|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
1-613 |
0e+00 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 1302.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 1 MALWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPEQILRSD 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 161 QPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 241 IASISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGC 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 401 ALEELTIAEMKEFSEVIEEDVYDILTIESCLEKRSALGGVSPQQVAYAVDQAEKRLSQRDTSIVKVRPARLTDIEALEGM 480
Cdd:PRK12308 401 ALEELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAARDTSGVKVRPARLTDIDAIEGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 481 VAYWANMGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYVYDSGLAEIRSLGVEAGWQGQGQGTAIVQHLVEKARQMA 560
Cdd:PRK12308 481 VAYWAGLGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYIYDSGLAEIRSLGVEAGWQVQGQGSALVQYLVEKARQMA 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1633128600 561 IKKVFVLTRTPEFFMKHDFLPTSKSLLPEKVLKDCDQCPRQHACDEVALEVNL 613
Cdd:PRK12308 561 IKKVFVLTRVPEFFMKQGFSPTSKSLLPEKVLKDCDQCPRQHACDEVALEVNL 613
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
1-455 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 956.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 1 MALWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPEQILRSD 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 161 QPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 241 IASISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGC 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1633128600 401 ALEELTIAEMKEFSEVIEEDVYDILTIESCLEKRSALGGVSPQQVAYAVDQAEKR 455
Cdd:PRK04833 401 PLEDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAKAR 455
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
1-459 |
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: 729.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 1 MALWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPEQiLRSD 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFE-FDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRA 160
Cdd:COG0165 82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 161 QPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 241 IASISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGC 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1633128600 401 ALEELTIAEMKEFSEVIEEDVYDILTIESCLEKRSALGGVSPQQVAYAVDQAEKRLSQR 459
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAAL 460
|
|
| 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: 712.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 3 LWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPeQILRSDAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGP-FILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 83 DIHSWVEQQLIGKVG-DLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 162 PVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMSI 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 242 ASISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 322 QEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGCA 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1633128600 402 LEELTIAEMKEFSEVIEEDVYDILTIESCLEKRSALGGVSPQQVAYAVDQAEKRLS 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: 679.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 1 MALWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPEQILRSD 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 81 aEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRA 160
Cdd:PRK00855 84 -EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 161 QPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 241 IASISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGC 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1633128600 401 ALEELTIAEMKEFSEVIEEDVYDILTIESCLEKRSALGGVSPQQVAYAVDQAEKRLS 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: 631.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 22 SLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVmEDPEQILRSDAEDIHSWVEQQLIGKVGDLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEI-EAGAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 102 KLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYS 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 182 RLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMSIASISMLHLSRLAEDMIFYNS 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 262 GESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDMQEDKEGLFDALDTWNDCMEM 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 342 AALCFDGIKVNGERTLEAAKQGYANSTELADYLVA-KGIPFREAHHIVGVTVVAAIAKGCALEELTIAEMKEFSEVIEED 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 1633128600 421 VYDILTIESCLEKRSALGGVSPQQVAYAVDQAEKRL 456
Cdd:cd01359 400 VREALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-454 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 543.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 3 LWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVmEDPEQILRSDAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEI-EAGKFEWRPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 163 VTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMSIA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 243 SISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGCAL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1633128600 403 EELTIAEMKEFSEVIEEDVYDILTIESCLEKRSALGGVSPQQVAyavDQAEK 454
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVL---EQLEK 465
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
31-352 |
2.27e-119 |
|
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: 357.58 E-value: 2.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 31 EQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPEQILRSDaEDIHSWVEQQLIGKVGDL-GKKLHTGRSR 109
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSG-THDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 110 NDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLNDAIKR 189
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 190 LDTCPLGSGALAGTAY--PMDREELAHNLGFRRATRNSLDSVSDRDHVMELMSIASISMLHLSRLAEDMIFYNSGESNFI 267
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 268 ELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDMQEDKEGLFDALDTWNDCMEMAALCFD 347
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....*
gi 1633128600 348 GIKVN 352
Cdd:cd01334 321 GLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
2.65e-102 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 313.15 E-value: 2.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 6 GRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLELALNELKLEVMEDPEQILRSDAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 86 SWVEQQLIGKVGDL-------GKKLHTGRSRNDQVATDLKLWCRQQ-GNQLLLALDRLQSQMVNVASQHQETVLPGYTHL 157
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 158 QRAQPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDRE-------ELAHNLGFRRATRNSLDSVS 230
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaelvakELGFFTGLPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1633128600 231 DRDHVMELMSIASISMLHLSRLAEDMIFYNSGESNFIELADTV-TSGSSLMPQKKNPDALELIRGKTGRVYG 301
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEgEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
88-399 |
2.32e-59 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 213.56 E-value: 2.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 88 VEQQLIGKVG-DLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFA 166
Cdd:PRK02186 494 YEAYLIERLGeDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 167 HWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMSIASISM 246
Cdd:PRK02186 574 HYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAIS 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 247 LHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPlaYNKDMQEDKE 326
Cdd:PRK02186 654 TVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSP 731
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1633128600 327 G---LFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVA-KGIPFREAHHIVGVTVVAAIAKG 399
Cdd:PRK02186 732 MngpIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLEDGGVSATAVAESLVVrRSISFRSAHTQVGQAIRQSLDQG 808
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
87-343 |
2.06e-56 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 190.51 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 87 WVEQQLIGKVGDLGKKLH------TGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRA 160
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 161 QPVTFAHWCLAYVEMLERDYSRLNDAikrldtcplgsgalagtaypmdreelahnlgfrratrnsldsvsdrdHVMELMS 240
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 241 IASISMLHLSRLAEDMIFYNSGESNFIELAD-TVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNK 319
Cdd:cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|....
gi 1633128600 320 DMQEDKEGLFDALDTWNDCMEMAA 343
Cdd:cd01594 208 DSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
47-475 |
8.07e-53 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 189.04 E-value: 8.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 47 VNVLTEEEQQKLELA---LNEL-KLEVMEDPEQILRSDAEDIHSWVEQQLIGKVG-DLGKKLHTGRSRNDQVATDLKLWC 121
Cdd:PRK06705 49 IVMLTEENLMKKEEAkfiLHALkKVEEIPEEQLLYTEQHEDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYRMSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 122 RQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLGSGALA 201
Cdd:PRK06705 129 RRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 202 GTAYPMDREELAHNLGFRRATRNSLDSVSDRDHVMELMSIASISMLHLSRLAEDMIFYNSGESNFIELADTVTSGSSLMP 281
Cdd:PRK06705 209 TTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 282 QKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDMQED-----KEGLFDALDTWndCMEMAALcfDGIKVNgERT 356
Cdd:PRK06705 289 QKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDlqpylYKGIEKAIRVF--CIMNAVI--RTMKVE-EDT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 357 LEAAKQGYANS-TELADYLVAK-GIPFREAHHIVGVTVVAAIAKGCALEELTIAEMKEFSE------VIEEDVYDILTIE 428
Cdd:PRK06705 364 LKRRSYKHAITiTDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIYLQekfkiqLLEKEWEEIISPE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1633128600 429 SCLEKRSALGGVSPQQVAYAVDQaEKRLSQRDTSIVKVRPARLTDIE 475
Cdd:PRK06705 444 AFIQKRNVYGGPSKKEMERMINN-RKELFRKEEEVFEKEKQRILQAE 489
|
|
| PRK07757 |
PRK07757 |
N-acetyltransferase; |
464-609 |
1.65e-45 |
|
N-acetyltransferase;
Pssm-ID: 236088 [Multi-domain] Cd Length: 152 Bit Score: 158.43 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 464 VKVRPARLTDIEALEGMVAYWANMGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYVYDSGLAEIRSLGVEAGWQGQG 543
Cdd:PRK07757 2 MEIRKARLSDVKAIHALINVYAKKGLMLPRSLDELYENIRDFYVAEEEGEIVGCCALHILWEDLAEIRSLAVSEDYRGQG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633128600 544 QGTAIVQHLVEKARQMAIKKVFVLTRTPEFFMKHDFLPTSKSLLPEKVLKDCDQCPRQHACDEVAL 609
Cdd:PRK07757 82 IGRMLVEACLEEARELGVKRVFALTYQPEFFEKLGFREVDKEALPQKVWADCIKCPKFPNCDEIAM 147
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-437 |
1.72e-36 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 141.96 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 1 MALWGGRFTQAADTRFKDF--NDSLRFDYRLAEQDIVGSIAWSKALLSVNVLTEEEQQKLelaLNELkLEVMEDPEQIlR 78
Cdd:PRK06389 1 MKIWSGGAGEELENDFYDNivKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCV---INAL-IDIYKNGIEI-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 79 SDAEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLklwcrqqgnqLLLALDR-------LQSQMVNVASQHQETVL 151
Cdd:PRK06389 76 LDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADL----------NLFIIDKiieiekiLYEIIKVIPGFNLKGRL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 152 PGYTHLQRAQPVTFAHWcLAYVE-MLERDYSRLNDAIKRLDTCPLGSGALAGTAYPMDREELAHNLGFRRATRNSLDSVS 230
Cdd:PRK06389 146 PGYTHFRQAMPMTVNTY-INYIKsILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 231 DRDHVMELMS--IASISMlHLSRLAEDMIFYNsgESNFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMM 308
Cdd:PRK06389 225 LYIKTIENISylISSLAV-DLSRICQDIIIYY--ENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 309 TVKALPLAYNKDMQEDKEGLFDALDTWNDCMEMAALCFDGIKVngERTLEAAKQGYANSTELADYLVAKGIPFREAHHIV 388
Cdd:PRK06389 302 SELNKTTGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKF--EITNEKNIKNSVYATYNAWLAFKNGMDWKSAYAYI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1633128600 389 GvtvvAAIAKGCALEELT------IAEMKEFSEVIEEDVYDILTIESCLEKRSAL 437
Cdd:PRK06389 380 G----NKIREGEVLDEYQpedltdYIDVNELKRINHNIKIIIEPREKLIEYAENL 430
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
7.73e-31 |
|
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: 114.82 E-value: 7.73e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633128600 364 YANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGCALEELTIAEMKEFSEVIEEDVYDILTIESCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
464-613 |
3.89e-30 |
|
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440859 [Multi-domain] Cd Length: 132 Bit Score: 115.09 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 464 VKVRPARLTDIEALEGMVAYWAnmgenlprsrneLVRDIGSFAVAEHHGEVTGCASLYVYDSGLAEIRSLGVEAGWQGQG 543
Cdd:COG1246 1 MTIRPATPDDVPAILELIRPYA------------LEEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRG 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1633128600 544 QGTAIVQHLVEKARQMAIKKVFVLTRTP--EFFMKHDFLPTSKSLLPEkvlkdcdqcPRQHACDEVALEVNL 613
Cdd:COG1246 69 IGRRLLEALLAEARELGLKRLFLLTTSAaiHFYEKLGFEEIDKEDLPY---------AKVWQRDSVVMEKDL 131
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
38-310 |
1.36e-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: 102.97 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 38 IAWSKALLSVNVLTEEEQQKLELALNELKLevmeDPEQILRSDAE---DIHSwVEQQLIGKVGDLGKK-LHTGRSRNDQV 113
Cdd:cd01595 19 AALAEAQAELGLIPKEAAEEIRAAADVFEI----DAERIAEIEKEtghDVIA-FVYALAEKCGEDAGEyVHFGATSQDIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 114 ATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTC 193
Cdd:cd01595 94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 194 ----PLGSGALAGTAYPMDREELAHNLGFRRATRNSLdsVSDRDHVMELMSIasISMLH--LSRLAEDMIFYNSGESNFI 267
Cdd:cd01595 174 gisgAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQ--IEPRDRIAELLSA--LALIAgtLEKIATDIRLLQRTEIGEV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1633128600 268 EL---ADTVtsGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTV 310
Cdd:cd01595 250 EEpfeKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALENL 293
|
|
| N-Ac-Glu-synth |
TIGR01890 |
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ... |
383-589 |
2.49e-22 |
|
amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 273856 [Multi-domain] Cd Length: 429 Bit Score: 99.87 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 383 EAHHIVGVTVVAAI--AKGCALEELTIAEMKEFSEVIEEDvYDILTIESCLEkrSALGGVSPQQ-VAYAVDQAE-KRLSQ 458
Cdd:TIGR01890 193 KADKLIYFTLSPGIsdPDGTLAAELSPQEVESLAERLGSE-TTRRLLSAAVK--ACRGGVHRSHiVSYAEDGSLlQELFT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 459 RD---TSIVK-----VRPARLTDIEALEGMVAYWANMGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYVY-DSGLAE 529
Cdd:TIGR01890 270 RDgigTSISKeafesIRQATIDDIGGIAALIRPLEEQGILVRRSREYLEREISEFSIIEHDGNIIGCAALYPYaEEDCGE 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633128600 530 IRSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVL-TRTPEFFMKHDFLPTSKSLLPE 589
Cdd:TIGR01890 350 MACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLtTRTGHWFRERGFQTASVDELPE 410
|
|
| PRK07922 |
PRK07922 |
amino-acid N-acetyltransferase; |
464-581 |
1.34e-21 |
|
amino-acid N-acetyltransferase;
Pssm-ID: 236132 [Multi-domain] Cd Length: 169 Bit Score: 91.91 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 464 VKVRPARLTDIEALEGMVAYWANMGENLPRSRNELVRDIGSFAVAEH-HGEVTGCASLYVYDSGLAEIRSLGVEAGWQGQ 542
Cdd:PRK07922 6 ITVRRARTSDVPAIKRLVDPYAQGRILLEKNLVTLYEAVQEFWVAEHlDGEVVGCGALHVMWEDLAEIRTVAVDPAARGR 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 1633128600 543 GQGTAIVQHLVEKARQMAIKKVFVLTRTPEFFMKHDFLP 581
Cdd:PRK07922 86 GVGHAIVERLLDVARELGLSRVFVLTFEVEFFARHGFVE 124
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
97-438 |
4.97e-21 |
|
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: 96.16 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 97 GDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEML 176
Cdd:cd01597 87 DAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSEL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 177 ERDYSRLNDAIKRLDTCPLG--SGALA--GTAYPMDREELAHNLGFRRATRNSLdsvSDRDHVMELMSIasISMLH--LS 250
Cdd:cd01597 167 LRHRERLDELRPRVLVVQFGgaAGTLAslGDQGLAVQEALAAELGLGVPAIPWH---TARDRIAELASF--LALLTgtLG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 251 RLAEDMIFYNSGEsnFIELADTVTSG---SSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTvkalplaynkdMQEDKEG 327
Cdd:cd01597 242 KIARDVYLLMQTE--IGEVAEPFAKGrggSSTMPHKRNPVGCELIVALARRVPGLAALLLDA-----------MVQEHER 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 328 lfdALDTWN-------DCMEMAA-----LCF--DGIKVNGERTLE--AAKQGYANStELADYLVAKGIPFREAHHIVGVT 391
Cdd:cd01597 309 ---DAGAWHaewialpEIFLLASgaleqAEFllSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEA 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1633128600 392 VVAAIAKGCALEELtIAEMKEFSEVIEEDvydilTIESCLEKRSALG 438
Cdd:cd01597 385 CMRAVEEGRPLREV-LLEDPEVAAYLSDE-----ELDALLDPANYLG 425
|
|
| PRK05279 |
PRK05279 |
N-acetylglutamate synthase; Validated |
460-590 |
9.02e-21 |
|
N-acetylglutamate synthase; Validated
Pssm-ID: 235386 [Multi-domain] Cd Length: 441 Bit Score: 95.22 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 460 DTSIVKVRPARLTD-------IEALEgmvaywaNMGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYVY-DSGLAEIR 531
Cdd:PRK05279 291 MESLEQLRRATIDDvggilelIRPLE-------EQGILVRRSREQLEREIDKFTVIERDGLIIGCAALYPFpEEKMGEMA 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 532 SLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVL-TRTPEFFMKHDFLPTSKSLLPEK 590
Cdd:PRK05279 364 CLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLtTRTAHWFLERGFVPVDVDDLPEA 423
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-428 |
1.16e-20 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 95.44 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 106 GRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLND 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 186 AIKRLDTCPLGSGALaGTAYPMDRE-------ELAHNLG--FRRATrNSLDSVSDRDHVMELMSIASISMLHLSRLAEDM 256
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyiervvkHLAAITGlpLVGAE-DLVDATQNTDAFVEVSGALKVCAVNLSKIANDL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 257 IFYNSG-ESNFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDMQEDKEGLFDALDT 334
Cdd:PRK13353 296 RLLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISI 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 335 W-NDCMEMAALCFDGIKVNGERtleaAKQGYANSTELADYLVakgiPFreahhiVGVTVVAAIAKGCALEELTIAEMKEF 413
Cdd:PRK13353 376 LtNACRAFTDNCVKGIEANEER----CKEYVEKSVGIATALN----PH------IGYEAAARIAKEAIATGRSVRELALE 441
|
330
....*....|....*.
gi 1633128600 414 SEVI-EEDVYDILTIE 428
Cdd:PRK13353 442 NGLLsEEELDLILDPF 457
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
124-445 |
1.02e-19 |
|
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: 92.07 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 124 QGNQLLLA-LDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLNDAIKRLDTCPLG--SGAL 200
Cdd:COG0015 113 EALELLLPdLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGgaVGTY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 201 A--GTAYPMDREELAHNLGFRRATrnSLDSVSDRDHVMELMS----IASIsmlhLSRLAEDMIFYNSGESNFIE---LAD 271
Cdd:COG0015 193 AahGEAWPEVEERVAEKLGLKPNP--VTTQIEPRDRHAELFSalalIAGS----LEKIARDIRLLQRTEVGEVEepfAKG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 272 TVtsGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVK---------------ALPLAYnkdmqedkeGLFD-ALDTW 335
Cdd:COG0015 267 QV--GSSAMPHKRNPIDSENIEGLARLARALAAALLEALAswherdlsdssvernILPDAF---------LLLDgALERL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 336 NDCMemaalcfDGIKVNGER---TLEAAKqGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGCALEELtIAEMKE 412
Cdd:COG0015 336 LKLL-------EGLVVNPERmraNLDLTG-GLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL-LAADPE 406
|
330 340 350
....*....|....*....|....*....|...
gi 1633128600 413 FSEVIEEDvydilTIESCLEKRSALgGVSPQQV 445
Cdd:COG0015 407 IPAELSKE-----ELEALFDPANYL-GAADEIV 433
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-409 |
6.89e-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: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 106 GRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLND 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 186 AIKRLDTCPLGSGALaGTAYPMDR-------EELAHN--LGFRRATrNSLDSVSDRDHVMELMSIASISMLHLSRLAEDM 256
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPPgyielvvEKLSEItgLPLKRAE-NLIDATQNTDAFVEVSGALKRLAVKLSKIANDL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 257 IFYNSG------ESNFIEladtVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKA--------LPL-AYNkdm 321
Cdd:cd01357 291 RLLSSGpraglgEINLPA----VQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAgqlelnvfEPViAYN--- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 322 qedkegLFDALDTWNDCMEM-AALCFDGIKVNGERtleaAKQGYANSTELADYLVakgipfreahHIVGVTVVAAIAKGC 400
Cdd:cd01357 364 ------LLESIDILTNAVRTlRERCIDGITANEER----CREYVENSIGIVTALN----------PYIGYEAAAEIAKEA 423
|
....*....
gi 1633128600 401 ALEELTIAE 409
Cdd:cd01357 424 LETGRSVRE 432
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
126-384 |
4.54e-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: 77.85 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 126 NQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLNDAIKRLdtCPLGSGALA-GT- 203
Cdd:cd01596 153 ERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERL--RELNLGGTAvGTg 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 204 --AYPMDREELAHNL------GFRRATrNSLDSVSDRDHVMELMSIASISMLHLSRLAEDMIFYNSG------EsnfIEL 269
Cdd:cd01596 231 lnAPPGYAEKVAAELaeltglPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGpraglgE---INL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 270 aDTVTSGSSLMPQKKNP---DALELIrgkTGRVYGSLAAMMMTVKA--------LPL-AYNkdmqedkegLFDALDTWND 337
Cdd:cd01596 307 -PANQPGSSIMPGKVNPvipEAVNMV---AAQVIGNDTAITMAGSAgqlelnvfKPViAYN---------LLQSIRLLAN 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 338 CMEM-AALCFDGIKVNGERTLEAAKQ------------GYANSTELADYLVAKGIPFREA 384
Cdd:cd01596 374 ACRSfRDKCVEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
61-294 |
2.83e-13 |
|
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: 71.81 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 61 ALNELKLEVMEDPEQILRSDAE---DIHSWVeQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQS 137
Cdd:cd01360 41 AAEEIRKKAKFDVERVKEIEAEtkhDVIAFV-TAIAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 138 QMVNVASQHQETVLPGYTHLQRAQPVTFAH-WCLAYVEMlERDYSRLNDAIKRLDTCPLgSGALaGTAYPMD---REELA 213
Cdd:cd01360 120 VLKKKALEHKDTVMVGRTHGIHAEPTTFGLkFALWYAEF-KRHLERLKEARERILVGKI-SGAV-GTYANLGpevEERVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 214 HNLGFRRATRNSldSVSDRDHVMELMS----IAS------ISMLHLSR--LAEDMIFYNSGEsnfieladtvtSGSSLMP 281
Cdd:cd01360 197 EKLGLKPEPIST--QVIQRDRHAEYLStlalIAStlekiaTEIRHLQRteVLEVEEPFSKGQ-----------KGSSAMP 263
|
250
....*....|...
gi 1633128600 282 QKKNPDALELIRG 294
Cdd:cd01360 264 HKRNPILSENICG 276
|
|
| PLN02825 |
PLN02825 |
amino-acid N-acetyltransferase |
467-590 |
1.52e-11 |
|
amino-acid N-acetyltransferase
Pssm-ID: 215441 [Multi-domain] Cd Length: 515 Bit Score: 67.11 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 467 RPARLTDIEALEGMVAYWANMGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYVY-DSGLAEIRSLGVEAGWQGQGQG 545
Cdd:PLN02825 371 RMARVEDLAGIRQIIRPLEESGILVRRTDEELLRALDSFVVVEREGSIIACAALFPFfEEKCGEVAAIAVSPECRGQGQG 450
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1633128600 546 TAIVQHLVEKARQMAIKKVFVL-TRTPEFFMKHDFLPTSKSLLPEK 590
Cdd:PLN02825 451 DKLLDYIEKKAASLGLEKLFLLtTRTADWFVRRGFSECSIESLPEA 496
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
466-588 |
2.96e-11 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 61.64 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 466 VRPARLTDIEALEGMV-AYWANMGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLY----VYDSGLAEIRSLGVEAGWQ 540
Cdd:COG3153 1 IRPATPEDAEAIAALLrAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSpvdiDGEGPALLLGPLAVDPEYR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1633128600 541 GQGQGTAIVQHLVEKARQMAIKKVFVLT--RTPEFFMKHDFLPTSKSLLP 588
Cdd:COG3153 81 GQGIGRALMRAALEAARERGARAVVLLGdpSLLPFYERFGFRPAGELGLT 130
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
94-383 |
1.29e-10 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 63.87 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 94 GKVGDLGKKLHT--GRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLA 171
Cdd:PRK14515 130 GDYHYISPNSHVnmAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 172 YVEMLERDYSRLNDAIKRLDTCPLGSGALaGTAYPMDRE-------ELAHNLGFRRATRNSL-DSVSDRDHVMELMSIAS 243
Cdd:PRK14515 210 YSRVLERDMKRIQQSRQHLYEVNMGATAV-GTGLNADPEyieavvkHLAAISELPLVGAEDLvDATQNTDAYTEVSAALK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 244 ISMLHLSRLAEDMIFYNSGESnfIELADTV----TSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNK 319
Cdd:PRK14515 289 VCMMNMSKIANDLRLMASGPR--VGLAEIMlparQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNV 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1633128600 320 DMQEDKEGLFDALDTWNDCMEM-AALCFDGIKVNGERTLEAAKQ------------GYANSTELADYLVAKGIPFRE 383
Cdd:PRK14515 367 MEPVLVFNLLQSISIMNNGFRAfTDNCLKGIEANEDRLKEYVEKsvgiitavnphiGYEAAARVAKEAIATGQSVRE 443
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
464-566 |
4.36e-10 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 58.85 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 464 VKVRPARLTDIEALEGMVAYWANMG----ENLPRSRNELVRDIGSFA-------VAEHHGEVTGCASLYVY-----DSGL 527
Cdd:COG1247 2 MTIRPATPEDAPAIAAIYNEAIAEGtatfETEPPSEEEREAWFAAILapgrpvlVAEEDGEVVGFASLGPFrprpaYRGT 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 1633128600 528 AEIrSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFV 566
Cdd:COG1247 82 AEE-SIYVDPDARGRGIGRALLEALIERARARGYRRLVA 119
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
483-579 |
5.90e-10 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 57.14 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 483 YWANMGENLPRSRNELVRDI-----GSFAVAEHHGEVTGCASLYVYD--SGLAEIRSLGVEAGWQGQGQGTAIVQHLVEK 555
Cdd:pfam00583 8 LSEEFPEPWPDEPLDLLEDWdedasEGFFVAEEDGELVGFASLSIIDdePPVGEIEGLAVAPEYRGKGIGTALLQALLEW 87
|
90 100
....*....|....*....|....*....
gi 1633128600 556 ARQMAIKKVFVLTRTP-----EFFMKHDF 579
Cdd:pfam00583 88 ARERGCERIFLEVAADnlaaiALYEKLGF 116
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
106-384 |
6.07e-10 |
|
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: 61.75 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 106 GRSRND------QVATDLKLwcrqqGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERD 179
Cdd:cd01362 133 SQSSNDtfptamHIAAALAL-----QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 180 YSRLNDAIKRLDTCPLGsGALAGT---AYP-MDR---EELAHNLG--FRRATrNSLDSVSDRDHVMELMS----IASISM 246
Cdd:cd01362 208 IARIEAALPRLYELALG-GTAVGTglnAHPgFAEkvaAELAELTGlpFVTAP-NKFEALAAHDALVEASGalktLAVSLM 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 247 lhlsRLAEDMIFYNSG-ESNFIELA-DTVTSGSSLMPQKKNP---DALELIrgkTGRVYGSLAAmmMTVKA--------- 312
Cdd:cd01362 286 ----KIANDIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNPtqcEALTMV---AAQVMGNDAA--ITIAGssgnfelnv 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 313 -LPL-AYNkdmqedkegLFDALDTWND-CMEMAALCFDGIKVNGERTLEAAKQ------------GYANSTELADYLVAK 377
Cdd:cd01362 357 fKPViIYN---------LLQSIRLLADaCRSFADKCVAGIEPNRERIAELLERslmlvtalnphiGYDKAAKIAKKAHKE 427
|
....*..
gi 1633128600 378 GIPFREA 384
Cdd:cd01362 428 GLTLKEA 434
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
108-428 |
6.57e-10 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 61.68 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 108 SRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLNDAI 187
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 188 KRLdtCPLGSGALA-GT------AYPMD-REELAH--NLGFRRATrNSLDSVSDRDHVMELMSIASISMLHLSRLAEDMI 257
Cdd:PRK12273 222 ELL--REVNLGATAiGTglnappGYIELvVEKLAEitGLPLVPAE-DLIEATQDTGAFVEVSGALKRLAVKLSKICNDLR 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 258 FYNSG------ESNFIEladtVTSGSSLMPQKKNPDALELIRGKTGRVYG-----SLAA--------MMMTVkalpLAYN 318
Cdd:PRK12273 299 LLSSGpraglnEINLPA----VQAGSSIMPGKVNPVIPEVVNQVCFQVIGndttvTMAAeagqlelnVMEPV----IAYN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 319 kdmqedkegLFDALDTWNDCMEM-AALCFDGIKVNGERTLEAAKqgyaNSTELADYLVakgipfreahHIVGVTVVAAIA 397
Cdd:PRK12273 371 ---------LFESISILTNACRTlREKCIDGITANEERCREYVE----NSIGIVTALN----------PYIGYENAAEIA 427
|
330 340 350
....*....|....*....|....*....|....*..
gi 1633128600 398 KGCALEELTIAEMkefseVIE------EDVYDILTIE 428
Cdd:PRK12273 428 KEALETGKSVREL-----VLErgllteEELDDILSPE 459
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
91-384 |
6.72e-10 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 61.65 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 91 QLIGKVGDLGKKLH------TGRSRND------QVATDLKLwcrqqGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQ 158
Cdd:PRK00485 116 ELLGGELGSKKPVHpndhvnMSQSSNDtfptamHIAAVLAI-----VERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 159 RAQPVTFAHWCLAYVEMLERDYSRLNDAIKRLdtCPLgsgALAGTA----------YPmDR--EELAH--NLGFRRAtRN 224
Cdd:PRK00485 191 DATPLTLGQEFSGYAAQLEHGIERIEAALPHL--YEL---ALGGTAvgtglnahpgFA-ERvaEELAEltGLPFVTA-PN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 225 SLDSVSDRDHVMELM----SIAsISMLhlsRLAEDMIFYNSG------EsnfIELADTVtSGSSLMPQKKNPDALElirg 294
Cdd:PRK00485 264 KFEALAAHDALVEASgalkTLA-VSLM---KIANDIRWLASGprcglgE---ISLPENE-PGSSIMPGKVNPTQCE---- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 295 ktgrvygslaAMMM----------TVKA------------LPL-AYNkdMQEDKEGLFDALDTWNDcmemaaLCFDGIKV 351
Cdd:PRK00485 332 ----------ALTMvcaqvmgndaAVTFagsqgnfelnvfKPViAYN--FLQSIRLLADAMRSFAD------HCVVGIEP 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1633128600 352 NGERTLEAAKQ------------GYANSTELADYLVAKGIPFREA 384
Cdd:PRK00485 394 NRERIKELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKEA 438
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
505-566 |
9.07e-09 |
|
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
Pssm-ID: 173926 [Multi-domain] Cd Length: 65 Bit Score: 51.89 E-value: 9.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633128600 505 FAVAEHHGEVTGCASLYVYDS--GLAEIRSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFV 566
Cdd:cd04301 1 FLVAEDDGEIVGFASLSPDGSggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
501-579 |
2.14e-08 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 51.69 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 501 DIGSFAVAEHHGEVTGCASLYVY-DSGLAEIRSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVLTRTP--EFFMKH 577
Cdd:pfam13508 1 PGGRFFVAEDDGKIVGFAALLPLdDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRaaAFYEKL 80
|
..
gi 1633128600 578 DF 579
Cdd:pfam13508 81 GF 82
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
106-384 |
2.90e-07 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 53.16 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 106 GRSRNDQVATDLKLWCRQQGNQLLL-ALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLN 184
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIHSRLIpALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 185 DAIKRLDTCPLGSGALaGTAYPMDR---EELAH------NLGFRRAtRNSLDSVSDRDHVMELMSIASISMLHLSRLAED 255
Cdd:PLN00134 209 CTLPRLYELAQGGTAV-GTGLNTKKgfdEKIAAavaeetGLPFVTA-PNKFEALAAHDAFVELSGALNTVAVSLMKIAND 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 256 MIFYNSG-ESNFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMM----------TVKALpLAYNkdMQE 323
Cdd:PLN00134 287 IRLLGSGpRCGLGELNlPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAITVggsaghfelnVFKPL-IAYN--LLH 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1633128600 324 DKEGLFDALDTwndcmeMAALCFDGIKVNGERTLEA------------AKQGYANSTELADYLVAKGIPFREA 384
Cdd:PLN00134 364 SIRLLGDASAS------FRKNCVRGIEANRERISKLlheslmlvtalnPKIGYDKAAAVAKKAHKEGTTLKEA 430
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
91-292 |
3.97e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 52.36 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 91 QLIGKVG-DLGKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWC 169
Cdd:PRK05975 89 QLRAAVGeEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 170 LAYVEMLERDYSRLNDAikRLDTCPLGSGALAGT------AYPMDREELAHNLGFRRATRNSldsvSDRDHVMELMSIAS 243
Cdd:PRK05975 169 ASWRAPLLRHRDRLEAL--RADVFPLQFGGAAGTleklggKAAAVRARLAKRLGLEDAPQWH----SQRDFIADFAHLLS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1633128600 244 ISMLHLSRLAED--MIFYNSGEsnfIELADtvTSGSSLMPQKKNPDALELI 292
Cdd:PRK05975 243 LVTGSLGKFGQDiaLMAQAGDE---ISLSG--GGGSSAMPHKQNPVAAETL 288
|
|
| ElaA |
COG2153 |
Predicted N-acyltransferase, GNAT family [General function prediction only]; |
507-583 |
5.25e-07 |
|
Predicted N-acyltransferase, GNAT family [General function prediction only];
Pssm-ID: 441756 [Multi-domain] Cd Length: 134 Bit Score: 49.03 E-value: 5.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633128600 507 VAEHHGEVTGCASLYVYDSGLAEIRSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVLTRTP--EFFMKHDFLPTS 583
Cdd:COG2153 38 LAYDDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHavGFYEKLGFVPVG 116
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-404 |
1.51e-06 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 51.17 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 100 GKKLHTGRSRNDQVATDLKLWCRQQGNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERD 179
Cdd:PRK09053 99 ARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 180 YSRLNDAIKRLDTCPLG--SGALA--GTAYPMDREELAHNLGFrratrnSLDSVS---DRDHVMELMSIASISMLHLSRL 252
Cdd:PRK09053 179 RQRLAALRPRALVLQFGgaAGTLAslGEQALPVAQALAAELQL------ALPALPwhtQRDRIAEFASALGLLAGTLGKI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 253 AED---MIFYNSGEsnFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAAMMmtvKALPlaynkdmQEDKEGLF 329
Cdd:PRK09053 253 ARDvslLMQTEVGE--VFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATLF---AAMP-------QEHERALG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 330 DALDTWNDCMEMAAL----------CFDGIKVNGER---TLEAAKQ---GYANSTELADYLvakGIPfrEAHHIVGVTVV 393
Cdd:PRK09053 321 GWHAEWDTLPELACLaagalaqmaqIVEGLEVDAARmraNLDLTHGlilAEAVMLALADRI---GRL--DAHHLVEQASK 395
|
330
....*....|.
gi 1633128600 394 AAIAKGCALEE 404
Cdd:PRK09053 396 RAVAEGRHLRD 406
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
462-558 |
5.34e-06 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 46.20 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 462 SIVKVRPAR---LTDIEALEGMVaywanmgenlpRSRNELVRDiGSFAVAEHHGEVTGCASLYVYDSGLAEIRSLGVEAG 538
Cdd:COG0454 2 SIRKATPEDinfILLIEALDAEL-----------KAMEGSLAG-AEFIAVDDKGEPIGFAGLRRLDDKVLELKRLYVLPE 69
|
90 100
....*....|....*....|
gi 1633128600 539 WQGQGQGTAIVQHLVEKARQ 558
Cdd:COG0454 70 YRGKGIGKALLEALLEWARE 89
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
516-570 |
1.67e-05 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 43.49 E-value: 1.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1633128600 516 GCASLYV-YDSGLAEIRSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVLTRT 570
Cdd:COG0456 1 GFALLGLvDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVRE 56
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
106-384 |
7.88e-05 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 45.68 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 106 GRSRNDQVATDLKLWCRQQ-GNQLLLALDRLQSQMVNVASQHQETVLPGYTHLQRAQPVTFAHWCLAYVEMLERDYSRLN 184
Cdd:PRK12425 135 SQSSNDCFPTAMHIAAAQAvHEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 185 DAIKRLdtCPLGSGALA-GT---AYPMDREELAHNLgfrrATRNSLDSVSDRDHVMELMSIASISMLH---------LSR 251
Cdd:PRK12425 215 AALPAV--CELAQGGTAvGTglnAPHGFAEAIAAEL----AALSGLPFVTAPNKFAALAGHEPLVSLSgalktlavaLMK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 252 LAEDMIFYNSG-ESNFIELADTVTS-GSSLMPQKKNPDALELIRGKTGRVYGSLAAMMMTVKALPLAYNKDMQEDKEGLF 329
Cdd:PRK12425 289 IANDLRLLGSGpRAGLAEVRLPANEpGSSIMPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLL 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633128600 330 DALDTWND-CMEMAALCFDGIKVNGERTLEAAKQ------------GYANSTELADYLVAKGIPFREA 384
Cdd:PRK12425 369 QSIRLLADgCRNFQQHCVAGLEPDAEQMAAHLERglmlvtalnphiGYDKAAEIAKKAYAEGTTLREA 436
|
|
| RimL |
COG1670 |
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ... |
460-569 |
1.73e-03 |
|
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441276 [Multi-domain] Cd Length: 173 Bit Score: 39.60 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 460 DTSIVKVRPARLTDIEAL------EGMVAYWANMGENLPRSRNELVR--------DIGSFAVAE-HHGEVTGCASLYVYD 524
Cdd:COG1670 4 ETERLRLRPLRPEDAEALaellndPEVARYLPGPPYSLEEARAWLERlladwadgGALPFAIEDkEDGELIGVVGLYDID 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1633128600 525 --SGLAEIrSLGVEAGWQGQGQGTAIVQHLVEKA-RQMAIKKVFVLTR 569
Cdd:COG1670 84 raNRSAEI-GYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVD 130
|
|
| COG3393 |
COG3393 |
Predicted acetyltransferase, GNAT family [General function prediction only]; |
513-568 |
2.07e-03 |
|
Predicted acetyltransferase, GNAT family [General function prediction only];
Pssm-ID: 442620 [Multi-domain] Cd Length: 86 Bit Score: 37.58 E-value: 2.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1633128600 513 EVTGCASLYVYDSGLAEIRSLGVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVLT 568
Cdd:COG3393 1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYV 56
|
|
| PRK03624 |
PRK03624 |
putative acetyltransferase; Provisional |
463-570 |
3.94e-03 |
|
putative acetyltransferase; Provisional
Pssm-ID: 235142 [Multi-domain] Cd Length: 140 Bit Score: 37.99 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 463 IVKVRPARLTDIEAlegMVAYWANMGenLPRSRNELVRDI--------GSFAVAEHHGEVTGcaSLYV-YDSGLAEIRSL 533
Cdd:PRK03624 2 AMEIRVFRQADFEA---VIALWERCD--LTRPWNDPEMDIerklnhdpSLFLVAEVGGEVVG--TVMGgYDGHRGWAYYL 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1633128600 534 GVEAGWQGQGQGTAIVQHLVEKARQMAIKKVFVLTRT 570
Cdd:PRK03624 75 AVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVRE 111
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
276-429 |
6.43e-03 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 38.47 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 276 GSSLMPQKKNPDALELIRG--KTGRVYGSLAAMMMTV-------------KALPlaynkdmqeDKEGLFDA-LDTWNDCM 339
Cdd:PRK08937 58 GSSAMPHKRNPIGSERITGlaRVLRSYLVTALENVPLwherdlshssaerIALP---------DAFLALDYiLNRFVNIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633128600 340 EmaalcfdGIKVNGERTLE--AAKQGYANSTELADYLVAKGIPFREAHHIVGVTVVAAIAKGCALEELTIAEMKEFSEVI 417
Cdd:PRK08937 129 E-------NLVVFPENIERnlDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWKNQKDLRELLEADERFTKQLT 201
|
170
....*....|..
gi 1633128600 418 EEDVYDILTIES 429
Cdd:PRK08937 202 KEELDELFDPEA 213
|
|
| |
