|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
1-397 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 537.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 1 MSSKLWEK--SVTVDHDVESYTVGRdrEMDLYLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKI 78
Cdd:PRK00855 2 MSNKLWGGrfSEGPDELVERFTASI--SFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 79 EDDIEDVHSQVELMLTRKLGDIGKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHL 158
Cdd:PRK00855 80 SPELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 159 QVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRgKTER 238
Cdd:PRK00855 160 QRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDR-DFAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 239 VVAQALGGIAATIAKLSFDACMFNSQNFGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSG 318
Cdd:PRK00855 239 EFLSAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 319 YFRDLQLIKENFLPAFDSLIEIISMVTQMLSEVKVNTEILKDPRYSLMFSVEEV-NHLTLEGVPFRDAYKQVGLAIERGE 397
Cdd:PRK00855 319 YNRDLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLaDYLVRKGVPFREAHEIVGKAVREAE 398
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
1-396 |
1.81e-126 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 374.44 E-value: 1.81e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 1 MSSKLWEK--SVTVDHDVESYT--VGRDREmdlyLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDF 76
Cdd:COG0165 1 MSMKLWGGrfSEGPDELVEEFNasISFDKR----LAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 77 KIEDDIEDVHSQVELMLTRKLGDIGKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYT 156
Cdd:COG0165 77 EFDPELEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 157 HLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFD-----SMDynVV---- 227
Cdd:COG0165 157 HLQRAQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDgptenSLD--AVsdrd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 228 YAqmgrgkTErvVAQALGGIAATIAKLSFDACMFNSQNFGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQ-ALpy 306
Cdd:COG0165 235 FA------LE--FLSAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIgNL-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 307 eITLITN--NLPSGYFRDLQLIKENFLPAFDSLIEIISMVTQMLSEVKVNTEILKD--PR-YSLMFSVeeVNHLTLEGVP 381
Cdd:COG0165 305 -TGLLTTmkGLPLAYNKDLQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREaaGAgFSTATDL--ADYLVRKGVP 381
|
410
....*....|....*....
gi 1518537807 382 FRDAYKQVG----LAIERG 396
Cdd:COG0165 382 FREAHEIVGrlvrYAEEKG 400
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
21-397 |
2.78e-118 |
|
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: 352.62 E-value: 2.78e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 21 VGRDREmdlyLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKIEDDIEDVHSQVELMLTRKLGDI 100
Cdd:cd01359 2 ISFDRR----LFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 101 GKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDD 180
Cdd:cd01359 78 GGKLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 181 LTVLLAAYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKTERVVAqALGGIAATIAKLSFDACM 260
Cdd:cd01359 158 LERLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLS-AAALLMVHLSRLAEDLIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 261 FNSQNFGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFRDLQLIKENFLPAFDSLIEI 340
Cdd:cd01359 237 WSTQEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIAS 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 341 ISMVTQMLSEVKVNTEILKDpRYSLMFSV--EEVNHLTLE-GVPFRDAYKQVGLAIERGE 397
Cdd:cd01359 317 LRLLTGVISTLTVNPERMRE-AAEAGFSTatDLADYLVREkGVPFREAHHIVGRAVRLAE 375
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
28-396 |
2.42e-109 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 330.47 E-value: 2.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 28 DLYLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKIEDDIEDVHSQVELMLTRKLG-DIGKKIHS 106
Cdd:TIGR00838 24 DKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDEDIHMAIERELIDRVGeDLGGKLHT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 107 GRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLA 186
Cdd:TIGR00838 104 GRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 187 AYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRG-KTERVVAQALggIAATIAKLSFDACMFNSQN 265
Cdd:TIGR00838 184 ALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDfILELLFVAAL--IMVHLSRFAEDLILWSTGE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 266 FGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFRDLQLIKENFLPAFDSLIEIISMVT 345
Cdd:TIGR00838 262 FGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQEDKEPLFDALKTVELSLEMAT 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1518537807 346 QMLSEVKVNTEILKDpRYSLMFS--VEEVNHLTLEGVPFRDAYKQVG----LAIERG 396
Cdd:TIGR00838 342 GMLDTITVNKERMEE-AASAGFSnaTELADYLVRKGVPFREAHHIVGelvaTAIERG 397
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
34-354 |
3.60e-85 |
|
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: 263.59 E-value: 3.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 34 YDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKIEDDIEDVHSQVELMLTRKLGDI-GKKIHSGRSRND 112
Cdd:cd01334 3 ADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSSND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 113 QVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTN 192
Cdd:cd01334 83 IVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 193 RNPLGSAA--GYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGkteRVV--AQALGGIAATIAKLSFDACMFNSQNFGF 268
Cdd:cd01334 163 VLPLGGGAvgTGANAPPIDRERVAELLGFFGPAPNSTQAVSDRD---FLVelLSALALLAVSLSKIANDLRLLSSGEFGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 269 IKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFRDLQLIKENFLPAFDSLIEIISMVTQML 348
Cdd:cd01334 240 VELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVL 319
|
....*.
gi 1518537807 349 SEVKVN 354
Cdd:cd01334 320 EGLEVN 325
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
4-396 |
5.05e-80 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 255.42 E-value: 5.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 4 KLW--EKSVTVDHDVESYT--VGRDREMdlylAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKIE 79
Cdd:PLN02646 17 KLWggRFEEGVTPAVEKFNesISFDKRL----YKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEWR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 80 DDIEDVHSQVELMLTRKLGDIGKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQ 159
Cdd:PLN02646 93 PDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 160 VAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGkterV 239
Cdd:PLN02646 173 RAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRD----F 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 240 VAQALGGIAAT---IAKLSFDACMFNSQNFGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLP 316
Cdd:PLN02646 249 VLEFLFANSITaihLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 317 SGYFRDLQLIKEnflPAFDSLIEIISMV---TQMLSEVKVNTEILKDPRYSLMFSVEEV-NHLTLEGVPFRDAY----KQ 388
Cdd:PLN02646 329 TAYNRDLQEDKE---PLFDSVDTVSDMLevaTEFAQNITFNPERIKKSLPAGMLDATTLaDYLVRKGVPFRETHhivgAA 405
|
....*...
gi 1518537807 389 VGLAIERG 396
Cdd:PLN02646 406 VALAESKG 413
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
28-396 |
2.03e-76 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 245.28 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 28 DLYLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKI-EDDIEDVHSQVELMLTRKLGDIGKKIHS 106
Cdd:PRK04833 26 DYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQIlASDAEDIHSWVEGKLIDKVGDLGKKLHT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 107 GRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLA 186
Cdd:PRK04833 106 GRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 187 AYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKtervVAQALGGIAATIAKLS-F--DACMFNS 263
Cdd:PRK04833 186 ALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDH----VLELLSDASISMVHLSrFaeDLIFFNS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 264 QNFGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFRDLQLIKENFLPAFDSLIEIISM 343
Cdd:PRK04833 262 GEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHM 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1518537807 344 VTQMLSEVKVNTE-ILKDPRYSLMFSVEEVNHLTLEGVPFRDAYKQVG----LAIERG 396
Cdd:PRK04833 342 AALVLDGIQVKRPrCQEAAQQGYANATELADYLVAKGVPFREAHHIVGeavvEAIRQG 399
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
28-396 |
3.70e-70 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 233.52 E-value: 3.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 28 DLYLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIY-KVIEQGDFKIEDDIEDVHSQVELMLTRKLGDIGKKIHS 106
Cdd:PRK12308 26 DYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKlEVMEDPEQILLSDAEDIHSWVEQQLIGKVGDLGKKLHT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 107 GRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLA 186
Cdd:PRK12308 106 GRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLED 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 187 AYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKTERVVAQAlgGIAAT-IAKLSFDACMFNSQN 265
Cdd:PRK12308 186 ALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA--SISMLhLSRLAEDLIFYNSGE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 266 FGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFRDLQLIKENFLPAFDSLIEIISMVT 345
Cdd:PRK12308 264 SGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQEDKEGLFDALDTWNDCMEMAA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1518537807 346 QMLSEVKVNTE-ILKDPRYSLMFSVEEVNHLTLEGVPFRDAYKQVG----LAIERG 396
Cdd:PRK12308 344 LCFDGIKVNGErTLEAAKQGYANATELADYLVAKGIPFREAHHIVGvavvGAIAKG 399
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
4-397 |
4.51e-44 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 159.67 E-value: 4.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 4 KLWEKSVTVDHDVESYT--VGRDREMDLYLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYkvieQGDFKIEDD 81
Cdd:PRK06389 2 KIWSGGAGEELENDFYDniVKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIY----KNGIEIDLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 82 IEDVHSQVELMLTRKLGDIGKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYkdvLMPGYTHLQVA 161
Cdd:PRK06389 78 LEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIPGFNLKG---RLPGYTHFRQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 162 MPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKTERVVA 241
Cdd:PRK06389 155 MPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIENIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 242 QALGGIAATIAKLSFDACMFNSQnfGFIKLPDEYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFR 321
Cdd:PRK06389 235 YLISSLAVDLSRICQDIIIYYEN--GIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHR 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1518537807 322 DLQLIKENFLPAFDSLIEIISMVTQMLSEVK---VNTEILKDPRYSLMFSVEEVnhltLEGVPFRDAYKQVGLAIERGE 397
Cdd:PRK06389 313 DFQIVKDSTISFINNFERILLGLPDLLYNIKfeiTNEKNIKNSVYATYNAWLAF----KNGMDWKSAYAYIGNKIREGE 387
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
27-298 |
2.83e-43 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 154.45 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 27 MDLYLAPYDVLGSLAHITMLQSIGLLTKPELETLTAELRNIYKVIEQGD-FKIEDDIEDVHSQVELMLTRKLGDI----- 100
Cdd:pfam00206 20 FNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDqFPLKVWQEGSGTAVNMNLNEVIGELlgqlv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 101 --GKKIHSGRSRNDQVLVDLKLYIRSRI-EDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESL 177
Cdd:pfam00206 100 hpNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 178 VDDLTVLLAAYSVTNRNPLGSAA----GYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKTERVV--AQALGGIAATI 251
Cdd:pfam00206 180 TRDRERLQQLLPRLLVLPLGGGTavgtGLNADPEFAELVAKELGFFTGLPVKAPNSFEATSDRDAVVelSGALALLATSL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1518537807 252 AKLSFDACMFNSQNFGFIKLPDEYTT-GSSIMPHKKNPDVFELTRAKC 298
Cdd:pfam00206 260 SKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKA 307
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
88-345 |
2.49e-39 |
|
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: 141.21 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 88 QVELMLTRKLGDIGKKIH------SGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVA 161
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 162 MPSSFGLWFGAYAESLVDDLTVLLAAYSVtnrnplgsaagygssfplnrtmttrllgfdsmdynvvyaqmgrgkterVVA 241
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEAAVA------------------------------------------------EAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 242 QALGGIAATIAKLSFDACMFNSQNFGFIKLPD-EYTTGSSIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYF 320
Cdd:cd01594 127 DALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDN 206
|
250 260
....*....|....*....|....*
gi 1518537807 321 RDLQLIKENFLPAFDSLIEIISMVT 345
Cdd:cd01594 207 EDSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
21-393 |
1.81e-32 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 130.74 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 21 VGRDREMDLYLAPYDVLGSL--AHITMLQSIGLLTKPELETLTAELRNIYkviEQGDFKIEDDI--EDVHSQVELMLTRK 96
Cdd:PRK02186 425 VYGPGASEAPLAELDHLAAIdeAHLVMLGDTGIVAPERARPLLDAHRRLR---DAGFAPLLARPapRGLYMLYEAYLIER 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 97 LG-DIGKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAE 175
Cdd:PRK02186 502 LGeDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDG 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 176 SLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKTERVVAqALGGIAATIAKLS 255
Cdd:PRK02186 582 ALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLS-AMAAISTVLSRLA 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 256 FDACMFNSQNFGFIKLPDEYTTGSSIMPHKKNPDVFELTRAK-------CNK----LQALPYeitliTNNLPSGYFRdLQ 324
Cdd:PRK02186 661 QDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRagvvagaLASasaaLGKTPF-----SNSFEAGSPM-NG 734
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1518537807 325 LIKENFLPAFDSLIEIISMVTQMLSEVKVNTEILKDPRYSLMFSVEEVnhLTLEGVPFRDAYKQVGLAI 393
Cdd:PRK02186 735 PIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLEDGGVSATAVAESL--VVRRSISFRSAHTQVGQAI 801
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
41-416 |
8.14e-29 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 118.55 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 41 AHITMLQSIGLLTKPELETLTAELRNIYKVIEQGDFKIEDDiEDVHSQVELMLTRKLG-DIGKKIHSGRSRNDQVLVDLK 119
Cdd:PRK06705 47 AHIVMLTEENLMKKEEAKFILHALKKVEEIPEEQLLYTEQH-EDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 120 LYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSA 199
Cdd:PRK06705 126 MSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 200 AGYGSSFPLNRTMTTRLLGFDSMDYNVVYAQMGRGKTERvVAQALGGIAATIAKLSFDACMFNSQNFGFIKLPDEYTTGS 279
Cdd:PRK06705 206 ALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLE-VSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 280 SIMPHKKNPDVFELTRAKCNKLQALPYEITLITNNLPSGYFRDLQLIKENFL-PAFDSLIEIISMVTQMLSEVKVNTEIL 358
Cdd:PRK06705 285 SIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPYLyKGIEKAIRVFCIMNAVIRTMKVEEDTL 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 359 KDPRYSLMFSVEE-VNHLTLE-GVPFRDAYKQVGlAIERGEFVPPTEVHHTHEGSIgNLY 416
Cdd:PRK06705 365 KRRSYKHAITITDfADVLTKNyGIPFRHAHHAAS-VIANMSLEQKKELHELCFKDV-NIY 422
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
62-389 |
3.42e-20 |
|
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: 91.80 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 62 AELRNIYKVIEQgDFKIEDDIEDV--HS--QVELMLTRKLGDIGKK-IHSGRSRNDqvLVD--LKLYIRSRIEDVTKAMT 134
Cdd:cd01595 37 EEIRAAADVFEI-DAERIAEIEKEtgHDviAFVYALAEKCGEDAGEyVHFGATSQD--INDtaLALQLRDALDIILPDLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 135 GLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPLN----R 210
Cdd:cd01595 114 ALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISGAVGTHASLGPKgpevE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 211 TMTTRLLGFDSMDY-NVVYAQmgrgktERV--VAQALGGIAATIAKLSFDACMFNSQNFGFIKLP-DEYTTGSSIMPHKK 286
Cdd:cd01595 194 ERVAEKLGLKVPPItTQIEPR------DRIaeLLSALALIAGTLEKIATDIRLLQRTEIGEVEEPfEKGQVGSSTMPHKR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 287 NPDVFELTRAKCNKLQALpyeITLITNNLPSGYFRDLQL--IKENFLP-AFDSLIEIISMVTQMLSEVKVNTEILK---D 360
Cdd:cd01595 268 NPIDSENIEGLARLVRAL---AAPALENLVQWHERDLSDssVERNILPdAFLLLDAALSRLQGLLEGLVVNPERMRrnlD 344
|
330 340 350
....*....|....*....|....*....|
gi 1518537807 361 PRYSLMFSvEEVNH-LTLEGVPFRDAYKQV 389
Cdd:cd01595 345 LTWGLILS-EAVMMaLAKKGLGRQEAYELV 373
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
89-360 |
2.04e-15 |
|
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: 77.77 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 89 VELMLTRKLGDIGKKIHSGRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGL 168
Cdd:TIGR00928 76 VVYALKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 169 WFGAYAESLVDDLTVLLAAysvTNRNPLGSAAG-YG--SSFPLNRT----MTTRLLGFDSMDYNV------VYAQmgrgk 235
Cdd:TIGR00928 156 RFALWAEEMLRQLERLLQA---KERIKVGGISGaVGthAAAYPLVEeveeRVTEFLGLKPVPISTqieprdRHAE----- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 236 tervVAQALGGIAATIAKLSFDACMFNSQNFGFIKLP-DEYTTGSSIMPHKKNPDVFELTRAKCNKLQALpyeITLITNN 314
Cdd:TIGR00928 228 ----LLDALALLATTLEKFAVDIRLLQRTEHFEVEEPfGKGQVGSSAMPHKRNPIDFENVCGLARVIRGY---ASPALEN 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1518537807 315 LPSGYFRDL--QLIKENFLP-AFDSLIEIISMVTQMLSEVKVNTEILKD 360
Cdd:TIGR00928 301 APLWHERDLtdSSVERVILPdAFILADIMLKTTLKVVKKLVVNPENILR 349
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
131-292 |
2.58e-11 |
|
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: 65.11 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 131 KAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSvtnrNPL--------GSAAGY 202
Cdd:COG0015 120 PDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARE----RVLvgkiggavGTYAAH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 203 GSSFPLNRTMTTRLLGFDSM---------DYnvvYAQmgrgktervVAQALGGIAATIAKLSFDACMFNSQNFGFIKLP- 272
Cdd:COG0015 196 GEAWPEVEERVAEKLGLKPNpvttqieprDR---HAE---------LFSALALIAGSLEKIARDIRLLQRTEVGEVEEPf 263
|
170 180
....*....|....*....|
gi 1518537807 273 DEYTTGSSIMPHKKNPDVFE 292
Cdd:COG0015 264 AKGQVGSSAMPHKRNPIDSE 283
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
62-292 |
1.97e-10 |
|
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: 62.18 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 62 AELRNI----YKVIEQ-GDFKIE--DDIE-----DVHSQVElMLTRKLGDIGKKIHSGRSRNDQVLVDLKLYIRSRIEDV 129
Cdd:cd01360 32 AKLGVIpaeaAEEIRKkAKFDVErvKEIEaetkhDVIAFVT-AIAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 130 TKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAGYGSSFPL- 208
Cdd:cd01360 111 LKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKISGAVGTYANLGPe 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 209 --NRTMTTRLLGFDSMDYNVV----YAQmgrgktervVAQALGGIAATIAKLS-----------------FDAcmfnSQn 265
Cdd:cd01360 191 veERVAEKLGLKPEPISTQVIqrdrHAE---------YLSTLALIASTLEKIAteirhlqrtevleveepFSK----GQ- 256
|
250 260
....*....|....*....|....*..
gi 1518537807 266 fgfiklpdeytTGSSIMPHKKNPDVFE 292
Cdd:cd01360 257 -----------KGSSAMPHKRNPILSE 272
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
107-293 |
1.42e-09 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 60.00 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 107 GRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLA 186
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 187 AYSVTNRNPLG-SAAGYGssfpLN------RTMTTRLLGFDSMDY----NVVYA-QMGRGKTErvVAQALGGIAATIAKL 254
Cdd:PRK13353 218 AREHLYEVNLGgTAVGTG----LNadpeyiERVVKHLAAITGLPLvgaeDLVDAtQNTDAFVE--VSGALKVCAVNLSKI 291
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1518537807 255 SFDACMFNS---QNFGFIKLPdEYTTGSSIMPHKKNPDVFEL 293
Cdd:PRK13353 292 ANDLRLLSSgprTGLGEINLP-AVQPGSSIMPGKVNPVMPEV 332
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
122-296 |
2.59e-09 |
|
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: 58.79 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 122 IRSRIEDVTKAMTGLfnvlieqSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLGSAAG 201
Cdd:cd01597 118 LERDLDALLDALARL-------AATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGGAAG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 202 YGSSFP------LNRTMttRLLGFDSMDynvvyaqmGRGKTERV----VAQALGGIAATIAKLSFDACMFNSQNFGFIKL 271
Cdd:cd01597 191 TLASLGdqglavQEALA--AELGLGVPA--------IPWHTARDriaeLASFLALLTGTLGKIARDVYLLMQTEIGEVAE 260
|
170 180
....*....|....*....|....*.
gi 1518537807 272 P-DEYTTGSSIMPHKKNPDVFELTRA 296
Cdd:cd01597 261 PfAKGRGGSSTMPHKRNPVGCELIVA 286
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
107-288 |
4.71e-09 |
|
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: 58.30 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 107 GRSRNDQVLVDLKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLla 186
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARI-- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 187 aYSVTNR----NPLGSAAGYGSSFPLN---------RTMTTRLLG-----FDSMDYNVVYAQmgrgktervVAQALGGIA 248
Cdd:cd01357 211 -YKARERlrevNLGGTAIGTGINAPPGyielvveklSEITGLPLKraenlIDATQNTDAFVE---------VSGALKRLA 280
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1518537807 249 ATIAKLSFDACMFNS---QNFGFIKLPdEYTTGSSIMPHKKNP 288
Cdd:cd01357 281 VKLSKIANDLRLLSSgprAGLGEINLP-AVQPGSSIMPGKVNP 322
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
116-288 |
4.77e-09 |
|
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: 58.10 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 116 VDLkLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAysvtnRNP 195
Cdd:cd03302 103 TDL-IQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERL-----RDD 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 196 LG-----SAAGYGSSF------------PLNRtMTTRLLGFDSMdYNVVyAQMGRGKTERVVAQALGGIAATIAKLSFDA 258
Cdd:cd03302 177 LRfrgvkGTTGTQASFldlfegdhdkveALDE-LVTKKAGFKKV-YPVT-GQTYSRKVDIDVLNALSSLGATAHKIATDI 253
|
170 180 190
....*....|....*....|....*....|.
gi 1518537807 259 CMFnsQNFGFIKLPDEYT-TGSSIMPHKKNP 288
Cdd:cd03302 254 RLL--ANLKEVEEPFEKGqIGSSAMPYKRNP 282
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
131-288 |
6.44e-08 |
|
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: 54.74 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 131 KAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAA----YSVtnrnPLG-SAAGYGss 205
Cdd:cd01596 157 PALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAAlerlREL----NLGgTAVGTG-- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 206 fpLN------RTMTTRL-----LGFDSMDyNVVYAQMGRGKTERVVAqALGGIAATIAKLSFDACMFNS---QNFGFIKL 271
Cdd:cd01596 231 --LNappgyaEKVAAELaeltgLPFVTAP-NLFEATAAHDALVEVSG-ALKTLAVSLSKIANDLRLLSSgprAGLGEINL 306
|
170
....*....|....*..
gi 1518537807 272 PdEYTTGSSIMPHKKNP 288
Cdd:cd01596 307 P-ANQPGSSIMPGKVNP 322
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
132-288 |
2.13e-07 |
|
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: 52.89 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 132 AMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLG-SAAGYGssfpLN- 209
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGgTAVGTG----LNa 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 210 -----RTMTTRL-----LGFDSMDyNVVYAQMGRgktERVVAQ--ALGGIAATIAKLSFDACMFNS---QNFGFIKLPdE 274
Cdd:cd01362 235 hpgfaEKVAAELaeltgLPFVTAP-NKFEALAAH---DALVEAsgALKTLAVSLMKIANDIRWLGSgprCGLGELSLP-E 309
|
170
....*....|....
gi 1518537807 275 YTTGSSIMPHKKNP 288
Cdd:cd01362 310 NEPGSSIMPGKVNP 323
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
118-288 |
1.91e-06 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 50.05 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 118 LKLYIRSRIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAysvtnRNPL- 196
Cdd:COG1027 146 IRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEA-----AELLr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 197 -----GSAAGYGssfpLN------RTMTTRL---LGFD------------SMDynvVYAQmgrgktervVAQALGGIAAT 250
Cdd:COG1027 221 evnlgGTAIGTG----LNappgyiELVVEHLaeiTGLPlvraenlieatqDTD---AFVE---------VSGALKRLAVK 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1518537807 251 IAKLSFD--------ACMFNSqnfgfIKLPdEYTTGSSIMPHKKNP 288
Cdd:COG1027 285 LSKICNDlrllssgpRAGLGE-----INLP-AVQPGSSIMPGKVNP 324
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
125-294 |
1.26e-05 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 47.43 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 125 RIEDVTKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAA----YSVtnrNPLGSAA 200
Cdd:PRK12273 158 SLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAaellREV---NLGATAI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 201 GYGssfpLN------RTMTTRL-----LGF-------DSMDYNVVYAQmgrgktervVAQALGGIAATIAKLSFDACMFN 262
Cdd:PRK12273 235 GTG----LNappgyiELVVEKLaeitgLPLvpaedliEATQDTGAFVE---------VSGALKRLAVKLSKICNDLRLLS 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1518537807 263 S---QNFGFIKLPdEYTTGSSIMPHKKNPDVFELT 294
Cdd:PRK12273 302 SgprAGLNEINLP-AVQAGSSIMPGKVNPVIPEVV 335
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
132-288 |
4.37e-05 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 45.47 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 132 AMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAA----YSVtnrnPLG-SAAGYGssf 206
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAAlphlYEL----ALGgTAVGTG--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 207 pLN------RTMTTRL-----LGFDSMDyNVVYAQmgRGKTERVVAQ-ALGGIAATIAKLSFDACMFNS---QNFGFIKL 271
Cdd:PRK00485 236 -LNahpgfaERVAEELaeltgLPFVTAP-NKFEAL--AAHDALVEASgALKTLAVSLMKIANDIRWLASgprCGLGEISL 311
|
170
....*....|....*...
gi 1518537807 272 PD-EytTGSSIMPHKKNP 288
Cdd:PRK00485 312 PEnE--PGSSIMPGKVNP 327
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
132-288 |
6.36e-05 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 45.02 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 132 AMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLTVLLAAYSVTNRNPLG-SAAGYGssfpLN- 209
Cdd:COG0114 163 ALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGgTAVGTG----LNa 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 210 -----RTMTTRL-----LGFDSMDyNVVYAQMGRgktERVVAQ--ALGGIAATIAKLSFDACMFNS---QNFGFIKLPD- 273
Cdd:COG0114 239 hpgfaERVAAELaeltgLPFVSAP-NKFEALAAH---DALVELsgALKTLAVSLMKIANDIRWLASgprCGLGEIRLPAn 314
|
170
....*....|....*
gi 1518537807 274 EytTGSSIMPHKKNP 288
Cdd:COG0114 315 E--PGSSIMPGKVNP 327
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
40-292 |
2.75e-03 |
|
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: 39.91 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 40 LAHITMLQSIGLLTKPELEtltaELRNIYKvieqgDFKIED-----DIE-----DVHSqVELMLTRKL---GDIGKK--- 103
Cdd:cd01598 25 LSNLEEIPEVPPLTKEELK----FLRAIIE-----NFSEEDalrikEIEattnhDVKA-VEYFLKEKFetlGLLKKIkef 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 104 IHSGRSRNDQVLVDLKLYIRSRIEDV-TKAMTGLFNVLIEQSERYKDVLMPGYTHLQVAMPSSFGLWFGAYAESLVDDLT 182
Cdd:cd01598 95 IHFACTSEDINNLAYALMIKEARNEViLPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518537807 183 VL-------------------LAAYSvtNRNPLGSAAGYGSSFPLNRT-MTTRLLGFDSMdynvvyaqmgrgkTErvVAQ 242
Cdd:cd01598 175 QLkqieilgkfngavgnfnahLVAYP--DVDWRKFSEFFVTSLGLTWNpYTTQIEPHDYI-------------AE--LFD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1518537807 243 ALGGIAATIAKLSFDACMFNSQNFgFIKLPDEYTTGSSIMPHKKNPDVFE 292
Cdd:cd01598 238 ALARINTILIDLCRDIWGYISLGY-FKQKVKKGEVGSSTMPHKVNPIDFE 286
|
|
| |
