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Conserved domains on  [gi|510997737|ref|WP_016265578|]
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adenylosuccinate lyase [Latilactobacillus sakei]

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

CATH:  1.10.275.10|1.10.40.30|1.20.200.10
EC:  4.3.2.2
Gene Ontology:  GO:0004018|GO:0006188|GO:0009152
PubMed:  10673438
SCOP:  4001433

Graphical summary

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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 ...
 4-381 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: 650.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   4 RYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANASFDVEEINRLEAITHHDVVAFTRAVSESLGA 83
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  84 EKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKR 163
Cdd:cd01360   81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 164 NQERFERAAAGVEAGKISGAVGTFANISPEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRHL 243
Cdd:cd01360  161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 244 QRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILLDYI 323
Cdd:cd01360  241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510997737 324 LNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTAL 381
Cdd:cd01360  321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQREYYL 378
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 349-429 4.57e-33

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: 119.48  E-value: 4.57e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   349 HGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWDEQKDFRQLLEADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80


                   .
gi 510997737   429 F 429
Cdd:smart00998  81 L 81
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 4-381 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: 650.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   4 RYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANASFDVEEINRLEAITHHDVVAFTRAVSESLGA 83
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  84 EKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKR 163
Cdd:cd01360   81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 164 NQERFERAAAGVEAGKISGAVGTFANISPEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRHL 243
Cdd:cd01360  161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 244 QRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILLDYI 323
Cdd:cd01360  241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510997737 324 LNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTAL 381
Cdd:cd01360  321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQREYYL 378
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 1-428 0e+00

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 613.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   1 MLE-RYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANAS---FDVEEINRLEAITHHDVVAFTRA 76
Cdd:COG0015    1 LISpRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADdfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  77 VSESLGAE-KKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLA 155
Cdd:COG0015   81 LKEKVGAEaGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 156 TWYAEMKRNQERFERAAAGVEAGKISGAVGTFANIS---PEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATS 232
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 233 IEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERII 312
Cdd:COG0015  241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 313 LPDTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWDEQKDFRQL 392
Cdd:COG0015  321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 510997737 393 LEADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:COG0015  401 LAADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 1-428 0e+00

adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273345 [Multi-domain]  Cd Length: 435  Bit Score: 532.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737    1 MLERYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANASFDVEEINRL---EAITHHDVVAFTRAV 77
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIkeiEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   78 SESLGAEKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATW 157
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  158 YAEMKRNQERFERAAAGVEAGKISGAVGTFANISP---EIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  235 HFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  315 DTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWD-EQKDFRQLL 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEvDEPDLLEFL 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 510997737  394 EADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 225-418 2.05e-88

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 267.66  E-value: 2.05e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 225 TMAVVATSIEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDIS 304
Cdd:PRK08937  22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 305 HSSAERIILPDTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWD 384
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWK 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 510997737 385 EQKDFRQLLEADPKVMAQLTPAEMDDAFDYHWHL 418
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
Lyase_1 pfam00206
Lyase;
3-286 2.92e-73

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 232.26  E-value: 2.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737    3 ERYT--RPEMGAIWTTENRYQAWLEVE-----ILAVEAWAKLGDIPAEDAAKVRANA-----SFDVEEINRLEAITHHDV 70
Cdd:pfam00206   1 GRFTvpADALMGIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKALdevaeEGKLDDQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   71 VAFTRAVSESLG-------AEKKWVHYGLTSTDVVDTAQGYILKQAN-DLIRADIERFMAVLKQKAYEYQNTVMIGRTHG 142
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  143 VHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG--AVGTFANISPEIEAYVTENLG------IRAQDISTQVL 214
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510997737  215 PRDLHADYINTMAVVATSIEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRG 286
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 349-429 4.57e-33

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: 119.48  E-value: 4.57e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   349 HGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWDEQKDFRQLLEADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80


                   .
gi 510997737   429 F 429
Cdd:smart00998  81 L 81
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 350-428 2.72e-23

Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.


Pssm-ID: 463073 [Multi-domain]  Cd Length: 78  Bit Score: 92.86  E-value: 2.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  350 GLIYSQRVLLKLVdSGLSREAAYDLVQPKTALAWDEQK-DFRQLLEADPKVMAqLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:pfam10397   1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEEGKnDLRELLAADPEVTY-LSEEELDALFDPAYYLGRADEIVDRV 78
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 4-381 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: 650.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   4 RYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANASFDVEEINRLEAITHHDVVAFTRAVSESLGA 83
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  84 EKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKR 163
Cdd:cd01360   81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 164 NQERFERAAAGVEAGKISGAVGTFANISPEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRHL 243
Cdd:cd01360  161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 244 QRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILLDYI 323
Cdd:cd01360  241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510997737 324 LNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTAL 381
Cdd:cd01360  321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQREYYL 378
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 1-428 0e+00

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 613.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   1 MLE-RYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANAS---FDVEEINRLEAITHHDVVAFTRA 76
Cdd:COG0015    1 LISpRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADdfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  77 VSESLGAE-KKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLA 155
Cdd:COG0015   81 LKEKVGAEaGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 156 TWYAEMKRNQERFERAAAGVEAGKISGAVGTFANIS---PEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATS 232
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 233 IEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERII 312
Cdd:COG0015  241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 313 LPDTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWDEQKDFRQL 392
Cdd:COG0015  321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 510997737 393 LEADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:COG0015  401 LAADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 1-428 0e+00

adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273345 [Multi-domain]  Cd Length: 435  Bit Score: 532.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737    1 MLERYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANASFDVEEINRL---EAITHHDVVAFTRAV 77
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIkeiEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   78 SESLGAEKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATW 157
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  158 YAEMKRNQERFERAAAGVEAGKISGAVGTFANISP---EIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  235 HFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  315 DTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWD-EQKDFRQLL 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEvDEPDLLEFL 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 510997737  394 EADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 10-381 6.41e-180

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: 506.66  E-value: 6.41e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  10 MGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANA---SFDVEEINRLEAITHHDVVAFTRAVSESLGAE-K 85
Cdd:cd01595    1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAAdvfEIDAERIAEIEKETGHDVIAFVYALAEKCGEDaG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  86 KWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQ 165
Cdd:cd01595   81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 166 ERFERAAAGVEAGKISGAVGTFANIS---PEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRH 242
Cdd:cd01595  161 ERLEEARERVLVGGISGAVGTHASLGpkgPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 243 LQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILLDY 322
Cdd:cd01595  241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 510997737 323 ILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTAL 381
Cdd:cd01595  321 ALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKEENYL 379
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 5-428 4.65e-115

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: 343.84  E-value: 4.65e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   5 YTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANA---SFDVEEINRLEAITHHDVVAFTRAVSESL 81
Cdd:cd01597    6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAAdveRLDLEALAEATARTGHPAIPLVKQLTAAC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  82 GAE-KKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAE 160
Cdd:cd01597   86 GDAaGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 161 MKRNQERFERAAAGVEAGKISGAVGTFANIS---PEIEAYVTENLGIRAQDISTQVLpRDLHADYINTMAVVATSIEHFA 237
Cdd:cd01597  166 LLRHRERLDELRPRVLVVQFGGAAGTLASLGdqgLAVQEALAAELGLGVPAIPWHTA-RDRIAELASFLALLTGTLGKIA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 238 TEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTT 317
Cdd:cd01597  245 RDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIF 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 318 ILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSgLSREAAYDLVQPKTALAWDEQKDFRQLLEADP 397
Cdd:cd01597  325 LLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRAVEEGRPLREVLLEDP 403

                        410       420       430
                 ....*....|....*....|....*....|.
gi 510997737 398 KVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:cd01597  404 EVAAYLSDEELDALLDPANYLGSAPALVDRV 434
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 20-336 9.33e-110

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: 326.00  E-value: 9.33e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  20 YQAWLEVEILAVEAWAKLGDIPAEDAAKVRANASFDVEEINR----LEAITHHDVVAFTRAVSESLGAE-KKWVHYGLTS 94
Cdd:cd01334    1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAAdqveQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  95 TDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAG 174
Cdd:cd01334   81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 175 VEAGKI-SGAVGTFANISPEIEAYVTENLGI-RAQDISTQ-VLPRDLHADYINTMAVVATSIEHFATEIRHLQRTEVREV 251
Cdd:cd01334  161 LNVLPLgGGAVGTGANAPPIDRERVAELLGFfGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 252 EEFFAKgQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILLDYILNRFTRII 331
Cdd:cd01334  241 ELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319


                 ....*
gi 510997737 332 EKLTV 336
Cdd:cd01334  320 EGLEV 324
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 225-418 2.05e-88

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 267.66  E-value: 2.05e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 225 TMAVVATSIEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDIS 304
Cdd:PRK08937  22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 305 HSSAERIILPDTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWD 384
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWK 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 510997737 385 EQKDFRQLLEADPKVMAQLTPAEMDDAFDYHWHL 418
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
Lyase_1 pfam00206
Lyase;
3-286 2.92e-73

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 232.26  E-value: 2.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737    3 ERYT--RPEMGAIWTTENRYQAWLEVE-----ILAVEAWAKLGDIPAEDAAKVRANA-----SFDVEEINRLEAITHHDV 70
Cdd:pfam00206   1 GRFTvpADALMGIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKALdevaeEGKLDDQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   71 VAFTRAVSESLG-------AEKKWVHYGLTSTDVVDTAQGYILKQAN-DLIRADIERFMAVLKQKAYEYQNTVMIGRTHG 142
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  143 VHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG--AVGTFANISPEIEAYVTENLG------IRAQDISTQVL 214
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510997737  215 PRDLHADYINTMAVVATSIEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRG 286
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 3-375 1.76e-64

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: 213.33  E-value: 1.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   3 ERYTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLG-DIPAEDAAKVRANAS-FDVEEINRLEAITHHDVVAFTRAVSES 80
Cdd:cd03302    3 SRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGlDISDEQIEEMKANVEnIDFEIAAAEEKKLRHDVMAHVHAFGLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  81 LGAEKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAE 160
Cdd:cd03302   83 CPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 161 MKRNQERFERAAAGVEAGKISGAVGTFANI----------SPEIEAYVTENLGI-RAQDISTQVLPRDLHADYINTMAVV 229
Cdd:cd03302  163 LLMDLRNLERLRDDLRFRGVKGTTGTQASFldlfegdhdkVEALDELVTKKAGFkKVYPVTGQTYSRKVDIDVLNALSSL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 230 ATSIEHFATEIRHLQRTEvrEVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSL-WHERDISHSSA 308
Cdd:cd03302  243 GATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTqWFERTLDDSAN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510997737 309 ERIILPDTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSGLSREAAYDLV 375
Cdd:cd03302  321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERI 387
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 5-428 3.19e-63

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


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 210.26  E-value: 3.19e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   5 YTRPEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRAN---ASFDVEEINRLEAITHHD----VVAFTRAV 77
Cdd:PRK09053  12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAAcdaERLDLDALAQAAALAGNLaiplVKQLTAQV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  78 SESLGAEKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATW 157
Cdd:PRK09053  92 AARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGW 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 158 YAEMKRNQERFERAAAGVEAGKISGAVGTFANI----SPEIEAYVTE-NLGIRAQDISTQvlpRDLHADYINTMAVVATS 232
Cdd:PRK09053 172 LDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqaLPVAQALAAElQLALPALPWHTQ---RDRIAEFASALGLLAGT 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 233 IEHFATEIRHLQRTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERII 312
Cdd:PRK09053 249 LGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWHAEWDT 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 313 LPDTTILLDYILNRFTRIIEKLTVFPEKMKADMNLTHGLIYSQRVLLKLVDSgLSREAAYDLVQPKTALAWDEQKDFRQL 392
Cdd:PRK09053 329 LPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADR-IGRLDAHHLVEQASKRAVAEGRHLRDV 407

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 510997737 393 LEADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:PRK09053 408 LAEDPQVSAHLSPAALDRLLDPAHYLGQAHAWVDRV 443
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 85-328 4.69e-54

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: 179.73  E-value: 4.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  85 KKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRN 164
Cdd:cd01594   34 SALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVLGRD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 165 QERFERAAagveagkisgavgtfanispeieayvtenlgiraqdistqvlprdlHADYINTMAVVATSIEHFATEIRHLQ 244
Cdd:cd01594  114 LERLEEAA----------------------------------------------VAEALDALALAAAHLSKIAEDLRLLL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 245 RTEVREVEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILLDYIL 324
Cdd:cd01594  148 SGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSPSMREILADSLLLLIDAL 227


                 ....
gi 510997737 325 NRFT 328
Cdd:cd01594  228 RLLL 231
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 8-334 5.07e-48

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: 167.23  E-value: 5.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737    8 PEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKVRANAS---FDVEEINRLEAITHHDVVAFTRAVSESLGAE 84
Cdd:TIGR02426   9 PAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAaaaPDLEALAHAAATAGNPVIPLVKALRKAVAGE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   85 -KKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKR 163
Cdd:TIGR02426  89 aARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAAVLR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  164 NQERFERAAAGVEAGKISGAVGTFANISP---EIEAYVTENLGIRAQDISTQVLpRDLHADYINTMAVVATSIEHFATEI 240
Cdd:TIGR02426 169 ARDRLAALRTRALPLQFGGAAGTLAALGTrggAVAAALAARLGLPLPALPWHTQ-RDRIAEFGSALALVAGALGKIAGDI 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  241 RHLQRTEVrevEEFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVITGMEDVSLWHERDISHSSAERIILPDTTILL 320
Cdd:TIGR02426 248 ALLSQTEV---GEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPELVRLT 324

                         330
                  ....*....|....
gi 510997737  321 DYILNRFTRIIEKL 334
Cdd:TIGR02426 325 GGALRQAQVLAEGL 338
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 24-346 5.43e-38

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: 142.37  E-value: 5.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  24 LEVEILAVEAWAKLGDIP------AEDAAKVRA-----NASfDVEEINRLEAITHHDVVA---FTR---AVSESLGAEKK 86
Cdd:cd01598   15 VQVEVEWLIALSNLEEIPevppltKEELKFLRAiienfSEE-DALRIKEIEATTNHDVKAveyFLKekfETLGLLKKIKE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  87 WVHYGLTSTDVVDTAQGYILKQA-NDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQ 165
Cdd:cd01598   94 FIHFACTSEDINNLAYALMIKEArNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQY 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 166 ERFERAaagVEAGKISGAVGTFA-------NIS-PEIEAYVTENLGIRAQDISTQVLPRDLHADYINTMAVVATSIEHFA 237
Cdd:cd01598  174 KQLKQI---EILGKFNGAVGNFNahlvaypDVDwRKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALARINTILIDLC 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 238 TEI------RHLQRTevreveefFAKGQKGSSAMPHKRNPISSENVSG---LARVIRGHVITGMEdVSLWhERDISHSSA 308
Cdd:cd01598  251 RDIwgyislGYFKQK--------VKKGEVGSSTMPHKVNPIDFENAEGnlgLSNALLNHLSAKLP-ISRL-QRDLTDSTV 320

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 510997737 309 ERII-LPDTTILLDYilNRFTRIIEKLTVFPEKMKADMN 346
Cdd:cd01598  321 LRNIgVAFGHSLIAY--KSLLRGLDKLELNEARLLEDLD 357
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 18-346 3.35e-36

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 137.96  E-value: 3.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  18 NRYQAWLEVEIL-AVEAWAKLGDIPAEDAAKVRA----NASFDVEEINR---LEAITHHDVVA---FTR---AVSESLGA 83
Cdd:PRK09285  33 IRYRVQVEVEWLiALAAHPGIPEVPPFSAEANAFlraiVENFSEEDAARikeIERTTNHDVKAveyFLKeklAGLPELEA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  84 EKKWVHYGLTSTDVVDTAQGYILKQA-NDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMK 162
Cdd:PRK09285 113 VSEFIHFACTSEDINNLSHALMLKEArEEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 163 RNQERFEraaaGVE-AGKISGAVGTF-ANIS--PEI------EAYVtENLGIRAQDISTQVLPRDLHADYINTMAVVATS 232
Cdd:PRK09285 193 RQLKQLE----AVEiLGKINGAVGNYnAHLAayPEVdwhafsREFV-ESLGLTWNPYTTQIEPHDYIAELFDAVARFNTI 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 233 IEHFATEI------RHL-QRTEVREVeeffakgqkGSSAMPHKRNPISSENVSG---LARVIRGHVITGMEdVSLWhERD 302
Cdd:PRK09285 268 LIDLDRDVwgyislGYFkQKTKAGEI---------GSSTMPHKVNPIDFENSEGnlgLANALLEHLAAKLP-ISRW-QRD 336

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 510997737 303 IShssaeriilpDTTIL------LDYIL---NRFTRIIEKLTVFPEKMKADMN 346
Cdd:PRK09285 337 LT----------DSTVLrnlgvaFGYSLiayDSLLKGLGKLEVNEARLAEDLD 379
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 349-429 4.57e-33

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: 119.48  E-value: 4.57e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   349 HGLIYSQRVLLKLVDSGLSREAAYDLVQPKTALAWDEQKDFRQLLEADPKVMAQLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:smart00998   1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRV 80


                   .
gi 510997737   429 F 429
Cdd:smart00998  81 L 81
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 8-314 1.59e-26

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 109.37  E-value: 1.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737   8 PEMGAIWTTENRYQAWLEVEILAVEAWAKLGDIPAEDAAKV-RANASF--DVEEINRLEAITHHDVVAFTRAVSESLGAE 84
Cdd:PRK05975  18 DEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIaAACETFepDLAALRHATARDGVVVPALVRQLRAAVGEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  85 -KKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEY-QNTVMiGRTHGVHAEPTTFGLKLATWYAEMK 162
Cdd:PRK05975  98 aAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFgQNALM-GHTRMQAAIPITVADRLASWRAPLL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 163 RNQERFERAAAGVEAGKISGAVGTFANISPE---IEAYVTENLGI--RAQDISTqvlpRDLHADYINTMAVVATSIEHFA 237
Cdd:PRK05975 177 RHRDRLEALRADVFPLQFGGAAGTLEKLGGKaaaVRARLAKRLGLedAPQWHSQ----RDFIADFAHLLSLVTGSLGKFG 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 238 TEIRHL--QRTEVReveeffAKGQKGSSAMPHKRNPISSENVSGLARVIRGHViTGMEDvSLWHERDISHS--SAERIIL 313
Cdd:PRK05975 253 QDIALMaqAGDEIS------LSGGGGSSAMPHKQNPVAAETLVTLARFNATQV-SGLHQ-ALVHEQERSGAawTLEWMIL 324


                 .
gi 510997737 314 P 314
Cdd:PRK05975 325 P 325
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 350-428 2.72e-23

Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.


Pssm-ID: 463073 [Multi-domain]  Cd Length: 78  Bit Score: 92.86  E-value: 2.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  350 GLIYSQRVLLKLVdSGLSREAAYDLVQPKTALAWDEQK-DFRQLLEADPKVMAqLTPAEMDDAFDYHWHLSQVQTIFDRV 428
Cdd:pfam10397   1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEEGKnDLRELLAADPEVTY-LSEEELDALFDPAYYLGRADEIVDRV 78
PLN02848 PLN02848
adenylosuccinate lyase
 55-348 1.82e-21

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 95.96  E-value: 1.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  55 DVEEINRLEAITHHDVVA---FTRAVSES---LGAEKKWVHYGLTSTDVVDTAQGYILKQA-NDLIRADIERFMAVLKQK 127
Cdd:PLN02848  81 DALEVKKIERVTNHDVKAveyFLKQKCKShpeLAKVLEFFHFACTSEDINNLSHALMLKEGvNSVVLPTMDEIIKAISSL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 128 AYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRnqERFERAAAGVEaGKISGAVGTF-ANIS--PEI------EAYV 198
Cdd:PLN02848 161 AHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSR--QRKQLSEVKIK-GKFAGAVGNYnAHMSayPEVdwpavaEEFV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 199 TeNLGIRAQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRHL-------QRTEVREVeeffakgqkGSSAMPHKRNP 271
Cdd:PLN02848 238 T-SLGLTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWSYislgyfkQITKAGEV---------GSSTMPHKVNP 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 272 ISSENVSG---LARVIRGHVITGMEdVSLWhERDISHSSAER---------IILPDTTIlldyilnrftRIIEKLTVFPE 339
Cdd:PLN02848 308 IDFENSEGnlgLANAELSHLSMKLP-ISRM-QRDLTDSTVLRnmgvglghsLLAYKSTL----------RGIGKLQVNEA 375


                 ....*....
gi 510997737 340 KMKADMNLT 348
Cdd:PLN02848 376 RLAEDLDQT 384
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 35-289 5.66e-15

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: 76.43  E-value: 5.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  35 AKLGDIPAEDAAK-------VRANASFDVEEIN-RLEAItHHdvvAFTRAVSESLGAEKKWVHYGLTSTDVVDTAQGYIL 106
Cdd:cd01359   24 AEQGILTEEEAAKilaglakIRAEIEAGAFELDpEDEDI-HM---AIERRLIERIGDVGGKLHTGRSRNDQVATDLRLYL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 107 KQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGVE---AGkiSGA 183
Cdd:cd01359  100 RDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAYKRVNvspLG--AGA 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 184 -VGTFANISPEieaYVTENLG---IRAQDISTqVLPRDLHADYINTMAVVATSIEHFATEIrHLQRTevrevEEF----- 254
Cdd:cd01359  178 lAGTTFPIDRE---RTAELLGfdgPTENSLDA-VSDRDFVLEFLSAAALLMVHLSRLAEDL-ILWST-----QEFgfvel 247

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 510997737 255 ---FAkgqKGSSAMPHKRNPISSEnvsgLARVIRGHVI 289
Cdd:cd01359  248 pdaYS---TGSSIMPQKKNPDVLE----LIRGKAGRVI 278
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 75-414 5.34e-12

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 67.10  E-value: 5.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  75 RAVSESLGAEKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKL 154
Cdd:PRK00855  92 ARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 155 ATWYAEMKRNQERFERAAAGVEA---GkiSGA-VGTFANISPEieaYVTENLGIRAQDIST--QVLPRDLHADYINTMAV 228
Cdd:PRK00855 172 LAYAEMLARDLERLRDARKRVNRsplG--SAAlAGTTFPIDRE---RTAELLGFDGVTENSldAVSDRDFALEFLSAASL 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 229 VATSIEHFATEIRHLQRTEVREVE--EFFAkgqKGSSAMPHKRNPISSENVSG-LARVIrGH---VITGMEDVSLWHERD 302
Cdd:PRK00855 247 LMVHLSRLAEELILWSSQEFGFVElpDAFS---TGSSIMPQKKNPDVAELIRGkTGRVY-GNltgLLTVMKGLPLAYNRD 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 303 IshSSAERIILP--DTTILLdyiLNRFTRIIEKLTVFPEKMKADmnLTHGLIYSQRVLLKLVDSGLS-REaAYDLVQPKT 379
Cdd:PRK00855 323 L--QEDKEPLFDavDTLKLS---LEAMAGMLETLTVNKERMREA--AGKGFSTATDLADYLVRKGVPfRE-AHEIVGKAV 394

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 510997737 380 ALAWDEQKDFRQLLEADpkvMAQLTPAEMDDAFDY 414
Cdd:PRK00855 395 REAEERGVDLADLSLEE---LQAFSPLITEDVYEV 426
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 94-292 1.66e-11

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: 65.52  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  94 STDVVDTAQGYI--LKQANDLIRAdIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERA 171
Cdd:cd01596  135 SNDDFPPAAHIAaaLALLERLLPA-LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAA 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 172 AAGVEAGKISG-AVGTFANISPEIEAYVTENL----GI---RAQDI--STQVlprdlHADYINTMAV---VATSIEHFAT 238
Cdd:cd01596  214 LERLRELNLGGtAVGTGLNAPPGYAEKVAAELaeltGLpfvTAPNLfeATAA-----HDALVEVSGAlktLAVSLSKIAN 288

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510997737 239 EIRHLQ---RTEVREVEefFAKGQKGSSAMPHKRNPISSENVSGLA-RVIRGHVITGM 292
Cdd:cd01596  289 DLRLLSsgpRAGLGEIN--LPANQPGSSIMPGKVNPVIPEAVNMVAaQVIGNDTAITM 344
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 70-292 2.42e-11

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: 65.21  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  70 VVAfTRAvSESLG---AEKKWVH------YGLTSTDVVDTAQgYI---LKQANDLIRAdIERFMAVLKQKAYEYQNTVMI 137
Cdd:cd01362  105 VIA-NRA-IELLGgvlGSKKPVHpndhvnMSQSSNDTFPTAM-HIaaaLALQERLLPA-LKHLIDALDAKADEFKDIVKI 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 138 GRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG-AVGTFANISPEIEAYVTENL-------------- 202
Cdd:cd01362  181 GRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGtAVGTGLNAHPGFAEKVAAELaeltglpfvtapnk 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 203 --GIRAQDISTQVlprdlHADyINTMAVVATSIehfATEIRHLQ---RTEVREVEefFAKGQKGSSAMPHKRNPISSENV 277
Cdd:cd01362  261 feALAAHDALVEA-----SGA-LKTLAVSLMKI---ANDIRWLGsgpRCGLGELS--LPENEPGSSIMPGKVNPTQCEAL 329

                        250
                 ....*....|....*.
gi 510997737 278 SGL-ARVIRGHVITGM 292
Cdd:cd01362  330 TMVaAQVMGNDAAITI 345
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 105-278 1.04e-10

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 63.31  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 105 ILKQANDLIRAdIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG-A 183
Cdd:cd01357  148 LILLLRKLLDA-LAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGtA 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 184 VGTFANISPEIEAYVTENLG-------IRAQDI--STQVLprDLHADYINTMAVVATSIEHFATEIRHLQ---RTEVREV 251
Cdd:cd01357  227 IGTGINAPPGYIELVVEKLSeitglplKRAENLidATQNT--DAFVEVSGALKRLAVKLSKIANDLRLLSsgpRAGLGEI 304

                        170       180
                 ....*....|....*....|....*..
gi 510997737 252 EefFAKGQKGSSAMPHKRNPISSENVS 278
Cdd:cd01357  305 N--LPAVQPGSSIMPGKVNPVIPEVVN 329
fumC PRK00485
fumarate hydratase; Reviewed
 70-275 1.94e-10

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 62.42  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  70 VVAfTRAvSESLGAE---KKWVH------YGLTSTDVVDTAQgYI---LKQANDLIRAdIERFMAVLKQKAYEYQNTVMI 137
Cdd:PRK00485 109 VIA-NRA-SELLGGElgsKKPVHpndhvnMSQSSNDTFPTAM-HIaavLAIVERLLPA-LEHLRDTLAAKAEEFADIVKI 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 138 GRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG-AVGTFANISPEIEAYVTENL-------------- 202
Cdd:PRK00485 185 GRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGtAVGTGLNAHPGFAERVAEELaeltglpfvtapnk 264

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510997737 203 --GIRAQDISTQvlprdLHAdyinTMAVVATSIEHFATEIRHLQ---RTEVREVEefFAKGQKGSSAMPHKRNPISSE 275
Cdd:PRK00485 265 feALAAHDALVE-----ASG----ALKTLAVSLMKIANDIRWLAsgpRCGLGEIS--LPENEPGSSIMPGKVNPTQCE 331
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 94-284 1.69e-08

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 56.53  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  94 ST-DVVDTAqGYI--LKQANDLIRAdIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFER 170
Cdd:PRK13353 140 STnDVFPTA-IRIaaLNLLEGLLAA-MGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 171 AAAGVEAGKISG-AVGTFANISPEIEAYVTENLG-------IRAQDI--STQVLprDLHADYINTMAVVATSIEHFATEI 240
Cdd:PRK13353 218 AREHLYEVNLGGtAVGTGLNADPEYIERVVKHLAaitglplVGAEDLvdATQNT--DAFVEVSGALKVCAVNLSKIANDL 295

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 510997737 241 RHLQ---RTEVREVeeFFAKGQKGSSAMPHKRNPISSENVSGLA-RVI 284
Cdd:PRK13353 296 RLLSsgpRTGLGEI--NLPAVQPGSSIMPGKVNPVMPEVVNQIAfQVI 341
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 68-281 4.13e-06

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 48.84  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  68 HDVVAfTRAVsESLGAEKKWVHY---------GLTSTDVVDTA-QGYILKQANDLIRAdIERFMAVLKQKAYEYQNTVMI 137
Cdd:PRK14515 114 NEVIA-NRAL-ELLGMEKGDYHYispnshvnmAQSTNDAFPTAiHIATLNALEGLLQT-MGYMHDVFELKAEQFDHVIKM 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 138 GRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGV-EAGKISGAVGTFANISPE-IEAYVTENLGIR------AQDI 209
Cdd:PRK14515 191 GRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLyEVNMGATAVGTGLNADPEyIEAVVKHLAAISelplvgAEDL 270

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510997737 210 STQVLPRDLHADYINTMAVVATSIEHFATEIRHLQ---RTEVREVeeFFAKGQKGSSAMPHKRNPISSENVSGLA 281
Cdd:PRK14515 271 VDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMAsgpRVGLAEI--MLPARQPGSSIMPGKVNPVMPEVINQIA 343
PLN00134 PLN00134
fumarate hydratase; Provisional
 124-275 2.85e-05

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 46.22  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 124 LKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG-AVGT----FANISPEIEAYV 198
Cdd:PLN00134 163 LRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGtAVGTglntKKGFDEKIAAAV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 199 TENLG---IRAQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRHLQ---RTEVREVEefFAKGQKGSSAMPHKRNPI 272
Cdd:PLN00134 243 AEETGlpfVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGsgpRCGLGELN--LPENEPGSSIMPGKVNPT 320


                 ...
gi 510997737 273 SSE 275
Cdd:PLN00134 321 QCE 323
PLN02646 PLN02646
argininosuccinate lyase
 75-414 4.24e-05

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 45.49  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  75 RAVSESLGAEKKWVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKL 154
Cdd:PLN02646 104 ARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 155 ATWYAEMKRNQERFERAAAGVEAGKI-SGAV-GTFANISPEIEAyvtENLGIraqdisTQVLPRDLHA----DYintmaV 228
Cdd:PLN02646 184 LSHVEQLERDAGRLVDCRPRVNFCPLgSCALaGTGLPIDRFMTA---KDLGF------TAPMRNSIDAvsdrDF-----V 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 229 VATSIEHFATEIrHLQRTE----VREVEEF-FAKGQ----KGSSAMPHKRNPISSENVSGLARVIRGH---VITGMEDVS 296
Cdd:PLN02646 250 LEFLFANSITAI-HLSRLGeewvLWASEEFgFVTPSdavsTGSSIMPQKKNPDPMELVRGKSARVIGDlvtVLALCKGLP 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 297 LWHERDISHssaERIILPDTTILLDYILNRFTRIIEKLTVFPEKMKAdmNLTHGLIYSQRVLLKLVDSGLSREAAYDLVQ 376
Cdd:PLN02646 329 TAYNRDLQE---DKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKK--SLPAGMLDATTLADYLVRKGVPFRETHHIVG 403

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 510997737 377 PKTALAWDEQKDFRQLLEADpkvMAQLTPAEMDDAFDY 414
Cdd:PLN02646 404 AAVALAESKGCELSDLTLED---LKSINPVFEEDVYEV 438
PRK12308 PRK12308
argininosuccinate lyase;
22-279 2.88e-04

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 43.23  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  22 AWLEVEILAVEAWAKLGDIPAEDAAKVRAnasfDVEEINRLEAITHHDVVAftRAVSESLGAEKKWVHYGLTSTDVVDT- 100
Cdd:PRK12308  43 ALLSVGVLSEEEQQKLELALNELKLEVME----DPEQILLSDAEDIHSWVE--QQLIGKVGDLGKKLHTGRSRNDQVATd 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 101 AQGYILKQANDLIRAdIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFglklATW---YAEM-KRNQERFERAAAGVE 176
Cdd:PRK12308 117 LKLWCRQQGQQLLLA-LDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTF----AHWclaYVEMfERDYSRLEDALTRLD 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 177 AGKI-SGAV-GTFANISPEIEAYvteNLGIRAQDIST--QVLPRDlHAdyINTMAVVATSIEHFAteirhlqrtevREVE 252
Cdd:PRK12308 192 TCPLgSGALaGTAYPIDREALAH---NLGFRRATRNSldSVSDRD-HV--MELMSVASISMLHLS-----------RLAE 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 510997737 253 E--FFAKGQ-----------KGSSAMPHKRNPISSENVSG 279
Cdd:PRK12308 255 DliFYNSGEsgfieladtvtSGSSLMPQKKNPDALELIRG 294
aspA PRK12273
aspartate ammonia-lyase; Provisional
 105-284 5.25e-04

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 42.03  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 105 ILKQANDLIRAdIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAAGVEAGKISG-A 183
Cdd:PRK12273 155 LLLSLRKLLDA-LEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGAtA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 184 VGTFANISPEIEAYVTENLG-------IRAQDI--STQvlprDLHAdYINTMAV---VATSIEHFATEIRHLQ---RTEV 248
Cdd:PRK12273 234 IGTGLNAPPGYIELVVEKLAeitglplVPAEDLieATQ----DTGA-FVEVSGAlkrLAVKLSKICNDLRLLSsgpRAGL 308

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 510997737 249 REVEefFAKGQKGSSAMPHKRNPISSENVSGLA-RVI 284
Cdd:PRK12273 309 NEIN--LPAVQAGSSIMPGKVNPVIPEVVNQVCfQVI 343
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 126-290 1.62e-03

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 40.74  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 126 QKAYEYQNTVMIGRTHGVHAEPTTFGLKLATWYAEMKRNQERFERAAagveagkisgavgTFANISPeieayvtenLGIR 205
Cdd:PRK06705 148 QLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTY-------------KLLNQSP---------MGAA 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 206 AQDISTQVLPRDLHADYINTMAVVATSIEHFATEIRHLQRTEV---------REVEEFFAKGQKG-------------SS 263
Cdd:PRK06705 206 ALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLlmvmmtntsRWIHDFLLLATKEydgitvarpyvqiSS 285

                        170       180
                 ....*....|....*....|....*..
gi 510997737 264 AMPHKRNPISSENVSGLARVIRGHVIT 290
Cdd:PRK06705 286 IMPQKRNPVSIEHARAITSSALGEAFT 312
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 77-290 1.98e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 40.60  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737  77 VSESLGAEKK-WVHYGLTSTDVVDTAQGYILKQANDLIRADIERFMAVLKQKAYEYQNTVMIGRTHGVHAEPTTFGLKLA 155
Cdd:PRK02186 498 LIERLGEDVGgVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLL 577

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997737 156 TWYAEMKRNQERFERAAAGVEA---GKISGAvGTFANISPEIEAYVtenLGIRAQDIST--QVLPRDLHADYINTMAVVA 230
Cdd:PRK02186 578 AVDGALARETHALFALFEHIDVcplGAGAGG-GTTFPIDPEFVARL---LGFEQPAPNSldAVASRDGVLHFLSAMAAIS 653

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510997737 231 TSIEHFATEirhLQRTEVREVE--EFFAKGQKGSSAMPHKRNPISSENVSGLARVIRGHVIT 290
Cdd:PRK02186 654 TVLSRLAQD---LQLWTTREFAlvSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALAS 712
 
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.
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