|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
70-526 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 830.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:COG4770 83 GFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:COG4770 163 GGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:COG4770 243 PSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:COG4770 323 FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIAR 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEELRAPQ---DIVLASA 526
Cdd:COG4770 403 MRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAapeELALAAA 462
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
70-511 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 829.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:PRK08591 3 DKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:PRK08591 83 GFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:PRK08591 163 GGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:PRK08591 243 PSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:PRK08591 323 IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIAR 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKH 511
Cdd:PRK08591 403 MKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
70-515 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 809.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:TIGR00514 3 DKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:TIGR00514 83 GFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:TIGR00514 163 GGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:TIGR00514 243 PSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:TIGR00514 323 LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIAR 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEEL 515
Cdd:TIGR00514 403 MKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMG 448
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
70-526 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 663.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:PRK08654 83 GFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:PRK08654 163 GGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDErGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:PRK08654 243 PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:PRK08654 322 FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEELRAPQDIVLASA 526
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEEMKRYALEEE 458
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
71-510 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 657.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGYG 150
Cdd:PRK05586 4 KILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 151 FLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAGG 230
Cdd:PRK05586 84 FLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 231 GGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEAP 310
Cdd:PRK05586 164 GGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 311 SPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLRY 390
Cdd:PRK05586 244 SPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 391 KQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERM 470
Cdd:PRK05586 324 KQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKM 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1240952799 471 KRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPK 510
Cdd:PRK05586 404 KRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
70-518 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 625.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPS-SQSYLMVQNVLSAALTHRCTMLHPG 148
Cdd:PRK12999 6 KKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIHPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 149 YGFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATA 228
Cdd:PRK12999 86 YGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKASA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 229 GGGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEE 308
Cdd:PRK12999 166 GGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 309 APSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKL 388
Cdd:PRK12999 246 APAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 389 R------YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDS-HVYSDYVVPPSYDSLLGKLIVWAP 461
Cdd:PRK12999 326 HdleigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTAWGR 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1240952799 462 TREKAIERMKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEELRAP 518
Cdd:PRK12999 406 TFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFP 462
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
71-518 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 620.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGYG 150
Cdd:PRK06111 4 KVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 151 FLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAGG 230
Cdd:PRK06111 84 LLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 231 GGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEAP 310
Cdd:PRK06111 164 GGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 311 SPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLRY 390
Cdd:PRK06111 244 SPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 391 KQEDIVLRGHSIECRINAEDAfNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERM 470
Cdd:PRK06111 324 TQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1240952799 471 KRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEELRAP 518
Cdd:PRK06111 403 HDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVKKSTK 450
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
71-528 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 610.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSsQSYLMVQNVLSAALTHRCTMLHPGYG 150
Cdd:PRK07178 4 KILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHPGYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 151 FLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAGG 230
Cdd:PRK07178 83 FLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATSGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 231 GGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEAP 310
Cdd:PRK07178 163 GGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 311 SPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLRY 390
Cdd:PRK07178 243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 391 KQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERM 470
Cdd:PRK07178 323 KQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRG 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1240952799 471 KRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEEL-----RAPQDIVLASANA 528
Cdd:PRK07178 403 RRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTnysikRKPEELAAAIAAA 465
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
70-511 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 607.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:PRK08462 5 KRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:PRK08462 85 GFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:PRK08462 165 GGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLr 389
Cdd:PRK08462 245 PAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAfNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:PRK08462 324 PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAK 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKH 511
Cdd:PRK08462 403 MKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
71-520 |
0e+00 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 595.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSS-QSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:COG1038 6 KVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIHPGY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:COG1038 86 GFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:COG1038 166 GGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:COG1038 246 PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 ------YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDS-HVYSDYVVPPSYDSLLGKLIVWAPT 462
Cdd:COG1038 326 dpeigiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVKVTAWGRT 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 463 REKAIERMKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEE--ELRAPQD 520
Cdd:COG1038 406 FEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPElfDFPKRRD 465
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
71-526 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 572.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGYG 150
Cdd:PRK12833 7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 151 FLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAGG 230
Cdd:PRK12833 87 FLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 231 GGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYgNVVHFGERDCSIQRRNQKLLEEAP 310
Cdd:PRK12833 167 GGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 311 SPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLD-ERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:PRK12833 246 SPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:PRK12833 326 FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALAR 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEELRAPQDIVLASA 526
Cdd:PRK12833 406 AARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAALDAAASAA 462
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
71-520 |
0e+00 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 523.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSsQSYLMVQNVLSAALTHRCTMLHPGYG 150
Cdd:PRK08463 4 KILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHPGYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 151 FLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGI-ELANEIGYPVMIKATAG 229
Cdd:PRK08463 83 FLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIkIFARKIGYPVILKASGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:PRK08463 163 GGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:PRK08463 243 PCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 390 YKQEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIER 469
Cdd:PRK08463 323 LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNK 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1240952799 470 MKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEE-LRAPQD 520
Cdd:PRK08463 403 LERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQElLEKTED 454
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
70-508 |
4.71e-175 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 525.37 E-value: 4.71e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSqGLLQSTEEGIELANEIGYPVMIKATAG 229
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT-GLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 230 GGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEA 309
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 310 PSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDE-RGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKL 388
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEaRDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 389 RYKQ--EDIVLRGHSIECRINAEDAFNGFRPGPGRITSY-LPSGgpfVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREK 465
Cdd:TIGR02712 321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVqFPDD---VRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1240952799 466 AIERMKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFI 508
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
71-519 |
4.91e-169 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 508.21 E-value: 4.91e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 71 KILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSS---QSYLMVQNVLSAALTHRCTMLHP 147
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 148 GYGFLAENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKAT 227
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 228 AGGGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLE 307
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 308 EAPSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEK 387
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 388 LRYK------QEDIVLRGHSIECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDS-HVYSDYVVPPSYDSLLGKLIVWA 460
Cdd:TIGR01235 321 LPTPqlgvpnQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1240952799 461 PTREKAIERMKRALDETIIKGVPTTIDYHKLILDVQDFRDGKVDTAFIPKHEEELRAPQ 519
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVK 459
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
182-389 |
1.93e-96 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 291.13 E-value: 1.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 182 DKSTARETMKNAGVPTVPGSQGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEFVKLLQQAKSEAGAAFGN 261
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 262 DGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDCSIQRRNQKLLEEAPSPALTPELRKAMGDAAVAAAASIGYIGVGTV 341
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1240952799 342 EFLLDER-GYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
150-387 |
5.86e-68 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 219.74 E-value: 5.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 150 GFLAENANFVD----VCRSHGINfiGPNPDSIRVMGDKSTARETMKNAGVPtVPGSQgLLQSTEEGIELANEIGYPVMIK 225
Cdd:COG0439 20 AVLSESEFAVEtaaeLAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGFA-LVDSPEEALAFAEEIGYPVVVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 226 ATAGGGGRGMRLANEPKEFVKLLQQAKSEAGAAFGNDGVYLEKYIQNpRHIEFQVLADKyGNVVHfgerdCSIQRRNQK- 304
Cdd:COG0439 96 PADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 305 -----LLEEAPSPaLTPELRKAMGDAAVAAAASIGYI-GVGTVEFLLDERGYFYFMEMNTRIQVEH--PVTEMIFSVDLI 376
Cdd:COG0439 169 pyfveLGHEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLV 247
|
250
....*....|.
gi 1240952799 377 EEQIRVAMGEK 387
Cdd:COG0439 248 REQIRLALGEP 258
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
403-510 |
4.84e-56 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 183.08 E-value: 4.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 403 ECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERMKRALDETIIKGV 482
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 1240952799 483 PTTIDYHKLILDVQDFRDGKVDTAFIPK 510
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
403-508 |
7.25e-56 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 182.23 E-value: 7.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 403 ECRINAEDAFNGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERMKRALDETIIKGV 482
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*.
gi 1240952799 483 PTTIDYHKLILDVQDFRDGKVDTAFI 508
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
70-176 |
5.28e-53 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 174.98 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 70 EKILVANRGEIAVRIIRTAHEMGIPCVAVYSTIDKDALHVKLADASICIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY 149
Cdd:pfam00289 2 KKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGY 81
|
90 100
....*....|....*....|....*..
gi 1240952799 150 GFLAENANFVDVCRSHGINFIGPNPDS 176
Cdd:pfam00289 82 GFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
166-389 |
1.79e-16 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 82.74 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 166 GINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGsqGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEFV 245
Cdd:TIGR01369 653 GVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELR 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 246 KLLQqaksEAGAAFGNDGVYLEKYIQNPRHIEFQVLADKyGNV-------------VHFGERDCSIqrrnqklleeaPSP 312
Cdd:TIGR01369 731 RYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDG-EEVlipgimehieeagVHSGDSTCVL-----------PPQ 794
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1240952799 313 ALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDErGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEKLR 389
Cdd:TIGR01369 795 TLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
166-359 |
1.49e-15 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 79.15 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 166 GINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGsqGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEFV 245
Cdd:COG0458 98 GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 246 KLLQQAKSeagaAFGNDGVYLEKYIQNPRHIEFQVLADKYGNV-------------VHFGERDCSiqrrnqklleeAPSP 312
Cdd:COG0458 176 EYLERALK----VSPDHPVLIDESLLGAKEIEVDVVRDGEDNViivgimehiepagVHSGDSICV-----------APPQ 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1240952799 313 ALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYfYFMEMNTR 359
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRV-YVIEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
165-360 |
2.20e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 76.19 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 165 HGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGsqGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEF 244
Cdd:TIGR01369 110 YGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 245 VKLLQQAKSEAGAafgnDGVYLEKYIQNPRHIEFQVLADKYGNV-------------VHFGErdcSIQrrnqklleEAPS 311
Cdd:TIGR01369 188 KEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGD---SIV--------VAPS 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1240952799 312 PALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGY-FYFMEMNTRI 360
Cdd:TIGR01369 253 QTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGrYYVIEVNPRV 302
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
84-360 |
8.98e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 73.04 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 84 IIRTAHEMGIPCVAVYSTIDKDALHVKLADASIcIGEAPSSQSYLMVQNVLSAALTHRCTMLHPGY----GFLAENANFV 159
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVV-VVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 160 dvcrSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPtVPGSQgLLQSTEEGIELANEIGYPVMIKATAG--------GG 231
Cdd:COG3919 99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV-VLDSADDLDALAEDLGFPVVVKPADSvgydelsfPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 232 GRGMRLANEPKEFVKLLQQAkseagAAFGNDGVyLEKYIQNPRHIE--FQVLADKYGNVVHFgerdCSIQRRNQK----- 304
Cdd:COG3919 173 KKKVFYVDDREELLALLRRI-----AAAGYELI-VQEYIPGDDGEMrgLTAYVDRDGEVVAT----FTGRKLRHYppagg 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 305 ---LLEEAPSPALTPELRKAMGdaavaaaaSIGYIGVGTVEFLLDER-GYFYFMEMNTRI 360
Cdd:COG3919 243 nsaARESVDDPELEEAARRLLE--------ALGYHGFANVEFKRDPRdGEYKLIEINPRF 294
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
164-388 |
1.02e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 74.24 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 164 SHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQGllQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKE 243
Cdd:PRK12815 652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 244 FVKLLQQAKS--------------EAGAAFGNDG--VYLEKYIQnprHIEfqvladKYGnvVHFGERDCSIqrrnqklle 307
Cdd:PRK12815 730 LEAYLAENASqlypilidqfidgkEYEVDAISDGedVTIPGIIE---HIE------QAG--VHSGDSIAVL--------- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 308 eaPSPALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDErGYFYFMEMNTRIQVEHPVTEMIFSVDLIEEQIRVAMGEK 387
Cdd:PRK12815 790 --PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKS 866
|
.
gi 1240952799 388 L 388
Cdd:PRK12815 867 L 867
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
165-289 |
2.92e-11 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 66.27 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 165 HGINFIGPNPDSIRVMGDKSTARETMKNAGVPtVPGSqGLLQSTEEGIELANEIGYPVMIKA--TAGGGGRGMrlANEPK 242
Cdd:PRK05294 111 YGVELIGAKLEAIDKAEDRELFKEAMKKIGLP-VPRS-GIAHSMEEALEVAEEIGYPVIIRPsfTLGGTGGGI--AYNEE 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1240952799 243 EFVKLLQQ--AKSEAGAafgndgVYLEKYIQNPRHIEFQVLADKYGNVV 289
Cdd:PRK05294 187 ELEEIVERglDLSPVTE------VLIEESLLGWKEYEYEVMRDKNDNCI 229
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
171-359 |
2.28e-10 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 63.64 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 171 GPNPDSIRVMGDKSTARETMKNAGVPTVPGsqGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEFVKLLQQ 250
Cdd:PLN02735 691 GTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLET 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 251 A-KSEAGAAfgndgVYLEKYIQNPRHIEFQVLADKYGNVV-------------HFGERDCSIqrrnqklleeaPSPALTP 316
Cdd:PLN02735 769 AvEVDPERP-----VLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPS 832
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1240952799 317 ELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNTR 359
Cdd:PLN02735 833 SCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
83-357 |
5.15e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 60.72 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 83 RIIRTAHEMGIPCVAvystIDKDALHVKLADASICIGEAPSSQsylmvqnvLSAALtHRCTMLHPGYGFLaenanfvDVC 162
Cdd:COG0189 18 ALIEAAQRRGHEVEV----IDPDDLTLDLGRAPELYRGEDLSE--------FDAVL-PRIDPPFYGLALL-------RQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 163 RSHGINFIgPNPDSIRVMGDKSTARETMKNAGVPTVPgsQGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPK 242
Cdd:COG0189 78 EAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP--TLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 243 EFVKLLqqaksEAGAAFGNDGVYLEKYIQNPRHIEFQVLA-DkyGNVVHFGER-----DCsiqRRNQKLLEEAPSPALTP 316
Cdd:COG0189 155 ALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLVvG--GEPVAAIRRipaegEF---RTNLARGGRAEPVELTD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1240952799 317 ELR-------KAMGdaavaaaasigyIGVGTVEFLLDERGYfYFMEMN 357
Cdd:COG0189 225 EERelalraaPALG------------LDFAGVDLIEDDDGP-LVLEVN 259
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
172-356 |
1.52e-09 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 59.70 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 172 PNPDSIRVMGDKSTARETMKNAGVPTVPGSqgLLQSTEEGIELANEIGYPVMIKATAGG-GGRGMRLANEPKEFVKLLqq 250
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLEAAW-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 251 akseagAAFGNDGVYLEKYIqnPRHIEFQVLA--DKYGNVVHF--GErdcSIQRRNQklLEEAPSPA-LTPELRKAMGDA 325
Cdd:COG0026 155 ------AALGGGPCILEEFV--PFERELSVIVarSPDGEVATYpvVE---NVHRNGI--LDESIAPArISEALAAEAEEI 221
|
170 180 190
....*....|....*....|....*....|.
gi 1240952799 326 AVAAAASIGYIGVGTVEFLLDERGYFYFMEM 356
Cdd:COG0026 222 AKRIAEALDYVGVLAVEFFVTKDGELLVNEI 252
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
165-360 |
2.29e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 60.37 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 165 HGINFIGPNPDSIRVMGDKSTARETMKNAGVPTvpGSQGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEF 244
Cdd:PRK12815 111 YGVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 245 VKLLQQAKSEagAAFGNdgVYLEKYIQNPRHIEFQVLADKYGNV-------------VHFGErdcSIQrrnqklleEAPS 311
Cdd:PRK12815 189 EQLFKQGLQA--SPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCitvcnmenidpvgIHTGD---SIV--------VAPS 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1240952799 312 PALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERG-YFYFMEMNTRI 360
Cdd:PRK12815 254 QTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSkQYYLIEVNPRV 303
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
182-358 |
2.12e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 55.89 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 182 DKSTARETMKNAGVPTVPGSqgLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEfvklLQQAKSEAgAAFGN 261
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDE----LQAALELA-FKYDD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 262 DgVYLEKYIQNPrhiEFQ--VLAD-------------------KY--GNVVHFgerdCsiqrrnqklleeaPSPaLTPEL 318
Cdd:PRK01372 171 E-VLVEKYIKGR---ELTvaVLGGkalpvieivpagefydyeaKYlaGGTQYI----C-------------PAG-LPAEI 228
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1240952799 319 RKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFMEMNT 358
Cdd:PRK01372 229 EAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
164-383 |
1.84e-07 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 52.73 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 164 SHGINFIGPnPDSIRVMGDKSTARETMKNAGVPTvPGSqGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKE 243
Cdd:TIGR00768 71 SLGVPVINS-SDAILNAGDKFLSHQLLAKAGIPL-PRT-GLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 244 FVKLLQQAKSEAGAAfgnDGVYLEKYIQNP--RHIEFQVLADKygnVVHFGERDCSIQRRNQKLLEEAPSPA-LTPELR- 319
Cdd:TIGR00768 148 AESLLEHFEQLNGPQ---NLFLVQEYIKKPggRDIRVFVVGDE---VVAAIYRITSGHWRSNLARGGKAEPCsLTEEIEe 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 320 ------KAMGDaavaaaasigyiGVGTVEFLLDERGYFyFMEMNTRIQVEHpvTEMIFSVDLIEEQIRVA 383
Cdd:TIGR00768 222 laikaaKALGL------------DVAGVDLLESEDGLL-VNEVNANPEFKN--SVKTTGVNIAGKLLDYI 276
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
144-358 |
2.64e-07 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 52.42 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 144 MLHPGYGflaENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSqgLLQSTEEGI--ELANEIGYP 221
Cdd:COG1181 60 ALHGRGG---EDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYV--VLRRGELADleAIEEELGLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 222 VMIKATAGGGGRGMRLANEPKEFVKLLQqakseagAAFGNDGVYL-EKYIQNPrhiEFQV-------------------- 280
Cdd:COG1181 135 LFVKPAREGSSVGVSKVKNAEELAAALE-------EAFKYDDKVLvEEFIDGR---EVTVgvlgnggpralppieivpen 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 281 ----LADKY--GNVVHFgerdcsiqrrnqklleeAPSPaLTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGYFYFM 354
Cdd:COG1181 205 gfydYEAKYtdGGTEYI-----------------CPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLL 266
|
....
gi 1240952799 355 EMNT 358
Cdd:COG1181 267 EVNT 270
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
139-404 |
2.95e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.58 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 139 THRCTMLHPGY----GFLAENAN-FvdvcRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPgsQGLLQSTEEGIE 213
Cdd:PRK12767 67 KEKIDLLIPLIdpelPLLAQNRDrF----EEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPK--SYLPESLEDFKA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 214 --LANEIGYPVMIKATAGGGGRGMRLANEPKEfvklLQQAKSEagaafgNDGVYLEKYIQnprHIEF--QVLADKYGNVV 289
Cdd:PRK12767 141 alAKGELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEY------VPNLIIQEFIE---GQEYtvDVLCDLNGEVI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 290 HF----------GERDCSIQRRNQKLLEeapspaLTPELRKAMGdaavaaaaSIGYIgvgTVEFLLDERGYfYFMEMNTR 359
Cdd:PRK12767 208 SIvprkrievraGETSKGVTVKDPELFK------LAERLAEALG--------ARGPL---NIQCFVTDGEP-YLFEINPR 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1240952799 360 IQVEHPVTEMiFSVDLIEEQIRVAMGEK-----LRYkQEDIVLRGHSIEC 404
Cdd:PRK12767 270 FGGGYPLSYM-AGANEPDWIIRNLLGGEnepiiGEY-KEGLYMRRYDEVV 317
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
191-359 |
3.99e-07 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 49.94 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 191 KNAGVPTVPGSqgLLQSTEEGIELANEIGYPVMIKATAGG-GGRGMRLANEPKEfvklLQQAKSEAgaafGNDGVYLEKY 269
Cdd:pfam02222 1 QKLGLPTPRFM--AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEAD----LPQAWEEL----GDGPVIVEEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 270 IQNPRHIEFQVLADKYGnVVHFGERDCSIQRRNQKLLEEAPSPALTPELRKAMgDAAVAAAASIGYIGVGTVEFLLDERG 349
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQ-DIAKRLVDELGGVGVFGVELFVTEDG 148
|
170
....*....|
gi 1240952799 350 YFYFMEMNTR 359
Cdd:pfam02222 149 DLLINELAPR 158
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
172-356 |
1.18e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 50.92 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 172 PNPDSIRVMGDKSTARETMKNAGVPTVPGSqgLLQSTEEGIELANEIGYPVMIKATAGG-GGRGMRLANEPKEFvkllqq 250
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDL------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 251 akSEAGAAFGNDGVYLEKYIQNPRhiEFQVLA--DKYGNVVHF--GErdcSIQRRNQKLLEEAPsPALTPELRKAMGDAA 326
Cdd:PRK06019 162 --EAAWALLGSVPCILEEFVPFER--EVSVIVarGRDGEVVFYplVE---NVHRNGILRTSIAP-ARISAELQAQAEEIA 233
|
170 180 190
....*....|....*....|....*....|
gi 1240952799 327 VAAAASIGYIGVGTVEFLLDERGYFYFMEM 356
Cdd:PRK06019 234 SRIAEELDYVGVLAVEFFVTGDGELLVNEI 263
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
152-360 |
1.57e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 50.93 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 152 LAENAnfvdVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPgsQGLLQSTEEGIELANEIG-YPVMIKATAGG 230
Cdd:PLN02735 118 LAESG----ILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLDECFEIAEDIGeFPLIIRPAFTL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 231 GGRGMRLANEPKEFvkllqQAKSEAG-AAFGNDGVYLEKYIQNPRHIEFQVLADKYGNVVHFgerdCSIQR------RNQ 303
Cdd:PLN02735 192 GGTGGGIAYNKEEF-----ETICKAGlAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENidpmgvHTG 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1240952799 304 KLLEEAPSPALTPELRKAMGDAAVAAAASIGY-IGVGTVEFLLD-ERGYFYFMEMNTRI 360
Cdd:PLN02735 263 DSITVAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVNpVDGEVMIIEMNPRV 321
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
165-251 |
7.86e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.94 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 165 HGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGsqGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEF 244
Cdd:PRK05294 652 AGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEEL 729
|
....*..
gi 1240952799 245 VKLLQQA 251
Cdd:PRK05294 730 ERYMREA 736
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
190-358 |
3.91e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.61 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 190 MKNAGVPTVPgSQGLLQST------EEGIELANEIGYPVMIKATAGGGGRGMRLanepkefVKLLQQAKSEAGAAFGNDG 263
Cdd:pfam07478 2 LKAAGLPVVP-FVTFTRADwklnpkEWCAQVEEALGYPVFVKPARLGSSVGVSK-------VESREELQAAIEEAFQYDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 264 -VYLEKYIqNPRHIEFQVLADKYGNVVHFGER--DCSIQRRNQKLLEEAPS---PA-LTPELRKAMGDAAVAAAASIGYI 336
Cdd:pfam07478 74 kVLVEEGI-EGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSAQivvPAdLEEEQEEQIQELALKAYKALGCR 152
|
170 180
....*....|....*....|..
gi 1240952799 337 GVGTVEFLLDERGYFYFMEMNT 358
Cdd:pfam07478 153 GLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
182-271 |
4.45e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 46.30 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 182 DKSTARETMKNAGVPtVPgSQGLLQSTEEGIELANEIGYPVMIKATAGGGGRGMrlanepkeFVKLLQQAksEAGAAFGN 261
Cdd:PRK14016 214 DKELTKRLLAAAGVP-VP-EGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV--------TVNITTRE--EIEAAYAV 281
|
90
....*....|....*
gi 1240952799 262 -----DGVYLEKYIQ 271
Cdd:PRK14016 282 askesSDVIVERYIP 296
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
145-358 |
1.71e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 43.51 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 145 LHPGYGFLA------ENANFVDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTvPGSQGLlqsTEEGIElANEI 218
Cdd:PRK14569 55 LKPDKCFVAlhgedgENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPT-PMAKFL---TDKLVA-EDEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 219 GYPVMIKATAGGGGRGMRLANEPKEFVKLLQQAKS-------------EAGAAFGNDGVYLEKYIQnPRHiEFQVLADKY 285
Cdd:PRK14569 130 SFPVAVKPSSGGSSIATFKVKSIQELKHAYEEASKygevmieqwvtgkEITVAIVNDEVYSSVWIE-PQN-EFYDYESKY 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1240952799 286 G--NVVHFGERDCSiqrrnQKLLEeapspalTPELRKAMGDAavaaaasIGYIGVGTVEFLLDERGYFYFMEMNT 358
Cdd:PRK14569 208 SgkSIYHSPSGLCE-----QKELE-------VRQLAKKAYDL-------LGCSGHARVDFIYDDRGNFYIMEINS 263
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
166-345 |
2.11e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 43.90 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 166 GINfIGPNPDSIRVMGDKSTARETMKNAGVPTVPGSQglLQSTEEGIELANEIGYPVMIKATAGG-GGRGMRLANEPKEF 244
Cdd:PLN02948 106 GVD-VQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFME--IDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEEDL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 245 vkllqqakSEAGAAFG--NDGVYLEKYIQNPRHIEFQVLADKYGNVVHFGERDcSIQRRNQKLLEEAPSPaLTPELRKAM 322
Cdd:PLN02948 183 --------SSAVAALGgfERGLYAEKWAPFVKELAVMVARSRDGSTRCYPVVE-TIHKDNICHVVEAPAN-VPWKVAKLA 252
|
170 180
....*....|....*....|....
gi 1240952799 323 GDAAVAAAASIGYIGVGTVE-FLL 345
Cdd:PLN02948 253 TDVAEKAVGSLEGAGVFGVElFLL 276
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
171-386 |
4.98e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 42.91 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 171 GPNPDSIRVMGDKSTARETMKNAGVPtVPGSQgLLQSTEEGIELANEIGYPVMIKATAGGGGRGMRLANEPKEFVKLLQQ 250
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGID-VPRTH-ALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 251 AKSEAGAAFgndgvYLEKYIQNPrhiEFQV--LADKYGNVV------HFGERDCSIQrrnqkLLEEAPSPALTPElRKAM 322
Cdd:PRK02186 174 LRRAGTRAA-----LVQAYVEGD---EYSVetLTVARGHQVlgitrkHLGPPPHFVE-----IGHDFPAPLSAPQ-RERI 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 323 GDAAVAAAASIGY-IGVGTVEFLLDERGyFYFMEMNTR-----IQVehpVTEMIFSVDLIEEQIRVAMGE 386
Cdd:PRK02186 240 VRTVLRALDAVGYaFGPAHTELRVRGDT-VVIIEINPRlaggmIPV---LLEEAFGVDLLDHVIDLHLGV 305
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
220-386 |
8.98e-04 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 41.83 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 220 YPVMIKATAGGGGRGMRLANEPkefvkllqqakseagaAFGNDGVYLEKYIQNpRHIEFQVLADkygnvvhfgERDCSIQ 299
Cdd:COG2232 139 GPWLVKPIGGAGGWHIRPADSE----------------APPAPGRYFQRYVEG-TPASVLFLAD---------GSDARVL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240952799 300 RRNQKLLEEAPSP-----------ALTPELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGyFYFMEMNTRIQVEHPVTE 368
Cdd:COG2232 193 GFNRQLIGPAGERpfryggnigplALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLDLYE 271
|
170
....*....|....*...
gi 1240952799 369 MIFSVDLIEEQIRVAMGE 386
Cdd:COG2232 272 DATGGNLFDAHLRACRGE 289
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
159-231 |
1.81e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 40.77 E-value: 1.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1240952799 159 VDVCRSHGINFIGPNPDSIRVMGDKSTARETMKNAGVPTVPGsqgllQST---EEGIELANEIGYPVMIKA---TAGGG 231
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAY-----RVFtdlEEALAYLEEQGAPIVVKAdglAAGKG 152
|
|
| |
