|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
2-467 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 823.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 2 KFSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHP 81
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 82 GYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKAS 161
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 162 AGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVE 241
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 242 EAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQ 321
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 322 LPLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAI 401
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446595329 402 RLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHFKNDPslhyQVLSLETLAIAAA 467
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL----AAAAPEELALAAA 462
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 666.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHPG 82
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASA 162
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 163 GGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEE 242
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQL 322
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 323 PLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIR 402
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446595329 403 LLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHFKNDPS 451
Cdd:PRK08591 402 RMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 639.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHPG 82
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASA 162
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 163 GGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEE 242
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQL 322
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 323 PLKQQELTLNGHAIEVRLYAEDPRQdFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIR 402
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAIS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446595329 403 LLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHFK 447
Cdd:PRK06111 401 RLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLV 445
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-484 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 628.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHPG 82
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASA 162
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 163 GGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEE 242
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDaSGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQL 322
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 323 PLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIR 402
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 403 LLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHFKNDPSLHYQVLSLETL--AIAAALFSQSKGTAVWQT 480
Cdd:PRK08654 401 RMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEEMKRYALEEEERekTLSEKFFPGNKKVAAIAA 480
|
....
gi 446595329 481 GLGV 484
Cdd:PRK08654 481 AVNA 484
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-445 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 609.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 1 MKFSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASK-VSESYLSIAKIIEACKKTGADAV 79
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKhPVRAYLDIDEIIRVAKQAGVDAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 80 HPGYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVK 159
Cdd:PRK12999 83 HPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 160 ASAGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKV 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 240 VEEAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANG 319
Cdd:PRK12999 243 VEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 320 EQL------PLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGM-LATDEVSPFYDPMVAKVIA 392
Cdd:PRK12999 323 ATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNaFAGAEITPYYDSLLVKLTA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446595329 393 YGKTREDAIRLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQH 445
Cdd:PRK12999 403 WGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDET 455
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-445 |
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: 600.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 1 MKFSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASK--VsESYLSIAKIIEACKKTGADA 78
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKgpV-DAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 79 VHPGYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMV 158
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 159 KASAGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQK 238
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 239 VVEEAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVAN 318
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 319 GEQL-------PlKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATD-EVSPFYDPMVAKV 390
Cdd:COG1038 321 GYSLddpeigiP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGaVITPYYDSLLVKV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446595329 391 IAYGKTREDAIRLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQH 445
Cdd:COG1038 400 TAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-448 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 572.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHPG 82
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASA 162
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 163 GGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEE 242
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQL 322
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 323 PLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIR 402
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQ 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446595329 403 LLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHFKN 448
Cdd:PRK05586 402 KMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLVD 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
2-445 |
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: 569.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 2 KFSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHP 81
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 82 GYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKAS 161
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 162 AGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVE 241
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 242 EAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQ 321
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 322 LPLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAI 401
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446595329 402 RLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQH 445
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-468 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 529.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSeSYLSIAKIIEACKKTGADAVHPG 82
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASA 162
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 163 GGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEE 242
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQL 322
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 323 PLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIR 402
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 403 LLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHfkndPSL-HYQVLSLE---TLAIAAAL 468
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH----PELtNYSIKRKPeelAAAIAAAI 466
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-444 |
6.81e-180 |
|
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: 542.70 E-value: 6.81e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHPG 82
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGyEGDRQDLEYLATQAEQIGFPIMVKASA 162
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 163 GGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEE 242
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDAS-GAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQ 321
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEArDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 322 LPLKQ--QELTLNGHAIEVRLYAEDPRQDFLPQTGKILRwkpATLPN-VRIDHGMLATDEVSPFYDPMVAKVIAYGKTRE 398
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTD---VQFPDdVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446595329 399 DAIRLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQ 444
Cdd:TIGR02712 397 DAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-446 |
2.70e-173 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 500.81 E-value: 2.70e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 1 MKFSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVH 80
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 81 PGYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKA 160
Cdd:PRK08462 82 PGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 161 SAGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVV 240
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 241 EEAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGE 320
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 321 QLPlKQQELTLNGHAIEVRLYAEDPRQdFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDA 400
Cdd:PRK08462 322 ELP-SQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446595329 401 IRLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHF 446
Cdd:PRK08462 400 IAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEHF 445
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-444 |
4.02e-171 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 496.20 E-value: 4.02e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 1 MKFSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVH 80
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 81 PGYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKA 160
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 161 SAGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHgNYVYLFERDCSIQRRHQKVV 240
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 241 EEAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLD-ASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANG 319
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 320 EQLPLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKI--LRWkpATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTR 397
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIdaLVW--PQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446595329 398 EDAIRLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQ 444
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEA 446
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
5-458 |
7.73e-161 |
|
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: 491.65 E-value: 7.73e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 5 KVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGAS---KVSESYLSIAKIIEACKKTGADAVHP 81
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdlGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 82 GYGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKAS 161
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 162 AGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVE 241
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 242 EAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQ 321
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 322 LPLK------QQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHG-MLATDEVSPFYDPMVAKVIAYG 394
Cdd:TIGR01235 321 LPTPqlgvpnQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGnSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446595329 395 KTREDAIRLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHfkndPSLHYQVLS 458
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT----PELFQFVKS 460
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
3-447 |
4.87e-152 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 447.72 E-value: 4.87e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVsESYLSIAKIIEACKKTGADAVHPG 82
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEG-DRQDLEYLATQAEQIGFPIMVKAS 161
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 162 AGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVE 241
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 242 EAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQ 321
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 322 LPLKQQELTLNGHAIEVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAI 401
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446595329 402 RLLARAVDDSVLLGVNSNKQFLVNLLRHPVVVAGDTNTAFIQQHFK 447
Cdd:PRK08463 401 NKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
117-323 |
1.23e-83 |
|
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: 261.47 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 117 KRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQASELFEALQTARSEAENAFGSG 196
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 197 ELILEKAVIAPRHVEIQVFGDTHGNYVYLFERDCSIQRRHQKVVEEAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVE 276
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446595329 277 FLLDA-SGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQLP 323
Cdd:pfam02786 162 FALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
3-110 |
2.18e-62 |
|
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: 201.95 E-value: 2.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 3 FSKVLVANRGEIAVRVMQTAKAMGYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLSIAKIIEACKKTGADAVHPG 82
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 446595329 83 YGFLSENTDFAQACIDNQITFIGPTASA 110
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
64-321 |
3.04e-56 |
|
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: 191.62 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 64 IAKIIEAC----KKTGADAVhpgygfLSENTD----FAQACidNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGY 135
Cdd:COG0439 2 IDAIIAAAaelaRETGIDAV------LSESEFavetAAELA--EELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 136 EGDrqDLEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQASELFEALQTARSEAENAFGSGELILEKaVIAPRHVEIQVF 215
Cdd:COG0439 74 LVD--SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEE-FLEGREYSVEGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 216 GDtHGNYVYlferdCSIQRRHQK---VVE---EAPCPvMTPELRQQMGEAAVAAAKACAYV-GAGTVEFLLDASGAFYFL 288
Cdd:COG0439 151 VR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLI 223
|
250 260 270
....*....|....*....|....*....|....*
gi 446595329 289 EMNTRLQVEH--PVTELITGLDLVEWQLRVANGEQ 321
Cdd:COG0439 224 EINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
337-442 |
2.14e-46 |
|
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: 159.12 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 337 EVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIRLLARAVDDSVLLGV 416
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*.
gi 446595329 417 NSNKQFLVNLLRHPVVVAGDTNTAFI 442
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
337-444 |
5.11e-43 |
|
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: 149.95 E-value: 5.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 337 EVRLYAEDPRQDFLPQTGKILRWKPATLPNVRIDHGMLATDEVSPFYDPMVAKVIAYGKTREDAIRLLARAVDDSVLLGV 416
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 446595329 417 NSNKQFLVNLLRHPVVVAGDTNTAFIQQ 444
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
579-644 |
1.13e-21 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 88.63 E-value: 1.13e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446595329 579 IRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
566-645 |
2.73e-20 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 87.26 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 566 AAPEATDVAGDGKIRAPMDGAV-------VNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKR 638
Cdd:COG0511 50 AAAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYG 129
|
....*..
gi 446595329 639 QMLFSIQ 645
Cdd:COG0511 130 QPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
577-645 |
6.06e-18 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 87.59 E-value: 6.06e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446595329 577 GKIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQ 645
Cdd:PRK09282 523 GAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
555-644 |
2.74e-17 |
|
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: 86.29 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 555 NGN---VLIRNMTYAAPEAT----DVAGDGKIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEI 627
Cdd:COG1038 1048 NGQpreVRVRDRSVKVTVASrekaDPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEV 1127
|
90
....*....|....*..
gi 446595329 628 LGQQGQQVKKRQMLFSI 644
Cdd:COG1038 1128 LVKEGDQVEAGDLLIEL 1144
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
574-644 |
1.58e-16 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 77.21 E-value: 1.58e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446595329 574 AGDGKIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:PRK05641 82 AGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
534-641 |
4.66e-15 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 79.03 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 534 DGVlRRVQYVLdddqlyldrdNGN---VLIRNMTYAAPEAT----DVAGDGKIRAPMDGAVVNILVNEGDQVVKGQTLLI 606
Cdd:PRK12999 1038 DGM-RTVYFEL----------NGQpreVQVRDRSVKSTVAArekaDPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAV 1106
|
90 100 110
....*....|....*....|....*....|....*
gi 446595329 607 LEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQML 641
Cdd:PRK12999 1107 IEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLL 1141
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
566-644 |
1.08e-13 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 68.30 E-value: 1.08e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446595329 566 AAPEATDVAGDGKIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:PRK06549 51 QAPQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-292 |
1.75e-12 |
|
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: 68.59 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 105 GPTASAIeLMgSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQASELFEALQT 184
Cdd:COG1181 86 GVLASAL-AM-DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 185 ARSEaenafgSGELILEKAvIAPRHVEIQVFGD-------------THGNYVYlferdcsiqrrHQK-----VVEEAPCP 246
Cdd:COG1181 164 AFKY------DDKVLVEEF-IDGREVTVGVLGNggpralppieivpENGFYDY-----------EAKytdggTEYICPAR 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446595329 247 VmTPELRQQMGEaavaaakacaYV----------GAGTVEFLLDASGAFYFLEMNT 292
Cdd:COG1181 226 L-PEELEERIQE----------LAlkafralgcrGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
566-644 |
8.14e-12 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 68.03 E-value: 8.14e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446595329 566 AAPEATDVAGDGKIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:PRK14040 514 AAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
579-644 |
1.18e-11 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 60.69 E-value: 1.18e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446595329 579 IRAPMDG-----AVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:pfam00364 3 IKSPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
578-645 |
6.22e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 58.26 E-value: 6.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446595329 578 KIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQ 645
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
575-646 |
5.70e-10 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 62.43 E-value: 5.70e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446595329 575 GDGKIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQI 646
Cdd:PRK14042 524 GPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEV 595
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
584-644 |
3.00e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 53.56 E-value: 3.00e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:cd06849 14 EGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
20-294 |
1.58e-08 |
|
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: 58.09 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 20 QTAKAM---GYQTVAVYSdadrNARHVQEADE---AVYIGASKVSesylSIAKIIEackKTGADAVHPGYGFLS------ 87
Cdd:TIGR01369 31 QACKALkeeGYRVILVNS----NPATIMTDPEmadKVYIEPLTPE----AVEKIIE---KERPDAILPTFGGQTalnlav 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 88 --ENTDFAQACidnQITFIGPTASAIELMGSKRLSKIAMIEAGVPcVPGYEGDRQDLEYLATqAEQIGFPIMVKASAGGG 165
Cdd:TIGR01369 100 elEESGVLEKY---GVEVLGTPVEAIKKAEDRELFREAMKEIGEP-VPESEIAHSVEEALAA-AKEIGYPVIVRPAFTLG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 166 GRGMRLVQQASELFEAlqtarseAENAF---GSGELILEKAVIAPRHVEIQVFGDTHGNYVYLferdCSIQR-----RHQ 237
Cdd:TIGR01369 175 GTGGGIAYNREELKEI-------AERALsasPINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHT 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446595329 238 K---VVeeAPCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDA-SGAFYFLEMNTRL 294
Cdd:TIGR01369 244 GdsiVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPdSGRYYVIEVNPRV 302
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
584-644 |
2.93e-08 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 50.84 E-value: 2.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:COG0508 16 EGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
101-322 |
1.26e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 54.98 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 101 ITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDrqDLEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQASELFE 180
Cdd:PRK12815 655 LTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTAT--DEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 181 ALqtarseaENAFGSGELILEKAVIAPRHVEIQVFGDthGNYVYL---FErdcsiqrrHqkvVEEA-----------PCP 246
Cdd:PRK12815 733 YL-------AENASQLYPILIDQFIDGKEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQ 792
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446595329 247 VMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLdASGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANGEQL 322
Cdd:PRK12815 793 SLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
592-645 |
1.78e-07 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 52.92 E-value: 1.78e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446595329 592 VNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQ 645
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVIE 273
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-292 |
3.38e-07 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 52.42 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 105 GPTASAIELmgSKRLSKIAMIEAGVPCVPGYEGDRQdlEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQASELFEALqt 184
Cdd:PRK01372 89 GVLASALAM--DKLRTKLVWQAAGLPTPPWIVLTRE--EDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 185 arseaENAFGSGELILEKAVIAPRHVEIQVFGDT----------HGNYVYlferdcsiqrrHQKVVEEA-----PCPvMT 249
Cdd:PRK01372 163 -----ELAFKYDDEVLVEKYIKGRELTVAVLGGKalpvieivpaGEFYDY-----------EAKYLAGGtqyicPAG-LP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446595329 250 PELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEMNT 292
Cdd:PRK01372 226 AEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
127-292 |
7.67e-07 |
|
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: 50.01 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 127 AGVPCVP-------GYEGDRQdlEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQASELFEALqtarseaENAFGSGELI 199
Cdd:pfam07478 5 AGLPVVPfvtftraDWKLNPK--EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI-------EEAFQYDEKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 200 LEKAVIAPRHVEIQVFGDTHGNYVYLFER--DCSIQRRHQKVVEEAP---CPV-MTPELRQQMGEAAVAAAKACAYVGAG 273
Cdd:pfam07478 76 LVEEGIEGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSAqivVPAdLEEEQEEQIQELALKAYKALGCRGLA 155
|
170
....*....|....*....
gi 446595329 274 TVEFLLDASGAFYFLEMNT 292
Cdd:pfam07478 156 RVDFFLTEDGEIVLNEVNT 174
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
35-321 |
9.31e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 51.04 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 35 DADRNARHVQEADEAvYIGASKVSESYlsIAKIIEACKKTGADAVHPGY----GFLSENTD-FAQAcidnQITFIGPTAS 109
Cdd:PRK12767 32 DISELAPALYFADKF-YVVPKVTDPNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQNRDrFEEI----GVKVLVSSKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 110 AIELMGSKRLSKIAMIEAGVPCVPGYEGDRQDLEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQaselFEALQTARSEA 189
Cdd:PRK12767 105 VIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVND----KEELEFLLEYV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 190 ENafgsgeLILEKaVIAPRHVEIQVFGDTHGNYVylferdCSIQRRHQKVVEEAPCPVMT---PELRQQMgeaaVAAAKA 266
Cdd:PRK12767 181 PN------LIIQE-FIEGQEYTVDVLCDLNGEVI------SIVPRKRIEVRAGETSKGVTvkdPELFKLA----ERLAEA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446595329 267 CAYVGAGTVEFLLDaSGAFYFLEMNTRLQVEHPVTeLITGLDLVEWQLRVANGEQ 321
Cdd:PRK12767 244 LGARGPLNIQCFVT-DGEPYLFEINPRFGGGYPLS-YMAGANEPDWIIRNLLGGE 296
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
584-636 |
1.46e-06 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 50.95 E-value: 1.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVK 636
Cdd:PRK11856 16 EGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVP 68
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
20-290 |
2.13e-06 |
|
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: 50.07 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 20 QTAKAMGYQtVAVYSDAdrnarhvqEADEAVYIGASKVSESYLSIAKIIEACKKtgADAVhpgyGFLSEN--TDFAQACi 97
Cdd:COG0026 8 LAAKRLGYR-VHVLDPD--------PDSPAAQVADEHIVADYDDEEALREFAER--CDVV----TFEFENvpAEALEAL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 98 dNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEGDrqDLEYLATQAEQIGFPIMVKASAGG-GGRGMRLVQQAS 176
Cdd:COG0026 72 -EAEVPVRPGPEALEIAQDRLLEKAFLAELGIPVAPFAAVD--SLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 177 ELFEALQtarseaenAFGSGELILEK--------AVIAPRhveiqvfgDTHGNYVY--LFErdcSIQRRHQKVVEEAPCP 246
Cdd:COG0026 149 DLEAAWA--------ALGGGPCILEEfvpferelSVIVAR--------SPDGEVATypVVE---NVHRNGILDESIAPAR 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446595329 247 VmTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEM 290
Cdd:COG0026 210 I-SEALAAEAEEIAKRIAEALDYVGVLAVEFFVTKDGELLVNEI 252
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
100-216 |
2.77e-06 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 49.73 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 100 QITFIGP--TASAIelmgS--KRLSKIAMIEAGVPCVPGY---EGDRQDLEYlATQAEQIGFPIMVKASAGGGGRGMRLV 172
Cdd:PRK01966 107 GIPYVGCgvLASAL----SmdKILTKRLLAAAGIPVAPYVvltRGDWEEASL-AEIEAKLGLPVFVKPANLGSSVGISKV 181
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446595329 173 QQASELFEALQTARSEAEnafgsgELILEKAvIAPRHVEIQVFG 216
Cdd:PRK01966 182 KNEEELAAALDLAFEYDR------KVLVEQG-IKGREIECAVLG 218
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
26-323 |
3.86e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 49.54 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 26 GYQTVAVYSDADRNARHVQEADEAVYIGASKVSESYLsIAKIIEACKKTGADAVHPGY----GFLSENTDFaqacIDNQI 101
Cdd:COG3919 28 GVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDPEAF-VDALLELAERHGPDVLIPTGdeyvELLSRHRDE----LEEHY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 102 TFIGPTASAIELMGSK-RLSKIAMiEAGVPCVPGYEGDrqDLEYLATQAEQIGFPIMVKASAG--------GGGRGMRLV 172
Cdd:COG3919 103 RLPYPDADLLDRLLDKeRFYELAE-ELGVPVPKTVVLD--SADDLDALAEDLGFPVVVKPADSvgydelsfPGKKKVFYV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 173 QQASELFEALQTARSEaenafgSGELILEKAVIAPRHVEIQVFG--DTHGNYVYLFerdcSIQRRHQK--------VVEE 242
Cdd:COG3919 180 DDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF----TGRKLRHYppaggnsaARES 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 243 APCPVMTPELRQQMGEAAvaaakacaYVGAGTVEFLLDA-SGAFYFLEMNTRLQVEHPVTeLITGLDLVEWQLRVANGEQ 321
Cdd:COG3919 250 VDDPELEEAARRLLEALG--------YHGFANVEFKRDPrDGEYKLIEINPRFWRSLYLA-TAAGVNFPYLLYDDAVGRP 320
|
..
gi 446595329 322 LP 323
Cdd:COG3919 321 LE 322
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
584-645 |
6.58e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 49.05 E-value: 6.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQ 645
Cdd:PRK11855 132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
584-646 |
3.06e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 47.12 E-value: 3.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQI 646
Cdd:PRK11855 15 EVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEA 77
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
98-322 |
4.81e-05 |
|
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: 46.53 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 98 DNQITFIGPTASAIELMGSK-RLSKIaMIEAGVPCVPGYEGdrQDLEYLATQAEQIGFPIMVKASAGGGGRGMRLVQQAS 176
Cdd:TIGR01369 651 EAGVPILGTSPESIDRAEDReKFSEL-LDELGIPQPKWKTA--TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 177 ELFEALQTArseaenAFGSGE---LI---LEKAviaprhVEIQVFGDTHGNYVYLferdCSIQrRHqkvVEEA------- 243
Cdd:TIGR01369 728 ELRRYLEEA------VAVSPEhpvLIdkyLEDA------VEVDVDAVSDGEEVLI----PGIM-EH---IEEAgvhsgds 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 244 ----PCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDAsGAFYFLEMNTRLQVEHPVTELITGLDLVEWQLRVANG 319
Cdd:TIGR01369 788 tcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLG 866
|
...
gi 446595329 320 EQL 322
Cdd:TIGR01369 867 KKL 869
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
561-636 |
6.18e-05 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 46.02 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 561 RNMTYAAPEATDVAGDGKIRAP-----MDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQV 635
Cdd:TIGR01348 101 AAQAQAAPAAGQSSGVQEVTVPdigdiEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSV 180
|
.
gi 446595329 636 K 636
Cdd:TIGR01348 181 P 181
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
579-627 |
7.29e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 41.33 E-value: 7.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446595329 579 IRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEI 627
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKV 53
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
63-293 |
1.03e-04 |
|
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: 45.25 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 63 SIAKIIEACKktgADAVHPGYG-----FLSEntDFAQACIDNQITFIGPTASAIELMGSKRLSKIAMIEAGVPCVPGYEG 137
Cdd:COG0458 61 DVLDIIEKEK---PDGVIVQFGgqtalNLAV--ELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 138 DRQDlEYLATqAEQIGFPIMVKASAGGGGRGMRLVQQASELFEALQtarsEAENAFGSGELILEKAVIAPRHVEIQVFGD 217
Cdd:COG0458 136 TSVE-EALAI-AEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 218 THGNYVYLferdCSIQrrHqkvVEEA-----------PCPVMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDaSGAFY 286
Cdd:COG0458 210 GEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVY 279
|
....*..
gi 446595329 287 FLEMNTR 293
Cdd:COG0458 280 VIEVNPR 286
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
584-644 |
3.03e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 43.57 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSI 644
Cdd:TIGR01347 14 EGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL 74
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
126-293 |
3.34e-04 |
|
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: 41.86 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 126 EAGVPcVPGYEgDRQDLEYLATQAEQIGFPIMVKASAGG-GGRGMRLVQQASELFEALQtarseaenAFGSGELILEKAV 204
Cdd:pfam02222 2 KLGLP-TPRFM-AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWE--------ELGDGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 205 iaPRHVEIQVFG--DTHGNyVYLFERDCSIQRRHQKVVEEAPCPvMTPELRQQMGEAAVAAAKACAYVGAGTVEFLLDAS 282
Cdd:pfam02222 72 --PFDRELSVLVvrSVDGE-TAFYPVVETIQEDGICRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTED 147
|
170
....*....|.
gi 446595329 283 GAFYFLEMNTR 293
Cdd:pfam02222 148 GDLLINELAPR 158
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
579-618 |
6.39e-04 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 42.24 E-value: 6.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446595329 579 IRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKS 618
Cdd:COG0845 26 VRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQ 65
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
101-205 |
7.86e-04 |
|
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: 42.31 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 101 ITFIGPTASAIELMGSKRLSKIAMIEAGVPcVPGYE--GDRQD-LEYLATQaeqiGFPIMVKAS--AGGGGrgmrlVQQA 175
Cdd:COG0151 87 IPVFGPSKAAAQLEGSKAFAKEFMARYGIP-TAAYRvfTDLEEaLAYLEEQ----GAPIVVKADglAAGKG-----VVVA 156
|
90 100 110
....*....|....*....|....*....|.
gi 446595329 176 SELFEALQTARSE-AENAFGSGElilEKAVI 205
Cdd:COG0151 157 ETLEEALAAVDDMlADGKFGDAG---ARVVI 184
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
578-617 |
1.08e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 37.42 E-value: 1.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446595329 578 KIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIK 617
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQ 43
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
106-290 |
1.41e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 41.29 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 106 PTASAIELMGSKRLSKIAMIEAGVPCVPGYE-GDRQDLEYLAtqaEQIGFPIMVKASAGG-GGRGMRLVQQASELfealq 183
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAVvDSAEDLEAAL---ADLGLPAVLKTRRGGyDGKGQWVIRSAEDL----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 184 tarSEAENAFGSGELILEK--------AVIAPRhveiqvfgDTHGNYVY--LFErdcSIQRRHQKVVEEAPCPVmTPELR 253
Cdd:PRK06019 162 ---EAAWALLGSVPCILEEfvpferevSVIVAR--------GRDGEVVFypLVE---NVHRNGILRTSIAPARI-SAELQ 226
|
170 180 190
....*....|....*....|....*....|....*..
gi 446595329 254 QQMGEAAVAAAKACAYVGAGTVEFLLDASGAFYFLEM 290
Cdd:PRK06019 227 AQAEEIASRIAEELDYVGVLAVEFFVTGDGELLVNEI 263
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
584-627 |
2.22e-03 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 41.01 E-value: 2.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446595329 584 DGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEI 627
Cdd:TIGR01348 13 EGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEI 56
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
592-645 |
2.33e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.30 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446595329 592 VNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVKKRQMLFSIQ 645
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
115-293 |
2.89e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 39.19 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 115 GSKRLSKIAMIEAGVPcVPGYEgDRQDLEYLATQAEQIGFPIMV-KASAGGGGRGMRLVQQASELFEALQTARSEaeNAF 193
Cdd:pfam01071 1 ASKSFAKDFMKRYGIP-TAEYE-TFTDPEEAKSYIQEAGFPAIVvKADGLAAGKGVIVASSNEEAIKAVDEILEQ--KKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595329 194 GSGElilEKAVIAPR--HVEIQVFGDTHGNYVYLFErdcsIQRRHQKVVEE------------APCPVMTPELRQQMGEA 259
Cdd:pfam01071 77 GEAG---ETVVIEEFleGEEVSVLAFVDGKTVKPLP----PAQDHKRAGEGdtgpntggmgaySPAPVITPELLERIKET 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446595329 260 ------AVAAAKACAYVGAGTVEFLLDASGAfYFLEMNTR 293
Cdd:pfam01071 150 iveptvDGLRKEGIPFKGVLYAGLMLTKDGP-KVLEFNCR 188
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
566-636 |
2.97e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 2.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446595329 566 AAPEATDVA----GDGKirapmdGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQVK 636
Cdd:PRK11854 202 AAAGVKDVNvpdiGGDE------VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVK 270
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
578-617 |
7.25e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 7.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446595329 578 KIRAPMDGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIK 617
Cdd:COG1566 47 TVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALA 86
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
566-635 |
8.39e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 39.22 E-value: 8.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446595329 566 AAPEATDVA----GDGKirapmdGAVVNILVNEGDQVVKGQTLLILEAMKIQQQIKSDVDGVVDEILGQQGQQV 635
Cdd:PRK11854 101 AAAAAKDVHvpdiGSDE------VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKV 168
|
|
| |
