|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
1-455 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 947.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 1 MALWGGRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNLTIILKDD 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 81 AEDIHSWVESKLIEKVGDLGKKLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 161 QPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 241 TASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 321 MQEDKEGIFDALETWQACLEIAELVLVDIQVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKE 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 493294414 401 PLEALSINEFQQFHHSIGDDVYPILSLESCLEKRCAKGGVNPQRVAEAIAVAKAN 455
Cdd:PRK04833 401 PLEDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAKAR 455
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
1-459 |
0e+00 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 784.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 1 MALWGGRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNLTIILKDD 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 81 AEDIHSWVESKLIEKVGDLGKKLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 161 QPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 241 TASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 321 MQEDKEGIFDALETWQACLEIAELVLVDIQVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKE 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 493294414 401 PLEALSINEFQQFHHSIGDDVYPILSLESCLEKRCAKGGVNPQRVAEAIAVAKANLASK 459
Cdd:PRK12308 401 ALEELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAAR 459
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
1-458 |
0e+00 |
|
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: 738.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 1 MALWGGRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNlTIILKDD 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAG-AFEFDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 81 AEDIHSWVESKLIEKVGDLGKKLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRA 160
Cdd:COG0165 82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 161 QPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 241 TASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 321 MQEDKEGIFDALETWQACLEIAELVLVDIQVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKE 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 493294414 401 PLEALSINEFQQFHHSIGDDVYPILSLESCLEKRCAKGGVNPQRVAEAIAVAKANLAS 458
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAA 459
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
3-457 |
0e+00 |
|
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: 704.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 3 LWGGRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNlTIILKDDAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREG-PFILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 83 DIHSWVESKLIEKVG-DLGKKLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 162 PVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLST 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 242 ASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 322 QEDKEGIFDALETWQACLEIAELVLVDIQVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKEP 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 493294414 402 LEALSINEFQQFHHSIGDDVYPILSLESCLEKRCAKGGVNPQRVAEAIAVAKANLA 457
Cdd:TIGR00838 400 LEELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG 455
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
1-457 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 701.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 1 MALWGGRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNlTIILKDD 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAG-KFEFSPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 81 AEDIHSWVESKLIEKVGDLGKKLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRA 160
Cdd:PRK00855 83 LEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 161 QPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 241 TASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 321 MQEDKEGIFDALETWQACLEIAELVLVDIQVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKE 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 493294414 401 PLEALSINEFQQFHHSIGDDVYPILSLESCLEKRCAKGGVNPQRVAEAIAVAKANLA 457
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
22-456 |
0e+00 |
|
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: 644.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 22 SLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNlTIILKDDAEDIHSWVESKLIEKVGDLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAG-AFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 102 KLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFS 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 182 RLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNS 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 262 GESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKDMQEDKEGIFDALETWQACLEI 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 342 AELVLVDIQVNTERTREAAQQGYANATELADYLVA-KGVPFREAHHIVGEAVVYAISKKEPLEALSINEFQQFHHSIGDD 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 493294414 421 VYPILSLESCLEKRCAKGGVNPQRVAEAIAVAKANL 456
Cdd:cd01359 400 VREALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-450 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 571.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 3 LWGGRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNlTIILKDDAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAG-KFEWRPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 83 DIHSWVESKLIEKVGDLGKKLHTGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 163 VTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLSTA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 243 SISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 323 EDKEGIFDALETWQACLEIAELVLVDIQVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKEPL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 493294414 403 EALSINEFQQFHHSIGDDVYPILSLESCLEKRCAKGGVNPQRVAEAIA 450
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLE 464
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
33-352 |
9.09e-121 |
|
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: 355.27 E-value: 9.09e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 33 DIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNLTIILKDDaEDIHSWVESKLIEKVGDL-GKKLHTGRSRND 111
Cdd:cd01334 4 DLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSG-THDVMAVEEVLAERAGELnGGYVHTGRSSND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 112 QVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMS 191
Cdd:cd01334 83 IVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 192 TCPLGSGALAGTAYG--IDRDLLARDLGFEEATRNSLDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSGESGFLEM 269
Cdd:cd01334 163 VLPLGGGAVGTGANAppIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEVEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 270 SDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKDMQEDKEGIFDALETWQACLEIAELVLVDI 349
Cdd:cd01334 243 PDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGL 322
|
...
gi 493294414 350 QVN 352
Cdd:cd01334 323 EVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
3.98e-103 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 309.68 E-value: 3.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 6 GRFTQQADAKFKYFNNSLRFDYRLAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVRAEVESNLTIILKDDAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 86 SWVESKLIEKVGDL-------GKKLHTGRSRNDQVAVDIKMWCKvQAV------ALQERIRALQERlvsvAEENQESVMP 152
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALK-DALsevllpALRQLIDALKEK----AKEFADIVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 153 GYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDR---DLLARDLGFEEA----TRNS 225
Cdd:pfam00206 156 GRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPefaELVAKELGFFTGlpvkAPNS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493294414 226 LDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSGESGFLEMSDRV-TSGSSLMPQKKNPDACELIRGKSGRVFG 301
Cdd:pfam00206 236 FEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEgEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
48-405 |
9.33e-60 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 210.09 E-value: 9.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 48 GILTVAELEQLIAALKEVRaevESNLTIILKDDA-EDIHSWVESKLIEKVG-DLGKKLHTGRSRNDQVAVDIKMWCKVQA 125
Cdd:PRK02186 456 GIVAPERARPLLDAHRRLR---DAGFAPLLARPApRGLYMLYEAYLIERLGeDVGGVLQTARSRNDINATTTKLHLREAT 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 126 VALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAY 205
Cdd:PRK02186 533 SRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTF 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 206 GIDRDLLARDLGFEEATRNSLDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQKKN 285
Cdd:PRK02186 613 PIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKN 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 286 PDACELIRGKSGRVFGALNGLLTTLKGLPlaYNKDMQEDKEG---IFDALETWQACLEIAELVLVDIQVNTERTREAAQQ 362
Cdd:PRK02186 693 PFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMngpIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLED 770
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 493294414 363 GYANATELADYLVA-KGVPFREAHHIVGEAVVYAISKKE----PLEAL 405
Cdd:PRK02186 771 GGVSATAVAESLVVrRSISFRSAHTQVGQAIRQSLDQGRssadALAAL 818
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
87-341 |
1.89e-57 |
|
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: 189.36 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 87 WVESKLIEKVGDLGKKLH------TGRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRA 160
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 161 QPVTFAHWCMAYYEMLERDFSRLSDAnkrmstcplgsgalagtaygidrdllardlgfeeatrnsldsvsdrdHILELLS 240
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 241 TASISMMHLSRFAEDLIIFNSGESGFL-EMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNK 319
Cdd:cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELgEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|..
gi 493294414 320 DMQEDKEGIFDALETWQACLEI 341
Cdd:cd01594 208 DSPSMREILADSLLLLIDALRL 229
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
44-449 |
8.25e-49 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 174.40 E-value: 8.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 44 ITSVGILTVAELEQLIAALKEVRAEVESNLtiILKDDAEDIHSWVESKLI-EKVGDLGKKLHTGRSRNDQVAVDIKMWCK 122
Cdd:PRK06705 52 LTEENLMKKEEAKFILHALKKVEEIPEEQL--LYTEQHEDLFFLVEHLISqEAKSDFVSNMHIGRSRNDMGVTMYRMSLR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 123 VQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAG 202
Cdd:PRK06705 130 RYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALST 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 203 TAYGIDRDLLARDLGFEEATRNSLDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSGESGFLEMSDRVTSGSSLMPQ 282
Cdd:PRK06705 210 TSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 283 KKNPDACELIRGKSGRVFGALNGLLTTLKGLPLAYNKDMQEDKEG-IFDALETWQACLEIAELVLVDIQVNTERTREAAQ 361
Cdd:PRK06705 290 KRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKRRSY 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 362 QGYANATELADYLVAK-GVPFREAHHIVGEAVVYAISKKEPLEAL---SINEFQQFHHSIG---DDVYPILSLESCLEKR 434
Cdd:PRK06705 370 KHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELcfkDVNIYLQEKFKIQlleKEWEEIISPEAFIQKR 449
|
410
....*....|....*
gi 493294414 435 CAKGGVNPQRVAEAI 449
Cdd:PRK06705 450 NVYGGPSKKEMERMI 464
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-435 |
1.12e-36 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 139.64 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 1 MALWGGrfTQQADAKFKYFNNSLRFDYR----LAIQDIEGSIGWAKAITSVGILTVAELEQLIAALKEVraeVESNLTII 76
Cdd:PRK06389 1 MKIWSG--GAGEELENDFYDNIVKDDIDadknLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDI---YKNGIEID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 77 LKDdaEDIHSWVESKLIEKVGDLGKKLHTGRSRNDQVAVDIKMWckvqavaLQERIRALQERLVSVAEE----NQESVMP 152
Cdd:PRK06389 76 LDL--EDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLF-------IIDKIIEIEKILYEIIKVipgfNLKGRLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 153 GYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALAGTAYGIDRDLLARDLGFEEATRNSLDSVSD- 231
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLy 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 232 RDHILELLSTASISMMHLSRFAEDLIIFNsgESGFLEMSDRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLK 311
Cdd:PRK06389 227 IKTIENISYLISSLAVDLSRICQDIIIYY--ENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 312 GLPLAYNKDMQEDKEGIFDALETWQACLeiaeLVLVDI--QVNTERTREAAQQGYANATELADYLVAKGVPFREAHHIVG 389
Cdd:PRK06389 305 NKTTGYHRDFQIVKDSTISFINNFERIL----LGLPDLlyNIKFEITNEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIG 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 493294414 390 EAV-----VYAISKKEPLEALSINEFQQFHHSIGDDVYPILSLESCLEKRC 435
Cdd:PRK06389 381 NKIregevLDEYQPEDLTDYIDVNELKRINHNIKIIIEPREKLIEYAENLI 431
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
1.99e-30 |
|
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of argininosuccinate lyase.
Pssm-ID: 464268 [Multi-domain] Cd Length: 68 Bit Score: 112.13 E-value: 1.99e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493294414 364 YANATELADYLVAKGVPFREAHHIVGEAVVYAISKKEPLEALSINEFQQFHHSIGDDVYPILSLESCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
124-405 |
8.97e-24 |
|
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: 103.09 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 124 QAVALQER-IRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsGAlAG 202
Cdd:cd01597 113 DALDLLERdLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFG-GA-AG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 203 T-----AYGID-RDLLARDLGFEEATRNSLdsvSDRDHILELLSTASISMMHLSRFAEDLIIFNSGESGFL-EMSDRVTS 275
Cdd:cd01597 191 TlaslgDQGLAvQEALAAELGLGVPAIPWH---TARDRIAELASFLALLTGTLGKIARDVYLLMQTEIGEVaEPFAKGRG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 276 GSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTlkglplaynkdMQEDKEGifdALETWQA--------------CLEI 341
Cdd:cd01597 268 GSSTMPHKRNPVGCELIVALARRVPGLAALLLDA-----------MVQEHER---DAGAWHAewialpeifllasgALEQ 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493294414 342 AELVLVDIQVNTERTRE--AAQQGYANAtELADYLVAKGVPFREAHHIVGEAVVYAISKKEPLEAL 405
Cdd:cd01597 334 AEFLLSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREV 398
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
17-388 |
7.19e-23 |
|
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: 99.89 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 17 KYFNNSLRFDYRLaiqDIEgsIGWAKAITSVGILTVAELEQLIAALKEVRAEVESnltiILKDDAE---DIHSwVESKLI 93
Cdd:cd01595 3 AIFSEENKLRTWL---DVE--AALAEAQAELGLIPKEAAEEIRAAADVFEIDAER----IAEIEKEtghDVIA-FVYALA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 94 EKVGDLGKK-LHTGRSRNDQV----AVDIKmwckvQAVA-LQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAH 167
Cdd:cd01595 73 EKCGEDAGEyVHFGATSQDINdtalALQLR-----DALDiILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 168 WCMAYYEMLERDFSRLSDANKRMSTCPLgSGAlAGT---AYGIDRDL---LARDLGFEEATRNSLdsVSDRDHILELLST 241
Cdd:cd01595 148 KFAVWAAELLRHLERLEEARERVLVGGI-SGA-VGThasLGPKGPEVeerVAEKLGLKVPPITTQ--IEPRDRIAELLSA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 242 asISMMH--LSRFAEDLIIFNSGESGFLE---MSDRVtsGSSLMPQKKNPDACELIRGKSGRVFGALNGLLTTLkglpla 316
Cdd:cd01595 224 --LALIAgtLEKIATDIRLLQRTEIGEVEepfEKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALENL------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 317 yNKDMQED------KEGIF-DALETWQACLEIAELVLVDIQVNTER-TREAAQQGYANATE---LAdyLVAKGVPFREAH 385
Cdd:cd01595 294 -VQWHERDlsdssvERNILpDAFLLLDAALSRLQGLLEGLVVNPERmRRNLDLTWGLILSEavmMA--LAKKGLGRQEAY 370
|
...
gi 493294414 386 HIV 388
Cdd:cd01595 371 ELV 373
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
128-405 |
1.35e-21 |
|
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: 96.69 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 128 LQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsGAlAGT--AY 205
Cdd:COG0015 118 LLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIG-GA-VGTyaAH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 206 GID----RDLLARDLGFEEATrnSLDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSGEsgFLEMSDRVTS---GSS 278
Cdd:COG0015 196 GEAwpevEERVAEKLGLKPNP--VTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTE--VGEVEEPFAKgqvGSS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 279 LMPQKKNPDACELIRGKSGRVFGALNGLLTTLkglplaynkdMQEDKEGIFDaletWQA--------------CLEIAEL 344
Cdd:COG0015 272 AMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSD----SSVernilpdafllldgALERLLK 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493294414 345 VLVDIQVNTERTRE--AAQQGYANATELADYLVAKGVPFREAHHIVGEAVVYAISKKEPLEAL 405
Cdd:COG0015 338 LLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL 400
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-383 |
5.28e-21 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 95.05 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 106 GRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSD 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 186 ANKRMSTCPLGSGALaGTAYGIDRDL-------LARDLGFEEATRNSL-DSVSDRDHILELLSTASISMMHLSRFAEDLI 257
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEYiervvkhLAAITGLPLVGAEDLvDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 258 IFNSG-ESGFLEMS-DRVTSGSSLMPQKKNPDACELIRGKSGRVFGalNGLLTTL--KGLPLAYNKDMQEDKEGIFDALE 333
Cdd:PRK13353 297 LLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIG--NDVTITLaaEAGQLELNVMEPVIAFNLLESIS 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493294414 334 TWQ-ACLEIAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFRE 383
Cdd:PRK13353 375 ILTnACRAFTDNCVKGIEANEERCKEYVEKsvgiatalnphiGYEAAARIAKEAIATGRSVRE 437
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
61-294 |
3.13e-16 |
|
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: 79.90 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 61 ALKEVRAEVESNLTIILKDDAE---DIHSWVESkLIEKVGDLGKKLHTGRSRNDQV----AVDIKMWCKVqavaLQERIR 133
Cdd:cd01360 41 AAEEIRKKAKFDVERVKEIEAEtkhDVIAFVTA-IAEYCGEAGRYIHFGLTSSDVVdtalALQLREALDI----ILKDLK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 134 ALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLgSGALaGTAYGID---RD 210
Cdd:cd01360 116 ELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKI-SGAV-GTYANLGpevEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 211 LLARDLGFEEATRNSldSVSDRDHILELLSTASISMMHLSRFAedLIIFNSGESGFLEMSDRVTS---GSSLMPQKKNPD 287
Cdd:cd01360 194 RVAEKLGLKPEPIST--QVIQRDRHAEYLSTLALIASTLEKIA--TEIRHLQRTEVLEVEEPFSKgqkGSSAMPHKRNPI 269
|
....*..
gi 493294414 288 ACELIRG 294
Cdd:cd01360 270 LSENICG 276
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-383 |
4.08e-16 |
|
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: 80.26 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 106 GRSRNDQVAVDIKMWCKVQAVALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSD 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 186 ANKRMSTCPLGsgalaGTAYG---------IDR--DLLARDLGFE-EATRNSLDSVSDRDHILELLSTASISMMHLSRFA 253
Cdd:cd01357 213 ARERLREVNLG-----GTAIGtginappgyIELvvEKLSEITGLPlKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 254 EDLIIFNSG-ESGFLEMS-DRVTSGSSLMPQKKNPDACELIRGKSGRVFGalNGLLTTLKG----------LPL-AYNkd 320
Cdd:cd01357 288 NDLRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIG--NDLTITMAAeagqlelnvfEPViAYN-- 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493294414 321 mqedkegIFDALETWQ-ACLEIAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFRE 383
Cdd:cd01357 364 -------LLESIDILTnAVRTLRERCIDGITANEERCREYVENsigivtalnpyiGYEAAAEIAKEALETGRSVRE 432
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
125-384 |
6.68e-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: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 125 AVALQER----IRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsgal 200
Cdd:cd01596 148 ALALLERllpaLEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLG---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 201 aGTAYG---------IDR--DLLAR--DLGFEEATrNSLDSVSDRDHILEL---LSTASISMMHLsrfAEDLIIFNSG-E 263
Cdd:cd01596 224 -GTAVGtglnappgyAEKvaAELAEltGLPFVTAP-NLFEATAAHDALVEVsgaLKTLAVSLSKI---ANDLRLLSSGpR 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 264 SGFLEMS-DRVTSGSSLMPQKKNPDACELIRGKSGRVFGalNGLLTTLKG----------LPL-AYNkdmqedkegIFDA 331
Cdd:cd01596 299 AGLGEINlPANQPGSSIMPGKVNPVIPEAVNMVAAQVIG--NDTAITMAGsagqlelnvfKPViAYN---------LLQS 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493294414 332 LETWQ-ACLEIAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFREA 384
Cdd:cd01596 368 IRLLAnACRSFRDKCVEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
125-384 |
4.80e-11 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 64.44 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 125 AVALQER----IRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsgal 200
Cdd:cd01362 149 ALALQERllpaLKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALG---- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 201 aGTAYG--------IDRDLLAR-----DLGFEEATrNSLDSVSDRDHILEL---LSTASISMMHLsrfAEDLIIFNSG-E 263
Cdd:cd01362 225 -GTAVGtglnahpgFAEKVAAElaeltGLPFVTAP-NKFEALAAHDALVEAsgaLKTLAVSLMKI---ANDIRWLGSGpR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 264 SGFLEMS-DRVTSGSSLMPQKKNPDACELIRGKSGRVFG--------ALNGLLTTLKGLPL-AYNkdmqedkegifdALE 333
Cdd:cd01362 300 CGLGELSlPENEPGSSIMPGKVNPTQCEALTMVAAQVMGndaaitiaGSSGNFELNVFKPViIYN------------LLQ 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493294414 334 TWQ----ACLEIAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFREA 384
Cdd:cd01362 368 SIRlladACRSFADKCVAGIEPNRERIAELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKEA 434
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
143-417 |
1.54e-10 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 63.09 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 143 AEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGSGALaGTAYGIDRDL-------LARD 215
Cdd:PRK14515 181 AEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAV-GTGLNADPEYieavvkhLAAI 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 216 LGFEEATRNSL-DSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSG-ESGFLE-MSDRVTSGSSLMPQKKNPDACELI 292
Cdd:PRK14515 260 SELPLVGAEDLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGpRVGLAEiMLPARQPGSSIMPGKVNPVMPEVI 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 293 RGKSGRVFGALNGLLTTLKGLPLAYNkdmQEDKEGIFDALETWQ----ACLEIAELVLVDIQVNTERTREAAQQ------ 362
Cdd:PRK14515 340 NQIAFQVIGNDHTICLASEAGQLELN---VMEPVLVFNLLQSISimnnGFRAFTDNCLKGIEANEDRLKEYVEKsvgiit 416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493294414 363 ------GYANATELADYLVAKGVPFREAhhivgeAVVYAISKKEPLEaLSINEFQQFHHSI 417
Cdd:PRK14515 417 avnphiGYEAAARVAKEAIATGQSVREL------CVKNGVLSQEDLE-LILDPFEMTHPGI 470
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
125-384 |
7.02e-10 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 60.88 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 125 AVALQER----IRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsgal 200
Cdd:PRK00485 153 VLAIVERllpaLEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALG---- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 201 aGTAYG-------------IDRdlLARDLG--FEEAtRNSLDSVSDRDHILEL---LSTASISMMHLsrfAEDLIIFNSG 262
Cdd:PRK00485 229 -GTAVGtglnahpgfaervAEE--LAELTGlpFVTA-PNKFEALAAHDALVEAsgaLKTLAVSLMKI---ANDIRWLASG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 263 -ESGF-------LEmsdrvtSGSSLMPQKKNPDACELIRGKSGRVFGalNGLLTTLKG----------LPL-AYNkdmqe 323
Cdd:PRK00485 302 pRCGLgeislpeNE------PGSSIMPGKVNPTQCEALTMVCAQVMG--NDAAVTFAGsqgnfelnvfKPViAYN----- 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493294414 324 dkegifdALETWQ----ACLEIAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFREA 384
Cdd:PRK00485 369 -------FLQSIRlladAMRSFADHCVVGIEPNRERIKELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKEA 438
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
125-384 |
8.57e-10 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 60.47 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 125 AVALQERI----RALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsgal 200
Cdd:PLN00134 145 ATEIHSRLipalKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQG---- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 201 aGTAYGIDrdlLARDLGFEEA--------TR-------NSLDSVSDRDHILEL---LSTASISmmhLSRFAEDLIIFNSG 262
Cdd:PLN00134 221 -GTAVGTG---LNTKKGFDEKiaaavaeeTGlpfvtapNKFEALAAHDAFVELsgaLNTVAVS---LMKIANDIRLLGSG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 263 -ESGFLEMS-DRVTSGSSLMPQKKNPDACELIRGKSGRVFGALNGL----------LTTLKGLpLAYNkdMQEDKEGIFD 330
Cdd:PLN00134 294 pRCGLGELNlPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAItvggsaghfeLNVFKPL-IAYN--LLHSIRLLGD 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493294414 331 ALETWqacleiAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFREA 384
Cdd:PLN00134 371 ASASF------RKNCVRGIEANRERISKLLHEslmlvtalnpkiGYDKAAAVAKKAHKEGTTLKEA 430
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
128-390 |
1.60e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 56.67 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 128 LQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLGsgalaGTAYG- 206
Cdd:PRK12273 162 LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLG-----ATAIGt 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 207 --------IDR--DLLAR--DLGFEEATrNSLDSVSDRDHILELLSTASISMMHLSRFAEDLIIFNSG-ESGFLEMS-DR 272
Cdd:PRK12273 237 glnappgyIELvvEKLAEitGLPLVPAE-DLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGpRAGLNEINlPA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 273 VTSGSSLMPQKKNPDACELIRGKSGRVFGalNGLLTTLKG----------LPL-AYNkdmqedkegIFDALETWQ-ACLE 340
Cdd:PRK12273 316 VQAGSSIMPGKVNPVIPEVVNQVCFQVIG--NDTTVTMAAeagqlelnvmEPViAYN---------LFESISILTnACRT 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493294414 341 IAELVLVDIQVNTERTREAAQQ------------GYANATELADYLVAKGVPFREahhIVGE 390
Cdd:PRK12273 385 LREKCIDGITANEERCREYVENsigivtalnpyiGYENAAEIAKEALETGKSVRE---LVLE 443
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
127-402 |
5.95e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 54.64 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 127 ALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDANKRMSTCPLG--SGALA--G 202
Cdd:PRK09053 126 LLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGgaAGTLAslG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 203 TAYGIDRDLLARDLGFEeatrnsLDSVS---DRDHILELLSTASISMMHLSRFAEDLIIFNSGESGFL-EMSDRVTSGSS 278
Cdd:PRK09053 206 EQALPVAQALAAELQLA------LPALPwhtQRDRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVfEPAAAGKGGSS 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 279 LMPQKKNPDACELIRGKSGRVfgalNGLLTTL-KGLPlaynkdmQEDKEgifdALETWQA--------------CLEIAE 343
Cdd:PRK09053 280 TMPHKRNPVGCAAVLTAATRA----PGLVATLfAAMP-------QEHER----ALGGWHAewdtlpelaclaagALAQMA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493294414 344 LVLVDIQVNTERTRE--AAQQG--YANATELAdylVAKGVPFREAHHIVGEAVVYAISKKEPL 402
Cdd:PRK09053 345 QIVEGLEVDAARMRAnlDLTHGliLAEAVMLA---LADRIGRLDAHHLVEQASKRAVAEGRHL 404
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
41-292 |
6.91e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 54.29 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 41 AKAITSVGILTVAELEQLIAALKEVRAEVeSNLTIILKDDAEDIHSWVEsKLIEKVG-DLGKKLHTGRSRNDqvAVDIKM 119
Cdd:PRK05975 41 AEAEAEHGIIPAEAAERIAAACETFEPDL-AALRHATARDGVVVPALVR-QLRAAVGeEAAAHVHFGATSQD--VIDTSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 120 WCKVQAVA--LQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLERDFSRLSDAnkRMSTCPLGS 197
Cdd:PRK05975 117 MLRLKAASeiLAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEAL--RADVFPLQF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 198 GALAGT------AYGIDRDLLARDLGFEEATR--NSLDSVSDRDHILELLSTAsismmhLSRFAEDLIIfnsgesgFLEM 269
Cdd:PRK05975 195 GGAAGTleklggKAAAVRARLAKRLGLEDAPQwhSQRDFIADFAHLLSLVTGS------LGKFGQDIAL-------MAQA 261
|
250 260
....*....|....*....|....*..
gi 493294414 270 SDRVT----SGSSLMPQKKNPDACELI 292
Cdd:PRK05975 262 GDEISlsggGGSSAMPHKQNPVAAETL 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-402 |
5.93e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 44.25 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 249 LSRFAEDLIIFNSGESGFLEMSDRVTS-GSSLMPQKKNPDACELIrgksgrvfgalNGLLTTLKGLPLAYNKDMQEDKEG 327
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGQkGSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 328 -----------IFDALETWQACLEIAELVLVDIQVNTER-TREAAQQGYANATE-LADYLVAKGVPFREAHHIVGEAVVY 394
Cdd:PRK08937 99 dlshssaeriaLPDAFLALDYILNRFVNILENLVVFPENiERNLDKTLGFIATErVLLELVEKGMGREEAHELIREKAME 178
|
....*...
gi 493294414 395 AISKKEPL 402
Cdd:PRK08937 179 AWKNQKDL 186
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
123-301 |
6.01e-05 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 45.30 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 123 VQAV--ALQERIRALQERLVSVAEENQESVMPGYTHLQRAQPVTFAHWCMAYYEMLerDFSRLSDANKRMSTCPLGSGal 200
Cdd:PRK12425 151 AQAVheQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQL--DYAERAIRAALPAVCELAQG-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 201 aGTAYGIDrdlLARDLGFEEA---------------TRNSLDSVSDRDHILEL---LSTASISMMHLsrfAEDLIIFNSG 262
Cdd:PRK12425 227 -GTAVGTG---LNAPHGFAEAiaaelaalsglpfvtAPNKFAALAGHEPLVSLsgaLKTLAVALMKI---ANDLRLLGSG 299
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493294414 263 -ESGFLEMSDRVTS-GSSLMPQKKNPDACELIRGKSGRVFG 301
Cdd:PRK12425 300 pRAGLAEVRLPANEpGSSIMPGKVNPTQCEALSMLACQVMG 340
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
138-290 |
1.15e-04 |
|
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: 44.23 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 138 RLVSVAEENQESVMPGYTHLQRAQPVTFA-HWCMAYYEML--ERDFSRLSDANK-RMSTCPLGSGALAGTAYGIDRD--- 210
Cdd:cd03302 125 RLAEFALEYKDLPTLGFTHYQPAQLTTVGkRACLWIQDLLmdLRNLERLRDDLRfRGVKGTTGTQASFLDLFEGDHDkve 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493294414 211 ----LLARDLGFEEATrNSLDSVSDRDHILELLSTASISMMHLSRFAEDLII---FNSGESGFleMSDRVtsGSSLMPQK 283
Cdd:cd03302 205 aldeLVTKKAGFKKVY-PVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLlanLKEVEEPF--EKGQI--GSSAMPYK 279
|
....*..
gi 493294414 284 KNPDACE 290
Cdd:cd03302 280 RNPMRSE 286
|
|
| |
