAEAGFSTatdlaDYLVReKGVPFREAHHIVGRAVRLA 374

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262089311 396 LAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHLAA 433
Cdd:cd01359  375 EEKGKDLSDLTLAELQAISPLFEEDVREALDPENSVER 412
fumC PRK00485
fumarate hydratase; Reviewed
 104-288 1.85e-09

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 59.33  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 104 SNDVVdtSTSMQLRDAFEIIE---PKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEE 180
Cdd:PRK00485 140 SNDTF--PTAMHIAAVLAIVErllPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEA 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 181 GKKRflLCK-TLG--VVGTG----SLMGSRALAVqkdVAKSLGLYSVEA-------ATQviprESLAEVQFIISLVGCTL 246
Cdd:PRK00485 218 ALPH--LYElALGgtAVGTGlnahPGFAERVAEE---LAELTGLPFVTApnkfealAAH----DALVEASGALKTLAVSL 288

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 262089311 247 DKIAIEIRNLQ---RTEIGEVEEPfkKGQLGSSAVPVKRNPIKSE 288
Cdd:PRK00485 289 MKIANDIRWLAsgpRCGLGEISLP--ENEPGSSIMPGKVNPTQCE 331
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 104-426 5.10e-09

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: 58.20  E-value: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 104 SNDvvDTSTSMQLRDAFEIIE---PKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEE 180
Cdd:cd01596  135 SND--DFPPAAHIAAALALLErllPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEA 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 181 GKKRFL-LCktLG--VVGTGsLMGSR--ALAVQKDVAKSLGLYSVEA-----ATQviPRESLAEVQFIISLVGCTLDKIA 250
Cdd:cd01596  213 ALERLReLN--LGgtAVGTG-LNAPPgyAEKVAAELAELTGLPFVTApnlfeATA--AHDALVEVSGALKTLAVSLSKIA 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 251 IEIRNLQ---RTEIGEVEEPfkKGQLGSSAVPVKRNPIKSERVSSLAriLRSFSN-----IAQENISLwhE--------- 313
Cdd:cd01596  288 NDLRLLSsgpRAGLGEINLP--ANQPGSSIMPGKVNPVIPEAVNMVA--AQVIGNdtaitMAGSAGQL--Elnvfkpvia 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 314 RDLSNSANerftipmgiILLDEMVNSMIKVIEGLTVNRQKILDNINKTKGriyaefILEALVKK-GiprmkaYDNIQRVA 392
Cdd:cd01596  362 YNLLQSIR---------LLANACRSFRDKCVEGIEANEERCKEYVENSLM------LVTALNPHiG------YEKAAEIA 420

                        330       340       350
                 ....*....|....*....|....*....|....
gi 262089311 393 FQTLAEDKNFKEAIIQDTsigsNLNMNELRKIFD 426
Cdd:cd01596  421 KEALKEGRTLREAALELG----LLTEEELDEILD 450
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 97-433 5.79e-09

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 57.85  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  97 WIHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIE 176
Cdd:PRK00855 104 KLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLE 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 177 RIEEGKKRFLLCktlgVVGTGSLMGS-----RALavqkdVAKSLG--------LYSVEAatqvipRESLAEVQFIISLVG 243
Cdd:PRK00855 184 RLRDARKRVNRS----PLGSAALAGTtfpidRER-----TAELLGfdgvtensLDAVSD------RDFALEFLSAASLLM 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 244 CTLDKIAIEIRNLQRTEIGEVEepfkkgqL------GSSAVPVKRNPI-------KSERV----SSLARILRsfsniaqe 306
Cdd:PRK00855 249 VHLSRLAEELILWSSQEFGFVE-------LpdafstGSSIMPQKKNPDvaelirgKTGRVygnlTGLLTVMK-------- 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 307 NISLWHERDLSnSANERF--TIPMGIILLdEMVNSMikvIEGLTVNRQKILDniNKTKGRIYAEFILEALVKKGIPRMKA 384
Cdd:PRK00855 314 GLPLAYNRDLQ-EDKEPLfdAVDTLKLSL-EAMAGM---LETLTVNKERMRE--AAGKGFSTATDLADYLVRKGVPFREA 386

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 262089311 385 YDNIQRVAFQTLAEDKNFKEAIIQDTSIGSNLNMNELRKIFDPNNHLAA 433
Cdd:PRK00855 387 HEIVGKAVREAEERGVDLADLSLEELQAFSPLITEDVYEVLTPEGSVAA 435
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 33-427 6.40e-09

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 57.70  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  33 EAQVALSQGKLN----IIPKNASREISLVARSNKITINKIKELESISEHDTAsivqaisqHCTPSTRpwIHYGLTSNDVV 108
Cdd:PRK14515  82 EAAQEILDGKWHdhfiVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYH--------YISPNSH--VNMAQSTNDAF 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 109 DTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKKRfLLC 188
Cdd:PRK14515 152 PTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQH-LYE 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 189 KTLGV--VGTGSLMGSRAL-AVQKDVAKSLGLYSVEA-----ATQviPRESLAEVQFIISLVGCTLDKIAIEIRNLQ--- 257
Cdd:PRK14515 231 VNMGAtaVGTGLNADPEYIeAVVKHLAAISELPLVGAedlvdATQ--NTDAYTEVSAALKVCMMNMSKIANDLRLMAsgp 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 258 RTEIGEVEEPFKkgQLGSSAVPVKRNPIKSERVSSLArilrsFSNIAQEnislwHERDLSNSANERFTIPMGIILLDEMV 337
Cdd:PRK14515 309 RVGLAEIMLPAR--QPGSSIMPGKVNPVMPEVINQIA-----FQVIGND-----HTICLASEAGQLELNVMEPVLVFNLL 376

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 338 NSMIKVIEGLTVNRQKILDNINKTKGRiyaefiLEALVKKGIPRMKA------YDNIQRVAFQTLAEDKNFKEAIIQDTS 411
Cdd:PRK14515 377 QSISIMNNGFRAFTDNCLKGIEANEDR------LKEYVEKSVGIITAvnphigYEAAARVAKEAIATGQSVRELCVKNGV 450

                        410
                 ....*....|....*.
gi 262089311 412 igsnLNMNELRKIFDP 427
Cdd:PRK14515 451 ----LSQEDLELILDP 462
PLN00134 PLN00134
fumarate hydratase; Provisional
 103-437 1.05e-07

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 53.93  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 103 TSNDVVdtSTSMQLRDAFEIIE---PKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIE 179
Cdd:PLN00134 131 SSNDTF--PTAMHIAAATEIHSrliPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 180 EGKKRfLLCKTLG--VVGTGsLMGSRALAVQ--KDVAKSLGLYSVEAATQViprESLA------EVQFIISLVGCTLDKI 249
Cdd:PLN00134 209 CTLPR-LYELAQGgtAVGTG-LNTKKGFDEKiaAAVAEETGLPFVTAPNKF---EALAahdafvELSGALNTVAVSLMKI 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 250 AIEIRNLQ---RTEIGEVEEPfkKGQLGSSAVPVKRNPIKSERVSSL-ARILRSFSNIAqenislwherdlSNSANERFT 325
Cdd:PLN00134 284 ANDIRLLGsgpRCGLGELNLP--ENEPGSSIMPGKVNPTQCEALTMVcAQVMGNHVAIT------------VGGSAGHFE 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 326 I----PM-------GIILLDEMVNSM-IKVIEGLTVNRQKIldninktkgriyAEFILEA--LVKKGIPRMkAYDNIQRV 391
Cdd:PLN00134 350 LnvfkPLiaynllhSIRLLGDASASFrKNCVRGIEANRERI------------SKLLHESlmLVTALNPKI-GYDKAAAV 416

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 262089311 392 AFQTLAEDKNFKEAIIqdtSIGSnLNMNELRKIFDPNNHLAASTKI 437
Cdd:PLN00134 417 AKKAHKEGTTLKEAAL---KLGV-LTAEEFDELVVPEKMTGPSDLP 458
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 105-426 1.44e-06

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: 50.21  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 105 NDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKKR 184
Cdd:cd01357  137 NDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARER 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 185 FLLCkTLG--VVGTG--SLMGSRALAVQKdVAKSLGLYSVEA-----ATQVIprESLAEVQFIISLVGCTLDKIAIEIRN 255
Cdd:cd01357  217 LREV-NLGgtAIGTGinAPPGYIELVVEK-LSEITGLPLKRAenlidATQNT--DAFVEVSGALKRLAVKLSKIANDLRL 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 256 LQ---RTEIGEVEEPFKkgQLGSSAVPVKRNPIKSERVSSLArilrsFSNIAQenislwherDLS-NSANER-------- 323
Cdd:cd01357  293 LSsgpRAGLGEINLPAV--QPGSSIMPGKVNPVIPEVVNQVA-----FQVIGN---------DLTiTMAAEAgqlelnvf 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 324 -----FTIPMGIILLDEMVNSMI-KVIEGLTVNRQKILDNINKTKGriyaefILEALVkkgiPRMkAYDNIQRVAFQTLA 397
Cdd:cd01357  357 epviaYNLLESIDILTNAVRTLReRCIDGITANEERCREYVENSIG------IVTALN----PYI-GYEAAAEIAKEALE 425

                        330       340
                 ....*....|....*....|....*....
gi 262089311 398 EDKNFKEAIIQDTsigsNLNMNELRKIFD 426
Cdd:cd01357  426 TGRSVRELVLEEG----LLTEEELDEILS 450
PLN02646 PLN02646
argininosuccinate lyase
 98-424 1.03e-05

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 47.80  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311  98 IHYGLTSNDVVDTSTSMQLRDAFEIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIIsfglkfaVWANELSLHIER 177
Cdd:PLN02646 117 LHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPV-------LLSHWLLSHVEQ 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 178 IEEGKKRFLLCK---TLGVVGTGSLMGSrALAVQKD-VAKSLGL-----YSVEAatqVIPRESLAEVQFIISLVGCTLDK 248
Cdd:PLN02646 190 LERDAGRLVDCRprvNFCPLGSCALAGT-GLPIDRFmTAKDLGFtapmrNSIDA---VSDRDFVLEFLFANSITAIHLSR 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 249 IAIEIRNLQRTEIGEVeEPFKKGQLGSSAVPVKRNPIKSERV-SSLARILRSFSNIAQ--ENISLWHERDLSNSAnerft 325
Cdd:PLN02646 266 LGEEWVLWASEEFGFV-TPSDAVSTGSSIMPQKKNPDPMELVrGKSARVIGDLVTVLAlcKGLPTAYNRDLQEDK----- 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 326 ipmgIILLD--EMVNSMIKVIEG----LTVNRQKILDNInkTKGRIYAEFILEALVKKGIPRMKAYDNIQR-VAfqtLAE 398
Cdd:PLN02646 340 ----EPLFDsvDTVSDMLEVATEfaqnITFNPERIKKSL--PAGMLDATTLADYLVRKGVPFRETHHIVGAaVA---LAE 410

                        330       340
                 ....*....|....*....|....*.
gi 262089311 399 DKNFKEaiiqdtsigSNLNMNELRKI 424
Cdd:PLN02646 411 SKGCEL---------SDLTLEDLKSI 427
PRK12425 PRK12425
class II fumarate hydratase;
103-294 2.29e-04

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 43.37  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 103 TSNDVVDTSTSMQLRDAF-EIIEPKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEG 181
Cdd:PRK12425 137 SSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 182 -KKRFLLCKTLGVVGTG-SLMGSRALAVQKDVAKSLGLYSVEAATQ---VIPRESLAEVQFIISLVGCTLDKIAIEIRNL 256
Cdd:PRK12425 217 lPAVCELAQGGTAVGTGlNAPHGFAEAIAAELAALSGLPFVTAPNKfaaLAGHEPLVSLSGALKTLAVALMKIANDLRLL 296

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 262089311 257 ---QRTEIGEVEEPfkKGQLGSSAVPVKRNPIKSERVSSLA 294
Cdd:PRK12425 297 gsgPRAGLAEVRLP--ANEPGSSIMPGKVNPTQCEALSMLA 335
PRK06389 PRK06389
argininosuccinate lyase; Provisional
 102-424 3.01e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235791 [Multi-domain]  Cd Length: 434  Bit Score: 39.88  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 102 LTSNDVVDTSTSMQLRDAFEIIEpKISKLISLILNKAKTYSTLPsvGRTHGQHASIISFGLKFAVWANELSLHIERIEeg 181
Cdd:PRK06389 104 LSRNEQVHADLNLFIIDKIIEIE-KILYEIIKVIPGFNLKGRLP--GYTHFRQAMPMTVNTYINYIKSILYHHINNLD-- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 182 kkRFLLCKTLGVVGTGSLMGSRALAVQKDVAKSLGLYSVEA----ATQVIPReSLAEVQFIISLVGCTLDKIAIEIRNLQ 257
Cdd:PRK06389 179 --SFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKnpvySSSLYIK-TIENISYLISSLAVDLSRICQDIIIYY 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 258 RTEIGEVEEPFKKGqlgSSAVPVKRNPIKSERVSSLARI---LRSFSNIAQENISLWHERDLSnsanerftipmgiILLD 334
Cdd:PRK06389 256 ENGIITIPDEFTTG---SSLMPNKRNPDYLELFQGIAAEsisVLSFIAQSELNKTTGYHRDFQ-------------IVKD 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 335 EMVnSMIKVIEGLTVNRQKILDNIN-------KTKGRIYAEFILEALVKKGIPRMKAYDNIQRvafqTLAEDKNFKEAII 407
Cdd:PRK06389 320 STI-SFINNFERILLGLPDLLYNIKfeitnekNIKNSVYATYNAWLAFKNGMDWKSAYAYIGN----KIREGEVLDEYQP 394

                        330
                 ....*....|....*..
gi 262089311 408 QDTSigSNLNMNELRKI 424
Cdd:PRK06389 395 EDLT--DYIDVNELKRI 409
aspA PRK12273
aspartate ammonia-lyase; Provisional
 125-294 3.21e-03

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 39.72  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 125 PKISKLISLILNKAKTYSTLPSVGRTHGQHASIISFGLKFAVWANELSLHIERIEEGKKRfLLCKTLG--VVGTG--SLM 200
Cdd:PRK12273 164 DALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAEL-LREVNLGatAIGTGlnAPP 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089311 201 GSRALAVQKdVAKSLGLYSVEA-----ATQVIprESLAEVQFIISLVGCTLDKIAIEIRNLQ---RTEIGEVEEPfkKGQ 272
Cdd:PRK12273 243 GYIELVVEK-LAEITGLPLVPAedlieATQDT--GAFVEVSGALKRLAVKLSKICNDLRLLSsgpRAGLNEINLP--AVQ 317

                        170       180
                 ....*....|....*....|..
gi 262089311 273 LGSSAVPVKRNPIKSERVSSLA 294
Cdd:PRK12273 318 AGSSIMPGKVNPVIPEVVNQVC 339
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH