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Conserved domains on  [gi|612673059|gb|EZS89125|]
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adenylosuccinate lyase [Staphylococcus aureus VET0159R]

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 ...
 4-378 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: 658.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   4 RYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKVNVERAQEIEQETRHDVVAFTRQVSETLGE 83
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  84 ERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQR 163
Cdd:cd01360   81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 164 NLQRFKQVREEIEVGKMSGAVGTFANIPPEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLEKFAVEIRNL 243
Cdd:cd01360  161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 244 QKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDYA 323
Cdd:cd01360  241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 612673059 324 LNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPK 378
Cdd:cd01360  321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQRE 375
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 350-429 1.55e-34

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: 123.33  E-value: 1.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   350 GLIFSQRVLLALINKGMVREEAYDKVQPKAMISWETKTPFRELIEQDESITSVLTKEELDECFDPKHHLNQVDTIFERAG 429
Cdd:smart00998   2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 4-378 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: 658.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   4 RYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKVNVERAQEIEQETRHDVVAFTRQVSETLGE 83
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  84 ERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQR 163
Cdd:cd01360   81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 164 NLQRFKQVREEIEVGKMSGAVGTFANIPPEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLEKFAVEIRNL 243
Cdd:cd01360  161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 244 QKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDYA 323
Cdd:cd01360  241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 612673059 324 LNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPK 378
Cdd:cd01360  321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQRE 375
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: 644.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   1 MIE-RYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAK---VNVERAQEIEQETRHDVVAFTRQ 76
Cdd:COG0015    1 LISpRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADdfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  77 VSETLG-EERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMA 155
Cdd:COG0015   81 LKEKVGaEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 156 LWYTEMQRNLQRFKQVREEIEVGKMSGAVGTFANIP---PEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATS 232
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 233 LEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIM 312
Cdd:COG0015  241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 313 LPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPKAMISWETKTPFREL 392
Cdd:COG0015  321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 612673059 393 IEQDESITSVLTKEELDECFDPKHHLNQVDTIFERA 428
Cdd:COG0015  401 LAADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 1-427 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: 566.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059    1 MIERYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNA---KVNVERAQEIEQETRHDVVAFTRQV 77
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKAnftEVDLERIKEIEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   78 SETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALW 157
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  158 YTEMQRNLQRFKQVREEIEVGKMSGAVGTFANIPP---EIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  235 KFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  315 DVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPKAMISWE-TKTPFRELI 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEvDEPDLLEFL 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 612673059  394 EQDESITSVLTKEELDECFDPKHHLNQVDTIFER 427
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVER 434
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 225-418 3.69e-96

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 287.31  E-value: 3.69e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 225 TLALIATSLEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDIS 304
Cdd:PRK08937  22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 305 HSSAERIMLPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPKAMISWE 384
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWK 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 612673059 385 TKTPFRELIEQDESITSVLTKEELDECFDPKHHL 418
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
Lyase_1 pfam00206
Lyase;
3-286 3.40e-87

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 268.08  E-value: 3.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059    3 ERYS--REEMSNIWTDQNRYEAWLEVE-----ILACEAWSELGHIPKADVQKIRQNAKVNVE-----RAQEIEQETRHDV 70
Cdd:pfam00206   1 GRFTvpADALMGIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKALDEVAEegkldDQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   71 VAFTRQVSETLGE-------ERKWVHYGLTSTDVVDTALSFVIKQAN-DIIEKDLERFIDVLAEKAKNYKYTLMMGRTHG 142
Cdd:pfam00206  81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  143 VHAEPTTFGVKMALWYTEMQRNLQRFKQVREEIEVGKMSG--AVGTFANIPPEIESYVCKHLG------IGTAPVSTQTL 214
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612673059  215 QRDRHAYYIATLALIATSLEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRG 286
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 350-429 1.55e-34

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: 123.33  E-value: 1.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   350 GLIFSQRVLLALINKGMVREEAYDKVQPKAMISWETKTPFRELIEQDESITSVLTKEELDECFDPKHHLNQVDTIFERAG 429
Cdd:smart00998   2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 350-428 5.19e-28

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: 105.57  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  350 GLIFSQRVLLALInKGMVREEAYDKVQPKAMISWET-KTPFRELIEQDESITsVLTKEELDECFDPKHHLNQVDTIFERA 428
Cdd:pfam10397   1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEEgKNDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADEIVDRV 78
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 4-378 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: 658.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   4 RYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKVNVERAQEIEQETRHDVVAFTRQVSETLGE 83
Cdd:cd01360    1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAFVTAIAEYCGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  84 ERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQR 163
Cdd:cd01360   81 AGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 164 NLQRFKQVREEIEVGKMSGAVGTFANIPPEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLEKFAVEIRNL 243
Cdd:cd01360  161 HLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIASTLEKIATEIRHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 244 QKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDYA 323
Cdd:cd01360  241 QRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVALWHERDISHSSVERVILPDATILLDYI 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 612673059 324 LNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPK 378
Cdd:cd01360  321 LRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQRE 375
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: 644.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   1 MIE-RYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAK---VNVERAQEIEQETRHDVVAFTRQ 76
Cdd:COG0015    1 LISpRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADdfeIDAERIKEIEKETRHDVKAFVYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  77 VSETLG-EERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMA 155
Cdd:COG0015   81 LKEKVGaEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 156 LWYTEMQRNLQRFKQVREEIEVGKMSGAVGTFANIP---PEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATS 232
Cdd:COG0015  161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGeawPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSALALIAGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 233 LEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIM 312
Cdd:COG0015  241 LEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALASWHERDLSDSSVERNI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 313 LPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPKAMISWETKTPFREL 392
Cdd:COG0015  321 LPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 612673059 393 IEQDESITSVLTKEELDECFDPKHHLNQVDTIFERA 428
Cdd:COG0015  401 LAADPEIPAELSKEELEALFDPANYLGAADEIVDRV 436
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 1-427 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: 566.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059    1 MIERYSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNA---KVNVERAQEIEQETRHDVVAFTRQV 77
Cdd:TIGR00928   1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKAnftEVDLERIKEIEAVTRHDVKAVVYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   78 SETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALW 157
Cdd:TIGR00928  81 KEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  158 YTEMQRNLQRFKQVREEIEVGKMSGAVGTFANIPP---EIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLE 234
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPlveEVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  235 KFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLP 314
Cdd:TIGR00928 241 KFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  315 DVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPKAMISWE-TKTPFRELI 393
Cdd:TIGR00928 321 DAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEvDEPDLLEFL 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 612673059  394 EQDESITSVLTKEELDECFDPKHHLNQVDTIFER 427
Cdd:TIGR00928 401 LEDERITKYLKEEELAELLDPETYIGNAGEIVER 434
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 10-376 0e+00

Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176467 [Multi-domain]  Cd Length: 381  Bit Score: 530.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  10 MSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKV---NVERAQEIEQETRHDVVAFTRQVSETLGEE-R 85
Cdd:cd01595    1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVfeiDAERIAEIEKETGHDVIAFVYALAEKCGEDaG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  86 KWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNL 165
Cdd:cd01595   81 EYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 166 QRFKQVREEIEVGKMSGAVGTFANI---PPEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLEKFAVEIRN 242
Cdd:cd01595  161 ERLEEARERVLVGGISGAVGTHASLgpkGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 243 LQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDY 322
Cdd:cd01595  241 LQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDA 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 612673059 323 ALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQ 376
Cdd:cd01595  321 ALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVK 374
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 5-428 5.19e-127

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: 374.27  E-value: 5.19e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   5 YSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKV---NVERAQEIEQETRHDVVAFTRQVSETL 81
Cdd:cd01597    6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVerlDLEALAEATARTGHPAIPLVKQLTAAC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  82 GEE-RKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTE 160
Cdd:cd01597   86 GDAaGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 161 MQRNLQRFKQVREEIEVGKMSGAVGTFA---NIPPEIESYVCKHLGIGTAPVSTQTlQRDRHAYYIATLALIATSLEKFA 237
Cdd:cd01597  166 LLRHRERLDELRPRVLVVQFGGAAGTLAslgDQGLAVQEALAAELGLGVPAIPWHT-ARDRIAELASFLALLTGTLGKIA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 238 VEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVT 317
Cdd:cd01597  245 RDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIF 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 318 IALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKgMVREEAYDKVQPKAMISWETKTPFRELIEQDE 397
Cdd:cd01597  325 LLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRAVEEGRPLREVLLEDP 403

                        410       420       430
                 ....*....|....*....|....*....|.
gi 612673059 398 SITSVLTKEELDECFDPKHHLNQVDTIFERA 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 1.34e-120

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: 353.73  E-value: 1.34e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  20 YEAWLEVEILACEAWSELGHIPKADVQKIRQNAKVNVER----AQEIEQETRHDVVAFTRQVSETLGEE-RKWVHYGLTS 94
Cdd:cd01334    1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGiaadQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  95 TDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQVREE 174
Cdd:cd01334   81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 175 IEVGKM-SGAVGTFANIPPEIESYVCKHLGI-GTAPVSTQTLQ-RDRHAYYIATLALIATSLEKFAVEIRNLQKTETREV 251
Cdd:cd01334  161 LNVLPLgGGAVGTGANAPPIDRERVAELLGFfGPAPNSTQAVSdRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 252 EEAFAKgQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDYALNRFTNIV 331
Cdd:cd01334  241 ELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319


                 ....*
gi 612673059 332 DRLTV 336
Cdd:cd01334  320 EGLEV 324
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 225-418 3.69e-96

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 287.31  E-value: 3.69e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 225 TLALIATSLEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDIS 304
Cdd:PRK08937  22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWHERDLS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 305 HSSAERIMLPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDKVQPKAMISWE 384
Cdd:PRK08937 102 HSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWK 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 612673059 385 TKTPFRELIEQDESITSVLTKEELDECFDPKHHL 418
Cdd:PRK08937 182 NQKDLRELLEADERFTKQLTKEELDELFDPEAFV 215
Lyase_1 pfam00206
Lyase;
3-286 3.40e-87

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 268.08  E-value: 3.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059    3 ERYS--REEMSNIWTDQNRYEAWLEVE-----ILACEAWSELGHIPKADVQKIRQNAKVNVE-----RAQEIEQETRHDV 70
Cdd:pfam00206   1 GRFTvpADALMGIFTDRSRFNFRLGEEdikglAALKKAAAKANVILKEEAAAIIKALDEVAEegkldDQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   71 VAFTRQVSETLGE-------ERKWVHYGLTSTDVVDTALSFVIKQAN-DIIEKDLERFIDVLAEKAKNYKYTLMMGRTHG 142
Cdd:pfam00206  81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  143 VHAEPTTFGVKMALWYTEMQRNLQRFKQVREEIEVGKMSG--AVGTFANIPPEIESYVCKHLG------IGTAPVSTQTL 214
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGgtAVGTGLNADPEFAELVAKELGfftglpVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612673059  215 QRDRHAYYIATLALIATSLEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRG 286
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 1-415 3.30e-72

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: 233.36  E-value: 3.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   1 MIERYSREEMSNIWTDQNRYEAWLEVEILACEAWSELG-HIPKADVQKIRQN-AKVNVERAQEIEQETRHDVVAFTRQVS 78
Cdd:cd03302    1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGlDISDEQIEEMKANvENIDFEIAAAEEKKLRHDVMAHVHAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  79 ETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWY 158
Cdd:cd03302   81 LLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 159 TEMQRNLQRFKQVREEIEVGKMSGAVGTFANI----------PPEIESYVCKHLGIGTA-PVSTQTLQRDRHAYYIATLA 227
Cdd:cd03302  161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFldlfegdhdkVEALDELVTKKAGFKKVyPVTGQTYSRKVDIDVLNALS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 228 LIATSLEKFAVEIRNLQKTEtrEVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPL-WHERDISHS 306
Cdd:cd03302  241 SLGATAHKIATDIRLLANLK--EVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTqWFERTLDDS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 307 SAERIMLPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDK-----VQPKAMI 381
Cdd:cd03302  319 ANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERirvlsHQAAAVV 398

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 612673059 382 SWETKTP-FRELIEQDESITSVltKEELDECFDPK 415
Cdd:cd03302  399 KQEGGDNdLIERIKNDAYFKPI--WDELDALLDPK 431
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 5-428 7.87e-69

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


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 225.28  E-value: 7.87e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   5 YSREEMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKVNVERAQEIEQETRHD-------VVAFTRQV 77
Cdd:PRK09053  12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALAgnlaiplVKQLTAQV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  78 SETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALW 157
Cdd:PRK09053  92 AARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGW 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 158 YTEMQRNLQRFKQVREEIEVGKMSGAVGTFANI---PPEIESYVCKHLGIGTAPVSTQTlQRDRHAYYIATLALIATSLE 234
Cdd:PRK09053 172 LDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeqALPVAQALAAELQLALPALPWHT-QRDRIAEFASALGLLAGTLG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 235 KFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSEN-ITGISRViRGYITTAYENVPLWHERDISHSSAERIML 313
Cdd:PRK09053 251 KIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAvLTAATRA-PGLVATLFAAMPQEHERALGGWHAEWDTL 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 314 PDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKgMVREEAYDKVQPKAMISWETKTPFRELI 393
Cdd:PRK09053 330 PELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILAEAVMLALADR-IGRLDAHHLVEQASKRAVAEGRHLRDVL 408

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 612673059 394 EQDESITSVLTKEELDECFDPKHHLNQVDTIFERA 428
Cdd:PRK09053 409 AEDPQVSAHLSPAALDRLLDPAHYLGQAHAWVDRV 443
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 42-328 4.30e-58

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


Pssm-ID: 176466 [Multi-domain]  Cd Length: 231  Bit Score: 190.13  E-value: 4.30e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  42 KADVQkIRQN-AKVNVERAqeieqetrhdvvaFTRQVSETLGEER--KWVHYGLTSTDVVDTALSFVIKQANDIIEKDLE 118
Cdd:cd01594    2 RADLL-VELAaALALVEEV-------------LAGRAGELAGGLHgsALVHKGRSSNDIGTTALRLALRDALDDLLPLLK 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 119 RFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQVReeievgkmsgavgtfanippeiesyv 198
Cdd:cd01594   68 ALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA-------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 199 ckhlgigtapvstqtlqrdrHAYYIATLALIATSLEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENIT 278
Cdd:cd01594  122 --------------------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVR 181

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 612673059 279 GISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDYALNRFT 328
Cdd:cd01594  182 GLAGLVIGNLVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
protocat_pcaB TIGR02426
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ...
 9-334 3.46e-55

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: 186.11  E-value: 3.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059    9 EMSNIWTDQNRYEAWLEVEILACEAWSELGHIPKADVQKIRQNAKVNVERAQEIEQETRHD---VVAFTRQVSETLGEE- 84
Cdd:TIGR02426  10 AALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAAAAPDLEALAHAAATAgnpVIPLVKALRKAVAGEa 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   85 RKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRN 164
Cdd:TIGR02426  90 ARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTFGLKAAGWLAAVLRA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  165 LQRFKQVREEIEVGKMSGAVGTFANIPP---EIESYVCKHLGIgTAPVSTQTLQRDRHAYYIATLALIATSLEKFAVEIR 241
Cdd:TIGR02426 170 RDRLAALRTRALPLQFGGAAGTLAALGTrggAVAAALAARLGL-PLPALPWHTQRDRIAEFGSALALVAGALGKIAGDIA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  242 NLQKTEtreVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALD 321
Cdd:TIGR02426 249 LLSQTE---VGEVFEAGGGGSSAMPHKRNPVGAALLAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPELVRLTG 325

                         330
                  ....*....|...
gi 612673059  322 YALNRFTNIVDRL 334
Cdd:TIGR02426 326 GALRQAQVLAEGL 338
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 24-348 6.69e-37

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: 139.68  E-value: 6.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  24 LEVEILACEAWSELGHIPKADV---------QKIRQNAKV-NVERAQEIEQETRHDVVA---FTRQVSETLGEERK---W 87
Cdd:cd01598   15 VQVEVEWLIALSNLEEIPEVPPltkeelkflRAIIENFSEeDALRIKEIEATTNHDVKAveyFLKEKFETLGLLKKikeF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  88 VHYGLTSTDVVDTALSFVIKQA-NDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQ 166
Cdd:cd01598   95 IHFACTSEDINNLAYALMIKEArNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 167 RFKQVreEIeVGKMSGAVGTFA-------NIP-PEIESYVCKHLGIGTAPVSTQTLQRDRHAYYIATLALIATSLEKFAV 238
Cdd:cd01598  175 QLKQI--EI-LGKFNGAVGNFNahlvaypDVDwRKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALARINTILIDLCR 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 239 EI-----RNL--QKTETREVeeafakgqkGSSAMPHKRNPIGSENITG---ISRVIRGYITTayeNVPL--WhERDISHS 306
Cdd:cd01598  252 DIwgyisLGYfkQKVKKGEV---------GSSTMPHKVNPIDFENAEGnlgLSNALLNHLSA---KLPIsrL-QRDLTDS 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 612673059 307 SAERimlpDVTIALDYALNRFTNI---VDRLTVFEDNMRNNIDKT 348
Cdd:cd01598  319 TVLR----NIGVAFGHSLIAYKSLlrgLDKLELNEARLLEDLDAN 359
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 350-429 1.55e-34

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: 123.33  E-value: 1.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059   350 GLIFSQRVLLALINKGMVREEAYDKVQPKAMISWETKTPFRELIEQDESITSVLTKEELDECFDPKHHLNQVDTIFERAG 429
Cdd:smart00998   2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEEGKDLRELLLADPEVTAYLSEEELEELFDPEYYLGHADAIVDRVL 81
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 18-276 1.86e-30

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 122.17  E-value: 1.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  18 NRYEAWLEVEIL----ACEAWSELGHIPKADVQKIRQNAK----VNVERAQEIEQETRHDVVA---FTRQVSETLGEERK 86
Cdd:PRK09285  33 IRYRVQVEVEWLialaAHPGIPEVPPFSAEANAFLRAIVEnfseEDAARIKEIERTTNHDVKAveyFLKEKLAGLPELEA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  87 ---WVHYGLTSTDVVDTALSFVIKQA-NDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQ 162
Cdd:PRK09285 113 vseFIHFACTSEDINNLSHALMLKEArEEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 163 RNLQRFKQVreEIeVGKMSGAVGTF-ANIP--PEI------ESYVCkHLGIGTAPVSTQTLQRDRHAYYIATLALIATSL 233
Cdd:PRK09285 193 RQLKQLEAV--EI-LGKINGAVGNYnAHLAayPEVdwhafsREFVE-SLGLTWNPYTTQIEPHDYIAELFDAVARFNTIL 268

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612673059 234 EKFAVEI---------RnlQKTETREVeeafakgqkGSSAMPHKRNPIGSEN 276
Cdd:PRK09285 269 IDLDRDVwgyislgyfK--QKTKAGEI---------GSSTMPHKVNPIDFEN 309
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 19-282 4.22e-29

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


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 116.69  E-value: 4.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  19 RYEAWLeveilaCEAWSELGHIPKADVQKIRQN-AKVNVERAQEIEQETRHDVV--AFTRQVSETLGEE-RKWVHYGLTS 94
Cdd:PRK05975  35 AFEAAL------AEAEAEHGIIPAEAAERIAAAcETFEPDLAALRHATARDGVVvpALVRQLRAAVGEEaAAHVHFGATS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  95 TDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQVREE 174
Cdd:PRK05975 109 QDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRAD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 175 IEVGKMSGAVGTFANIPPE---IESYVCKHLGIGTAPVStQTlQRDRHAYYIATLALIATSLEKFAVEIRNLQKTETrEV 251
Cdd:PRK05975 189 VFPLQFGGAAGTLEKLGGKaaaVRARLAKRLGLEDAPQW-HS-QRDFIADFAHLLSLVTGSLGKFGQDIALMAQAGD-EI 265

                        250       260       270
                 ....*....|....*....|....*....|.
gi 612673059 252 EEAfakGQKGSSAMPHKRNPIGSENITGISR 282
Cdd:PRK05975 266 SLS---GGGGSSAMPHKQNPVAAETLVTLAR 293
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 350-428 5.19e-28

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: 105.57  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  350 GLIFSQRVLLALInKGMVREEAYDKVQPKAMISWET-KTPFRELIEQDESITsVLTKEELDECFDPKHHLNQVDTIFERA 428
Cdd:pfam10397   1 GLIFSERVLLALV-KGLGREEAHELVQEAAMKAWEEgKNDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADEIVDRV 78
PLN02848 PLN02848
adenylosuccinate lyase
 60-394 6.02e-23

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 100.58  E-value: 6.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  60 QEIEQETRHDVVA---FTRQVSETLGEERK---WVHYGLTSTDVVDTALSFVIKQA-NDIIEKDLERFIDVLAEKAKNYK 132
Cdd:PLN02848  86 KKIERVTNHDVKAveyFLKQKCKSHPELAKvleFFHFACTSEDINNLSHALMLKEGvNSVVLPTMDEIIKAISSLAHEFA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 133 YTLMMGRTHGVHAEPTTFGVKMALWYTEMQRnlQRfKQVREEIEVGKMSGAVGTF-ANIP--PEI------ESYVcKHLG 203
Cdd:PLN02848 166 YVPMLSRTHGQPASPTTLGKEMANFAYRLSR--QR-KQLSEVKIKGKFAGAVGNYnAHMSayPEVdwpavaEEFV-TSLG 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 204 IGTAPVSTQTLQRDRHAYYIATLALIATSLEKFAVEIRNL-------QKTETREVeeafakgqkGSSAMPHKRNPIGSEN 276
Cdd:PLN02848 242 LTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWSYislgyfkQITKAGEV---------GSSTMPHKVNPIDFEN 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 277 ITGISRVIRGYITTAYENVPL--WhERDISHSSAERIM---LPDVTIALDYALNRftniVDRLTVFEDNMRNNIDKTFgl 351
Cdd:PLN02848 313 SEGNLGLANAELSHLSMKLPIsrM-QRDLTDSTVLRNMgvgLGHSLLAYKSTLRG----IGKLQVNEARLAEDLDQTW-- 385

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 612673059 352 ifsqRVLLALINKGMVR---EEAYDKVQPKAMISWETKTPFRELIE 394
Cdd:PLN02848 386 ----EVLAEPIQTVMRRygvPEPYEKLKELTRGRAVTKESMREFIE 427
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 75-349 2.33e-21

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: 95.69  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  75 RQVSETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKM 154
Cdd:cd01359   68 RRLIERIGDVGGKLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 155 ALWYTEMQRNLQRFKQVREEIEVGKM-SGA-VGTFANIPPEiesYVCKHLGIGTAPVST--QTLQRDRHAYYIATLALIA 230
Cdd:cd01359  148 LAYAEMLERDLERLADAYKRVNVSPLgAGAlAGTTFPIDRE---RTAELLGFDGPTENSldAVSDRDFVLEFLSAAALLM 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 231 TSLEKFAVEIRnLQKTETR---EVEEAFAkgqKGSSAMPHKRNPIGSENITGIS-RVIrGYIT---TAYENVPLWHERDI 303
Cdd:cd01359  225 VHLSRLAEDLI-LWSTQEFgfvELPDAYS---TGSSIMPQKKNPDVLELIRGKAgRVI-GALAgllTTLKGLPLAYNKDL 299

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 612673059 304 SHSSAeriMLPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTF 349
Cdd:cd01359  300 QEDKE---PLFDAVDTLIASLRLLTGVISTLTVNPERMREAAEAGF 342
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 94-413 2.58e-18

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: 86.81  E-value: 2.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  94 ST-DVVDTALSF-VIKQANDIIEKdLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQV 171
Cdd:cd01357  135 STnDVYPTALRLaLILLLRKLLDA-LAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKA 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 172 REEIEVGKMSG-AVGTFANIPPEIESYVCKHL----GIGTAPV-----STQTLqrDRHAYYIATLALIATSLEKFAVEIR 241
Cdd:cd01357  214 RERLREVNLGGtAIGTGINAPPGYIELVVEKLseitGLPLKRAenlidATQNT--DAFVEVSGALKRLAVKLSKIANDLR 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 242 NLqktetreveeafAKG-------------QKGSSAMPHKRNPIGSENITGISRVIRGY---ITTAYE------NV--PL 297
Cdd:cd01357  292 LL------------SSGpraglgeinlpavQPGSSIMPGKVNPVIPEVVNQVAFQVIGNdltITMAAEagqlelNVfePV 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 298 wherdISHSSAERIMLpdvtiaLDYALNRF-TNIVDRLTVFEDNMRNNIDKTFGLIfsqRVLLALInkgmvreeAYDKVQ 376
Cdd:cd01357  360 -----IAYNLLESIDI------LTNAVRTLrERCIDGITANEERCREYVENSIGIV---TALNPYI--------GYEAAA 417

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 612673059 377 PKAMISWETKTPFRELIEQdesiTSVLTKEELDECFD 413
Cdd:cd01357  418 EIAKEALETGRSVRELVLE----EGLLTEEELDEILS 450
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 94-415 5.75e-18

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 85.81  E-value: 5.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  94 ST-DVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQVR 172
Cdd:PRK13353 140 STnDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAR 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 173 EEIEVGKMSG-AVGTFANIPPEIESYVCKHL-GIGTAPVS--------TQTLqrDRHAYYIATLALIATSLEKFAVEIRN 242
Cdd:PRK13353 220 EHLYEVNLGGtAVGTGLNADPEYIERVVKHLaAITGLPLVgaedlvdaTQNT--DAFVEVSGALKVCAVNLSKIANDLRL 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 243 LQKTETREVEEAF--AKgQKGSSAMPHKRNPIGSENITGIS-RVI--RGYITTAYE------NV--PLwherdISHSSAE 309
Cdd:PRK13353 298 LSSGPRTGLGEINlpAV-QPGSSIMPGKVNPVMPEVVNQIAfQVIgnDVTITLAAEagqlelNVmePV-----IAFNLLE 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 310 RIMLpdvtiaLDYALNRFT-NIVDRLTVFEDNMRNNIDKTFGLIfsqRVLLALInkgmvreeAYDKVQPKAMISWETKTP 388
Cdd:PRK13353 372 SISI------LTNACRAFTdNCVKGIEANEERCKEYVEKSVGIA---TALNPHI--------GYEAAARIAKEAIATGRS 434

                        330       340
                 ....*....|....*....|....*..
gi 612673059 389 FRELIEQdesiTSVLTKEELDECFDPK 415
Cdd:PRK13353 435 VRELALE----NGLLSEEELDLILDPF 457
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 75-375 1.68e-16

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 80.97  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  75 RQVSETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKM 154
Cdd:PRK00855  92 ARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 155 ALWYTEMQRNLQRFKQVREEIEV---GkmSGA-VGTFANIPPEiesYVCKHLGIgTAP-------VSTqtlqRDRHAYYI 223
Cdd:PRK00855 172 LAYAEMLARDLERLRDARKRVNRsplG--SAAlAGTTFPIDRE---RTAELLGF-DGVtensldaVSD----RDFALEFL 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 224 ATLALIATSLEKFAVEIRNLQKTETREVE--EAFAkgqKGSSAMPHKRNPIGSENITG-ISRVIrGY---ITTAYENVPL 297
Cdd:PRK00855 242 SAASLLMVHLSRLAEELILWSSQEFGFVElpDAFS---TGSSIMPQKKNPDVAELIRGkTGRVY-GNltgLLTVMKGLPL 317

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612673059 298 WHERDIshSSAERIMLPDVTIALDyALNRFTNIVDRLTVFEDNMRNNIDKtfGLIFSQRVLLALINKGMVREEAYDKV 375
Cdd:PRK00855 318 AYNRDL--QEDKEPLFDAVDTLKL-SLEAMAGMLETLTVNKERMREAAGK--GFSTATDLADYLVRKGVPFREAHEIV 390
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 94-413 5.48e-15

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: 76.31  E-value: 5.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  94 STDVVDTA--LSFVIKQANDIIEKdLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQV 171
Cdd:cd01596  135 SNDDFPPAahIAAALALLERLLPA-LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAA 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 172 REEIEVGKMSG-AVGTFANIPPEIESYVCKHL----GIG--TAPVSTQTLQ-RDRHAYYIATLALIATSLEKFAVEIRNL 243
Cdd:cd01596  214 LERLRELNLGGtAVGTGLNAPPGYAEKVAAELaeltGLPfvTAPNLFEATAaHDALVEVSGALKTLAVSLSKIANDLRLL 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 244 qktetreveeafAKG-------------QKGSSAMPHKRNPIGSENITGIS-RVIrGY---ITTAYE------NV--PLw 298
Cdd:cd01596  294 ------------SSGpraglgeinlpanQPGSSIMPGKVNPVIPEAVNMVAaQVI-GNdtaITMAGSagqlelNVfkPV- 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 299 herdISHSSAERIMLpdvtiaLDYALNRFT-NIVDRLTVFEDNMRNNIDKTFGLIfsqrvlLALINK-GmvreeaYDKVQ 376
Cdd:cd01596  360 ----IAYNLLQSIRL------LANACRSFRdKCVEGIEANEERCKEYVENSLMLV------TALNPHiG------YEKAA 417

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 612673059 377 PKAMISWETKTPFRELIEQdesiTSVLTKEELDECFD 413
Cdd:cd01596  418 EIAKEALKEGRTLREAALE----LGLLTEEELDEILD 450
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 79-414 1.71e-14

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 75.04  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  79 ETLGEERKWVHY---------GLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTT 149
Cdd:PRK14515 123 ELLGMEKGDYHYispnshvnmAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIR 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 150 FGVKMALWYTEMQRNLQRFKQVREEI-EVGKMSGAVGTFANIPPEIESYVCKHLG-------IGTAPVSTQTLQRDRHAY 221
Cdd:PRK14515 203 LGQEFKAYSRVLERDMKRIQQSRQHLyEVNMGATAVGTGLNADPEYIEAVVKHLAaiselplVGAEDLVDATQNTDAYTE 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 222 YIATLALIATSLEKFAVEIRnLQKTETRE--VEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRG---YITTAYENVP 296
Cdd:PRK14515 283 VSAALKVCMMNMSKIANDLR-LMASGPRVglAEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGndhTICLASEAGQ 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 297 LwhERDISHSSAERIMLPDVTIaLDYALNRFT-NIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALinkgmvreEAYDKV 375
Cdd:PRK14515 362 L--ELNVMEPVLVFNLLQSISI-MNNGFRAFTdNCLKGIEANEDRLKEYVEKSVGIITAVNPHIGY--------EAAARV 430

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 612673059 376 QPKAMIsweTKTPFRELIEQDEsitsVLTKEELDECFDP 414
Cdd:PRK14515 431 AKEAIA---TGQSVRELCVKNG----VLSQEDLELILDP 462
aspA PRK12273
aspartate ammonia-lyase; Provisional
 94-419 6.85e-14

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 73.24  E-value: 6.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  94 ST-DVVDTALSF-VIKQANDIIEKdLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQV 171
Cdd:PRK12273 142 STnDAYPTAIRIaLLLSLRKLLDA-LEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRA 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 172 REEI-EVGkMSG-AVGTFANIPPEIESYVCKHL----GIGTAPVS-----TQtlqrDRHAY--YIATLALIATSLEKFAV 238
Cdd:PRK12273 221 AELLrEVN-LGAtAIGTGLNAPPGYIELVVEKLaeitGLPLVPAEdlieaTQ----DTGAFveVSGALKRLAVKLSKICN 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 239 EIR-------------NLQKTetreveeafakgQKGSSAMPHKRNPIGSENITGIS-RVIrGY---ITTAYE------NV 295
Cdd:PRK12273 296 DLRllssgpraglneiNLPAV------------QAGSSIMPGKVNPVIPEVVNQVCfQVI-GNdttVTMAAEagqlelNV 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 296 --PLwherdISHSSAERIMLpdvtiaLDYALNRF-TNIVDRLTVFEDNMRNNIDKTFGLIfsqrvlLALINK-Gmvreea 371
Cdd:PRK12273 363 mePV-----IAYNLFESISI------LTNACRTLrEKCIDGITANEERCREYVENSIGIV------TALNPYiG------ 419

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 612673059 372 YDKVQPKAMISWETKTPFRELIEQDEsitsVLTKEELDECFDPKHHLN 419
Cdd:PRK12273 420 YENAAEIAKEALETGKSVRELVLERG----LLTEEELDDILSPENMTH 463
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 67-291 5.88e-10

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 61.40  E-value: 5.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  67 RHDVVAFTRQVSETLGEERK-WVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHA 145
Cdd:PRK02186 488 RGLYMLYEAYLIERLGEDVGgVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPA 567

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 146 EPTTFGVKMALWYTEMQRNLQRFKQVREEIEV---GKMSGAvGTFANIPPEiesYVCKHLGIGTAPVST--QTLQRDRHA 220
Cdd:PRK02186 568 LPGSLGHYLLAVDGALARETHALFALFEHIDVcplGAGAGG-GTTFPIDPE---FVARLLGFEQPAPNSldAVASRDGVL 643

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612673059 221 YYIATLALIATSLEKFAveiRNLQKTETREVeeAF----AKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTA 291
Cdd:PRK02186 644 HFLSAMAAISTVLSRLA---QDLQLWTTREF--ALvslpDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASA 713
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 117-284 1.12e-09

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 59.82  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 117 LERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQVREEIEVGKMSG-AVGTFANIPPEIE 195
Cdd:cd01362  160 LKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGtAVGTGLNAHPGFA 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 196 SYVCKHL----GIG--TAPVSTQTL-QRDRHAYYIATLALIATSLEKFAVEIRNLqktetreveeafAKG---------- 258
Cdd:cd01362  240 EKVAAELaeltGLPfvTAPNKFEALaAHDALVEASGALKTLAVSLMKIANDIRWL------------GSGprcglgelsl 307

                        170       180       190
                 ....*....|....*....|....*....|
gi 612673059 259 ---QKGSSAMPHKRNPIGSENITGIS-RVI 284
Cdd:cd01362  308 penEPGSSIMPGKVNPTQCEALTMVAaQVM 337
fumC PRK00485
fumarate hydratase; Reviewed
 78-278 1.46e-08

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 56.64  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  78 SETLGEER---KWVH------YGLTSTDVVDTALSFVIKQAndiIEKDL----ERFIDVLAEKAKNYKYTLMMGRTHGVH 144
Cdd:PRK00485 115 SELLGGELgskKPVHpndhvnMSQSSNDTFPTAMHIAAVLA---IVERLlpalEHLRDTLAAKAEEFADIVKIGRTHLQD 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 145 AEPTTFGVKMALWYTEMQRNLQRFKQVRE---EIEVGkmsG-AVGTFANIPPEIESYVCKHL----GIG--TAPVSTQTL 214
Cdd:PRK00485 192 ATPLTLGQEFSGYAAQLEHGIERIEAALPhlyELALG---GtAVGTGLNAHPGFAERVAEELaeltGLPfvTAPNKFEAL 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612673059 215 -QRDRHAYYIATLALIATSLEKFAVEIRNLqktetreveeafAKG-------------QKGSSAMPHKRNPIGSENIT 278
Cdd:PRK00485 269 aAHDALVEASGALKTLAVSLMKIANDIRWL------------ASGprcglgeislpenEPGSSIMPGKVNPTQCEALT 334
PLN00134 PLN00134
fumarate hydratase; Provisional
 88-418 7.79e-07

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 51.23  E-value: 7.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  88 VHYGLTSTDVVDTALSF-VIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQ 166
Cdd:PLN00134 126 VNRSQSSNDTFPTAMHIaAATEIHSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLN 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 167 RFKQVREEI-EVGKMSGAVGTFANIPP----EIESYVCKHLGIG--TAPVSTQTLQrdRHAYYIAT---LALIATSLEKF 236
Cdd:PLN00134 206 RVQCTLPRLyELAQGGTAVGTGLNTKKgfdeKIAAAVAEETGLPfvTAPNKFEALA--AHDAFVELsgaLNTVAVSLMKI 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 237 AVEIRNLQKTETREVEE-AFAKGQKGSSAMPHKRNPIGSENITGISRVIRG---YITTAYE------NV--PLwherdIS 304
Cdd:PLN00134 284 ANDIRLLGSGPRCGLGElNLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGnhvAITVGGSaghfelNVfkPL-----IA 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 305 HSSAERIMLpdvtiaLDYALNRF-TNIVDRLTVFEDNMRNNIDKTFGLIFSqrvLLALInkgmvreeAYDKVQPKAMISW 383
Cdd:PLN00134 359 YNLLHSIRL------LGDASASFrKNCVRGIEANRERISKLLHESLMLVTA---LNPKI--------GYDKAAAVAKKAH 421

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 612673059 384 ETKTPFRELieqdESITSVLTKEELDECFDPKHHL 418
Cdd:PLN00134 422 KEGTTLKEA----ALKLGVLTAEEFDELVVPEKMT 452
PLN02646 PLN02646
argininosuccinate lyase
 59-290 3.37e-06

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 48.95  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  59 AQEIEQET------RHDV-VAFTRQVSETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNY 131
Cdd:PLN02646  81 EKEIEAGKfewrpdREDVhMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 132 KYTLMMGRTHGVHAEPttfgVKMALW---YTEM-QRNLQRFKQVREEIEVGKMsGAvGTFANIPPEIESY-VCKHLGIgT 206
Cdd:PLN02646 161 VDLVVPGYTHLQRAQP----VLLSHWllsHVEQlERDAGRLVDCRPRVNFCPL-GS-CALAGTGLPIDRFmTAKDLGF-T 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 207 APVSTQ---TLQRDRHAYYIATLALIATSLEKFAVEIRNLQKTETREVE--EAFAkgqKGSSAMPHKRNPIGSENITGIS 281
Cdd:PLN02646 234 APMRNSidaVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFVTpsDAVS---TGSSIMPQKKNPDPMELVRGKS 310


                 ....*....
gi 612673059 282 RVIRGYITT 290
Cdd:PLN02646 311 ARVIGDLVT 319
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 128-297 9.14e-06

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 47.67  E-value: 9.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 128 AKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQRFKQVREEIEVGKMSGAVGTFANIPpeIESYVCKHLgIGTA 207
Cdd:PRK06705 150 AADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTTSFP--IKRERVADL-LGFT 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 208 PVSTQTLQRDRHAYYI----ATLALIATSLEKFAVEIRNLQKTETREVEEAFAKGQKgSSAMPHKRNPIGSENITGISRV 283
Cdd:PRK06705 227 NVIENSYDAVAGADYLlevsSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQI-SSIMPQKRNPVSIEHARAITSS 305

                        170
                 ....*....|....*..
gi 612673059 284 IRGYITTAYE---NVPL 297
Cdd:PRK06705 306 ALGEAFTVFQmihNTPF 322
PRK12308 PRK12308
argininosuccinate lyase;
76-303 1.05e-05

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 47.86  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  76 QVSETLGEERKWVHYGLTSTDVVDTALSFVIKQANDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGvKMA 155
Cdd:PRK12308  91 QLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFA-HWC 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 156 LWYTEM-QRNLQRFKQVREEIEVGKM-SGAV-GTFANIPPEIesyVCKHLGIGTAPVSTQTLQRDR-HAYYIATLALIAT 231
Cdd:PRK12308 170 LAYVEMfERDYSRLEDALTRLDTCPLgSGALaGTAYPIDREA---LAHNLGFRRATRNSLDSVSDRdHVMELMSVASISM 246

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612673059 232 -SLEKFAVEIRNLQKTETREVEEAfAKGQKGSSAMPHKRNPIGSENITGISRVIRGYIT---TAYENVPLWHERDI 303
Cdd:PRK12308 247 lHLSRLAEDLIFYNSGESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAgmmMTVKALPLAYNKDM 321
PRK12425 PRK12425
class II fumarate hydratase;
88-278 1.93e-04

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 43.37  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059  88 VHYGLTSTDVVDTALSFVIKQA-NDIIEKDLERFIDVLAEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMQRNLQ 166
Cdd:PRK12425 132 VNRSQSSNDCFPTAMHIAAAQAvHEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAER 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673059 167 RFKQVREEI-EVGKMSGAVGTFANIPPEIESYVCKHLG------IGTAPVSTQTLQRDRHAYYIA-TLALIATSLEKFAV 238
Cdd:PRK12425 212 AIRAALPAVcELAQGGTAVGTGLNAPHGFAEAIAAELAalsglpFVTAPNKFAALAGHEPLVSLSgALKTLAVALMKIAN 291

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 612673059 239 EIRNLQKTETREVEEA-FAKGQKGSSAMPHKRNPIGSENIT 278
Cdd:PRK12425 292 DLRLLGSGPRAGLAEVrLPANEPGSSIMPGKVNPTQCEALS 332
 
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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