|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-473 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 848.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPpvegrnPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRP------PGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGP 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAEEYPDGFsgvkcSEDDARTLAAVAA 473
Cdd:COG4770 395 DREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL-----AAAAPEELALAAA 462
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 673.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPpvegrnPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHP------PGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIaEEY 451
Cdd:PRK08591 395 TREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL-EKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-500 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 653.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDgNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYrppvegRNPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRY------RSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIaEEYPDGFSGVKCSEDDARTLAAVAAEINLVAQ 480
Cdd:PRK08654 394 TREEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFI-EEETTILEEMKRYALEEEEREKTLSEKFFPGN 472
|
490 500
....*....|....*....|
gi 1229255125 481 RRDTQISGRLSPQKHSIAND 500
Cdd:PRK08654 473 KKVAAIAAAVNAYISSAKKD 492
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 636.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPyRNFLPSIGRLTRYRPpvegrnPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTL------PGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFI 447
Cdd:PRK06111 394 TREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-449 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 597.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSN-QSYIVIDKILAAIKEIGADAVH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 80 PGYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKA 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 160 SAGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVI 239
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 240 EEAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGE 319
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 320 KLRFA------QADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYrppvegRNPDGTVIRNDTG-VFEGGEISMYYDPMI 392
Cdd:PRK12999 324 TLHDLeigipsQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAY------RSPGGFGVRLDGGnAFAGAEITPYYDSLL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229255125 393 AKLCTWGPDRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAE 449
Cdd:PRK12999 398 VKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-455 |
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: 589.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSN-QSYIVIDKILAAIKEIGADAVH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 80 PGYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKA 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 160 SAGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVI 239
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 240 EEAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGE 319
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 320 KLR------FAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYrppvegRNPDGTVIRNDTG-VFEGGEISMYYDPMI 392
Cdd:COG1038 323 SLDdpeigiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAY------RSAGGFGIRLDGGnAYTGAVITPYYDSLL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229255125 393 AKLCTWGPDRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIaEEYPDGF 455
Cdd:COG1038 397 VKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFI-DETPELF 458
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-449 |
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: 579.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPpvegrnPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLP------PGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGK 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAE 449
Cdd:TIGR00514 395 TREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 573.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRltryrppVEGRN-PDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWG 399
Cdd:PRK05586 321 LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGK-------IEELYiPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229255125 400 PDRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAEEY 451
Cdd:PRK05586 394 KDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKL 445
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-448 |
0e+00 |
|
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: 553.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 3 KKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHPGY 82
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 83 GFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGhMGLIEDADEAVRIAGSIGYPVMIKASAG 162
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 163 GGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIEEA 242
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 243 PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRN-FYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEKL 321
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 322 RFAQ--ADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPPVEgrnpdgtvIRNDTGVFEGGEISMYYDPMIAKLCTWG 399
Cdd:TIGR02712 321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDD--------VRVDTWVETGTEVSPEYDPMLAKIIVHG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1229255125 400 PDRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIA 448
Cdd:TIGR02712 393 SDREDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLN 441
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-473 |
5.27e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 519.66 E-value: 5.27e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSnQSYIVIDKILAAIKEIGADAVHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKAS 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 161 AGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIE 240
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 241 EAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPpvegrnPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYA------PGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWAL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIaEEYPD--GFSGVKCSEDDARTLAAVAA 473
Cdd:PRK07178 394 TWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFV-ESHPEltNYSIKRKPEELAAAIAAAIA 467
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
2-470 |
1.41e-177 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 513.15 E-value: 1.41e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 2 IKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 82 YGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKASA 161
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 162 GGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHgNVVYLGERECSIQRRNQKVIEE 241
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 242 APSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRN-FYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGeFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 321 LRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPpvegrnPDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGP 400
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVW------PQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 401 DRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAEEYPDGFSGVKCSEDDARTLAA 470
Cdd:PRK12833 398 DRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAALDAAASAAVGEAA 467
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-451 |
2.54e-169 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 491.57 E-value: 2.54e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 2 IKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 82 YGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKASA 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 162 GGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIEE 241
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 242 APSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEKL 321
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 322 rFAQADVKLNGWAIESRLYAEDPyRNFLPSIGRLTRYRPPvEGRNpdgtvIRNDTGVFEGGEISMYYDPMIAKLCTWGPD 401
Cdd:PRK08462 324 -PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAP-GGRN-----VRMDSHAYAGYVVPPYYDSMIGKLIVWGED 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229255125 402 RISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAEEY 451
Cdd:PRK08462 396 RNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEHF 445
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-482 |
4.02e-156 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 458.89 E-value: 4.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 1 MIKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSnQSYIVIDKILAAIKEIGADAVHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GYGFLSENPRFAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRI-AGSIGYPVMIKA 159
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 160 SAGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVI 239
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 240 EEAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGE 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 320 KLRFAQADVKLNGWAIESRLYAEDPYRNFLPSIGRLTRYRPPVegrnpdGTVIRNDTGVFEGGEISMYYDPMIAKLCTWG 399
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPAL------GPSVRVDSHIYKDYTIPPYYDSMLAKLIVKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 400 PDRISAIDAMGHALDAFEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAEEYPDGFSGV--KCSEDDARTLAAVAAEINL 477
Cdd:PRK08463 394 TSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKTedRHQENKEEVIAAIAAALKK 473
|
....*
gi 1229255125 478 VAQRR 482
Cdd:PRK08463 474 IRESR 478
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
7.55e-94 |
|
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: 288.82 E-value: 7.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 115 DKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGD 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 195 DRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECSIQRRNQKVIEEAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTV 274
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1229255125 275 EFIVD-GNRNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEKLR 322
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
63-320 |
6.46e-59 |
|
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: 198.94 E-value: 6.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 63 IDKILAAIKEI----GADAVhpgygfLSEN----PRFAEALKAANvtFIGPPVNAIDAMGDKITSKKLAAEAGVStVPGH 134
Cdd:COG0439 2 IDAIIAAAAELaretGIDAV------LSESefavETAAELAEELG--LPGPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 135 MgLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDEEAREGFQLSRNEAKSSFGDDRIFIEKFVtQPRHIEIQVL 214
Cdd:COG0439 73 A-LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFL-EGREYSVEGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 215 GdQHGNVVYlgereCSIQRRNQK---VIE---EAPSPfLDEATRKAMGEQAVALAKAVGY-YSAGTVEFIVDGNRNFYFL 287
Cdd:COG0439 151 V-RDGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDGEPYLI 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1229255125 288 EMNTRLQVEH--PVTELITGIDLVEEMIRVASGEK 320
Cdd:COG0439 224 EINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
1.12e-58 |
|
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: 192.70 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 2 IKKILIANRGEIACRVIKSAKKKGIATVAVYSDADRNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIKEIGADAVHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1229255125 82 YGFLSENPRFAEALKAANVTFIGPPVNA 109
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-448 |
8.27e-50 |
|
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: 168.75 E-value: 8.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 336 ESRLYAEDPYRNFLPSIGRLTRYRPPvegrnpDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGPDRISAIDAMGHALDA 415
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP------GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDE 74
|
90 100 110
....*....|....*....|....*....|...
gi 1229255125 416 FEVEGIGHNLPFLSAVMDHPRFREGALTTAFIA 448
Cdd:smart00878 75 FRIRGVKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-449 |
2.17e-48 |
|
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: 164.97 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 336 ESRLYAEDPYRNFLPSIGRLTRYRPPvegrnpDGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGPDRISAIDAMGHALDA 415
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP------GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAE 74
|
90 100 110
....*....|....*....|....*....|....
gi 1229255125 416 FEVEGIGHNLPFLSAVMDHPRFREGALTTAFIAE 449
Cdd:pfam02785 75 FRIEGVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| PCC_BT |
pfam18140 |
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ... |
468-592 |
3.13e-45 |
|
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.
Pssm-ID: 465666 [Multi-domain] Cd Length: 126 Bit Score: 157.02 E-value: 3.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 468 LAAVAAEINLVAQRRDTQISGRLSPQKHSIANDWVVTLDGYSLPVRIAEGEGGTTINF-IDGGSLPIASDWHPGSQLGSF 546
Cdd:pfam18140 1 LAAIAAAIHAVRELRARRISGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVtVDGETVTVSSDWRPGDPLFRG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1229255125 547 TVGGKPIAVKVSRSGTGWRLRWRGMDVVAHVRKPRVAELAKLMPVK 592
Cdd:pfam18140 81 TVDGEPVTVQVERRAGGYRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
601-666 |
1.00e-22 |
|
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: 91.71 E-value: 1.00e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229255125 601 LLCPMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEF 666
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
92-322 |
7.73e-18 |
|
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: 88.13 E-value: 7.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 92 AEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGhmGLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIA 171
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 172 WNDEEAREGFQlsrnEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDqHGNVVYLGERECsiqrrnqkvIEEA--------- 242
Cdd:TIGR01369 724 YNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVLIPGIMEH---------IEEAgvhsgdstc 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 243 --PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNrNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVASGEK 320
Cdd:TIGR01369 790 vlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDG-EVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKK 868
|
..
gi 1229255125 321 LR 322
Cdd:TIGR01369 869 LE 870
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
604-666 |
8.90e-18 |
|
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: 87.83 E-value: 8.90e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEF 666
Cdd:COG1038 1082 PMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
60-291 |
2.63e-17 |
|
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: 83.23 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 60 YIVIDK--ILAAIKEIGADAVHPG-YGFLSENPRFAEALKAANVTFIGPPVNAIdAMG-DKITSKKLAAEAGVSTVPGHM 135
Cdd:COG1181 37 PIGIDVedLPAALKELKPDVVFPAlHGRGGEDGTIQGLLELLGIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPYVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 136 GLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDEEAREGFQLSRNEakssfgDDRIFIEKFVTqPRHIEIQVLG 215
Cdd:COG1181 116 LRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DDKVLVEEFID-GREVTVGVLG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 216 DQHGNVVYLGErecsIQRRN-----------QKVIEEAPSPfLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNF 284
Cdd:COG1181 189 NGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEP 263
|
....*..
gi 1229255125 285 YFLEMNT 291
Cdd:COG1181 264 YLLEVNT 270
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
604-667 |
2.75e-16 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 83.26 E-value: 2.75e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK12999 1082 PMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
547-667 |
6.73e-16 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 81.43 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 547 TVGGKPIAVKVSRSGTGWR----LRWRGMDVVAHVRKPRVAELAKLMPVKLPPDTSkmllCPMPGVITSILVKDGETVEA 622
Cdd:PRK09282 471 EVDGEKYEVKIEGVKAEGKrpfyLRVDGMPEEVVVEPLKEIVVGGRPRASAPGAVT----SPMPGTVVKVKVKEGDKVKA 546
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1229255125 623 GQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK09282 547 GDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
92-292 |
1.40e-14 |
|
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: 76.84 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 92 AEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMglIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIA 171
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGT--ATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 172 WNDEE----AREGFQLSRneakssfgDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLgereCSIQrrNqkvIEEA----- 242
Cdd:COG0458 169 YNEEEleeyLERALKVSP--------DHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsg 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229255125 243 ------PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRnFYFLEMNTR 292
Cdd:COG0458 232 dsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-321 |
2.85e-14 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 76.55 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 92 AEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGliEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIA 171
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 172 WNDEearegfQLSRNEAKSSFGDDRIFIEKFVTQpRHIEIQVLGDqhGNVVYLG---ERecsiqrrnqkvIEEA------ 242
Cdd:PRK12815 725 YDEP------ALEAYLAENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiEH-----------IEQAgvhsgd 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 243 -----PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNrNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRVAS 317
Cdd:PRK12815 785 siavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLL 863
|
....
gi 1229255125 318 GEKL 321
Cdd:PRK12815 864 GKSL 867
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
604-666 |
6.99e-14 |
|
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: 66.85 E-value: 6.99e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229255125 604 PMPGV-----ITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEF 666
Cdd:pfam00364 6 PMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-362 |
1.91e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 72.27 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 17 VIKSAKKKGIATVAVYSDADRNALHVKMADEaVHIGPAPSNQSYIVIDKILAAIKEIGADAVHPGY----GFLSENprfA 92
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDE-VVVVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRH---R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 93 EALkAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVStVPgHMGLIEDADEAVRIAGSIGYPVMIKAS--------AGGG 164
Cdd:COG3919 96 DEL-EEHYRLPYPDADLLDRLLDKERFYELAEELGVP-VP-KTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 165 GKGMRIAWNDEEAREGFqlsrneAKSSFGDDRIFIEKFVTQPRHIEIQVLG--DQHGNVVYLgereCSIQRRNQKVIEEA 242
Cdd:COG3919 173 KKKVFYVDDREELLALL------RRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 243 PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRN-FYFLEMNTRLQVEHPVTeLITGIDLVEEMIRVASGEKL 321
Cdd:COG3919 243 NSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRFWRSLYLA-TAAGVNFPYLLYDDAVGRPL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1229255125 322 RFAQADVKLNGWAIES-----RLYAEDPYRNFLPSIGRLTRYRPPV 362
Cdd:COG3919 322 EPVPAYREGVLWRVLPgdlllRYLRDGELRKRLRELLRRGKVVDAV 367
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
555-667 |
8.83e-13 |
|
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: 65.69 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 555 VKVSRSGTGWRLRWRGMDVVAHVRKPRVAELAKLMPVKLPPDTSKM----LLCPMPGVI-------TSILVKDGETVEAG 623
Cdd:COG0511 13 LEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAPAAAAAAAAASgggaVKSPMVGTFyrapspgAKPFVKVGDKVKAG 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1229255125 624 QPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:COG0511 93 DTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
604-667 |
8.43e-12 |
|
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: 68.70 E-value: 8.43e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:TIGR01235 1080 PMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
582-663 |
9.95e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 62.52 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 582 VAELAKLMPVKLPPDTSKMLLCPMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSL-AVD 660
Cdd:PRK06549 45 SPQVEAQAPQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVnPGD 124
|
...
gi 1229255125 661 ELI 663
Cdd:PRK06549 125 GLI 127
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
604-660 |
8.12e-11 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 60.65 E-value: 8.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSslAVD 660
Cdd:PRK05641 90 PMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGD--TVD 144
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
95-291 |
4.02e-10 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 61.68 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 95 LKAANVTFIGPPVNAiDAMG-DKITSKKLAAEAGVSTVPGHMGLIEDADEAV--RIAGSIGYPVMIKAsaggggkgmria 171
Cdd:PRK01966 103 LELLGIPYVGCGVLA-SALSmDKILTKRLLAAAGIPVAPYVVLTRGDWEEASlaEIEAKLGLPVFVKP------------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 172 wndeeAREGfqlsrneakSSFG--------------------DDRIFIEKFVtQPRHIEIQVLGDqHGNVVYLGERECS- 230
Cdd:PRK01966 170 -----ANLG---------SSVGiskvkneeelaaaldlafeyDRKVLVEQGI-KGREIECAVLGN-DPKASVPGEIVKPd 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 231 ---------IQRRNQKVIeEAPspfLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNT 291
Cdd:PRK01966 234 dfydyeakyLDGSAELII-PAD---LSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
92-321 |
7.16e-10 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 62.42 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 92 AEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGhmGLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIA 171
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 172 WNDEEAREGFqlsrNEAKSSFGDDRIFIEKFVTqpRHIEIQV--LGDqhGNVVYLG---ERecsiqrrnqkvIEEA---- 242
Cdd:PRK05294 724 YDEEELERYM----REAVKVSPDHPVLIDKFLE--GAIEVDVdaICD--GEDVLIGgimEH-----------IEEAgvhs 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 243 -------PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNrNFYFLEMNTRLQVEHPVTELITGIDLVEEMIRV 315
Cdd:PRK05294 785 gdsacslPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDD-EVYVIEVNPRASRTVPFVSKATGVPLAKIAARV 863
|
....*.
gi 1229255125 316 ASGEKL 321
Cdd:PRK05294 864 MLGKKL 869
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-293 |
7.42e-10 |
|
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: 62.32 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 2 IKKILIANRGEI----AC-------RVIKSAKKKGIATVAVYSDADRNALHVKMADEaVHIGPapsnqsyIVIDKILAAI 70
Cdd:TIGR01369 6 IKKILVIGSGPIvigqAAefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADK-VYIEP-------LTPEAVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 71 KEIGADAVHPGYG---------FLSEnprfAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMglIEDA 141
Cdd:TIGR01369 78 EKERPDAILPTFGgqtalnlavELEE----SGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEI--AHSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 142 DEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDEEARE----GFQLSRNeakssfgdDRIFIEKFVTQPRHIEIQVLGDQ 217
Cdd:TIGR01369 152 EEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEiaerALSASPI--------NQVLVEKSLAGWKEIEYEVMRDS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 218 HGNVVYLgereCSIQR------RNQKVIEEAPSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVD-GNRNFYFLEMN 290
Cdd:TIGR01369 224 NDNCITV----CNMENfdpmgvHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVN 299
|
...
gi 1229255125 291 TRL 293
Cdd:TIGR01369 300 PRV 302
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
62-291 |
1.81e-09 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 59.35 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 62 VIDKILAAIKEIGADAV----HPGYGflsENPRFAEALKAANVTFIGPPVN--AIdAMgDKITSKKLAAEAGVSTVPGHM 135
Cdd:PRK01372 44 PGEDIAAQLKELGFDRVfnalHGRGG---EDGTIQGLLELLGIPYTGSGVLasAL-AM-DKLRTKLVWQAAGLPTPPWIV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 136 glIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDEEAREGFQLsrnEAKSsfgDDRIFIEKFVTQPrhiEIQ--V 213
Cdd:PRK01372 119 --LTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALEL---AFKY---DDEVLVEKYIKGR---ELTvaV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 214 LGDQ----------HGNVVYlgerecsiqrrNQKVIEEA-----PSPFLDEATRKAMgEQAVALAKAVGYYSAGTVEFIV 278
Cdd:PRK01372 188 LGGKalpvieivpaGEFYDY-----------EAKYLAGGtqyicPAGLPAEIEAELQ-ELALKAYRALGCRGWGRVDFML 255
|
250
....*....|...
gi 1229255125 279 DGNRNFYFLEMNT 291
Cdd:PRK01372 256 DEDGKPYLLEVNT 268
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
540-664 |
1.92e-09 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 60.71 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 540 GSQLGSFTVGGKPIAVKVSRSGTgwrlrwrgmdvVAHVRKPRVAELAKLMPVKLPPDTSKM-LLCPMPGVITSILVKDGE 618
Cdd:PRK14040 476 GSETYTVEVEGKAYVVKVSEGGD-----------ISQITPAAPAAAPAAAAAAAPAAAAGEpVTAPLAGNIFKVIVTEGQ 544
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1229255125 619 TVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIM 664
Cdd:PRK14040 545 TVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
605-667 |
6.48e-08 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 49.79 E-value: 6.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229255125 605 MPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK08225 8 MAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
4-320 |
1.32e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 53.73 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 4 KILIANrgeIACRV--IKSAKK-KGIATVaVYSDADRNALHVKMADEAVhIGPAPSNQSYIviDKILAAIKEIGADAVHP 80
Cdd:PRK12767 3 NILVTS---AGRRVqlVKALKKsLLKGRV-IGADISELAPALYFADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 81 GY----GFLSENprfAEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGHMGLIEDADEAVRIAGSIGYPVM 156
Cdd:PRK12767 76 LIdpelPLLAQN---RDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 157 IK-----ASAggggkGMRIAWNDEEAREGFQLSRNeakssfgddrIFIEKFVTQPRhIEIQVLGDQHGNVVylgereCSI 231
Cdd:PRK12767 153 VKprdgsASI-----GVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQE-YTVDVLCDLNGEVI------SIV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 232 QRRNQKVIeeapspflDEATRKA-------MGEQAVALAKAVGYYSAGTVEFIVDGNRnFYFLEMNTRLQVEHPVTeLIT 304
Cdd:PRK12767 211 PRKRIEVR--------AGETSKGvtvkdpeLFKLAERLAEALGARGPLNIQCFVTDGE-PYLFEINPRFGGGYPLS-YMA 280
|
330
....*....|....*.
gi 1229255125 305 GIDLVEEMIRVASGEK 320
Cdd:PRK12767 281 GANEPDWIIRNLLGGE 296
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
2-293 |
1.98e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 54.40 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 2 IKKILIANRGEI----AC-------RVIKSAKKKGIATVAVYSDADRNALHVKMADEAvHIGPAPSNqsyiVIDKILAAI 70
Cdd:PLN02735 23 LKKIMILGAGPIvigqACefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRT-YIAPMTPE----LVEQVIAKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 71 KeigADAVHPGYG---FLSENPRFAE--ALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGhmGLIEDADEAV 145
Cdd:PLN02735 98 R---PDALLPTMGgqtALNLAVALAEsgILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPS--GIATTLDECF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 146 RIAGSIG-YPVMIKASAGGGGKGMRIAWNDEEAREGFQLSRNEAKSSfgddRIFIEKFVTQPRHIEIQVLGDQHGNVVYL 224
Cdd:PLN02735 173 EIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELEVMRDLADNVVII 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229255125 225 gereCSIQR------RNQKVIEEAPSPFLDEATRKAMGEQAVALAKAVGYYSAGT-VEFIV---DGnrNFYFLEMNTRL 293
Cdd:PLN02735 249 ----CSIENidpmgvHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVnpvDG--EVMIIEMNPRV 321
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
607-666 |
2.19e-07 |
|
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: 48.52 E-value: 2.19e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEF 666
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
84-292 |
6.53e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 52.86 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 84 FLSENPRFAeALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTVPGhmGLIEDADEAVRIAGSIGYPVMIKASAGG 163
Cdd:PLN02735 672 YLDKNPPPS-ASGNGNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 164 GGKGMRIAWNDEEaregfqLSR--NEAKSSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERECsiqrrnqkvIEE 241
Cdd:PLN02735 749 GGRAMEIVYSDDK------LKTylETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVVIGGIMEH---------IEQ 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229255125 242 A-----------PSPFLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNTR 292
Cdd:PLN02735 814 AgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
2-231 |
9.65e-07 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 52.41 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 2 IKKILIANRGEI--------------ACRVIKsakKKGIATVAVYS-------DADrnalhvkMADeAVHIGPapsnqsy 60
Cdd:PRK05294 7 IKKILIIGSGPIvigqacefdysgtqACKALR---EEGYRVVLVNSnpatimtDPE-------MAD-ATYIEP------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 61 I---VIDKILAaiKEiGADAVHPGYG---------FLSENprfaEALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGV 128
Cdd:PRK05294 69 ItpeFVEKIIE--KE-RPDAILPTMGgqtalnlavELAES----GVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 129 STVPGhmGLIEDADEAVRIAGSIGYPVMIkasaggggkgmR-----------IAWNDEE----AREGFQLSRNeakssfg 193
Cdd:PRK05294 142 PVPRS--GIAHSMEEALEVAEEIGYPVII-----------RpsftlggtgggIAYNEEEleeiVERGLDLSPV------- 201
|
250 260 270
....*....|....*....|....*....|....*...
gi 1229255125 194 dDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLgereCSI 231
Cdd:PRK05294 202 -TEVLIEESLLGWKEYEYEVMRDKNDNCIIV----CSI 234
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
590-660 |
3.28e-06 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 49.07 E-value: 3.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229255125 590 PVKLPPDTSKMLLCPM-------PGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVD 660
Cdd:PLN02983 189 PAKAPKSSHPPLKSPMagtfyrsPAPGEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVD 266
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
607-667 |
4.78e-06 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 49.62 E-value: 4.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
147-291 |
1.65e-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: 46.16 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 147 IAGSIGYPVMIKASAGGGGKGMRIAWNDEEAREGFQLSRNEakssfgDDRIFIEKFVtQPRHIEIQVLGDQHGNVVYLGE 226
Cdd:pfam07478 31 VEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------DEKVLVEEGI-EGREIECAVLGNEDPEVSPVGE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229255125 227 R--ECSIQRRNQKVIEEA-----PSPfLDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMNT 291
Cdd:pfam07478 104 IvpSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
94-293 |
1.77e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 48.04 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 94 ALKAANVTFIGPPVNAIDAMGDKITSKKLAAEAGVSTvpGHMGLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWN 173
Cdd:PRK12815 107 ILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 174 DEEAREGFQlsRNEAKSSFGDdrIFIEKFVTQPRHIEIQVLGDQHGNVVYLGERE----CSIQRRNQKVIeeAPSPFLDE 249
Cdd:PRK12815 185 LEELEQLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVCNMEnidpVGIHTGDSIVV--APSQTLTD 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1229255125 250 ATRKAMGEQAVALAKAVGYYSAGTVEFIVDGN-RNFYFLEMNTRL 293
Cdd:PRK12815 259 DEYQMLRSASLKIISALGVVGGCNIQFALDPKsKQYYLIEVNPRV 303
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
607-667 |
2.14e-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: 47.56 E-value: 2.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-314 |
3.46e-05 |
|
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: 46.09 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 16 RVIKSAKKKGIatvavysdadrNALHVKMADEAVHIGPAPSNQSYIVIDKILAAIkeIGADAVHPGYGFLsenprfaEAL 95
Cdd:COG0189 18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSEFDAVL--PRIDPPFYGLALL-------RQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 96 KAANVTFIGPPvNAIDAMGDKITSKKLAAEAGVSTVPghMGLIEDADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDE 175
Cdd:COG0189 78 EAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPP--TLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 176 EARegfqlSRNEAKSSFGDDRIFIEKFV--TQPRHIEIQVLGdqhGNVVYLGER-----ECSIQRRNQKVIEEAPspfLD 248
Cdd:COG0189 155 ALE-----SILEALTELGSEPVLVQEFIpeEDGRDIRVLVVG---GEPVAAIRRipaegEFRTNLARGGRAEPVE---LT 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229255125 249 EATRkamgEQAVALAKAVGYYSAGtVEFIVDGNRnFYFLEMNTRLQVEHpvTELITGIDLVEEMIR 314
Cdd:COG0189 224 DEER----ELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEAIAD 281
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
607-667 |
6.57e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 46.15 E-value: 6.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
92-289 |
8.78e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 45.14 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 92 AEALK--AANVTFIgPPVNAIDAMGDKITSKKLAAEAGVSTVPGHmgLIEDADEAVRIAGSIGYPVMIKASaggggkGM- 168
Cdd:PRK06019 76 AEALDalAARVPVP-PGPDALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTR------RGg 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 169 -------RIAwNDEEAREGFQLsrneakssFGDDRIFIEKFVTQPRhiEIQVLG--DQHGNVVY--LGErecSIQRRNQK 237
Cdd:PRK06019 147 ydgkgqwVIR-SAEDLEAAWAL--------LGSVPCILEEFVPFER--EVSVIVarGRDGEVVFypLVE---NVHRNGIL 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1229255125 238 VIEEAPSPfLDEATRKAMGEQAVALAKAVGYysAGT--VEFIVDGNRNFYFLEM 289
Cdd:PRK06019 213 RTSIAPAR-ISAELQAQAEEIASRIAEELDY--VGVlaVEFFVTGDGELLVNEI 263
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
604-662 |
1.16e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.65 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVLR------AERRATVKRITAEAGSSLAVDEL 662
Cdd:COG1566 51 KVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAqaeaqlAAAEAQLARLEAELGAEAEIAAA 115
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
607-667 |
1.55e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.99 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
119-159 |
2.45e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 44.35 E-value: 2.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1229255125 119 SKKLAAEAGVSTVPGHmgLIEDADEAVRIAGSIGYPVMIKA 159
Cdd:COG1042 493 AKALLAAYGIPVVPTR--LARSAEEAVAAAEEIGYPVVLKI 531
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
605-667 |
3.63e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 43.56 E-value: 3.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229255125 605 MPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
607-654 |
4.83e-04 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 38.96 E-value: 4.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAG 654
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEG 61
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
580-667 |
4.97e-04 |
|
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: 43.32 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 580 PRVAELAKLMPVKLPP--DTSKmllcpmpGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSL 657
Cdd:TIGR01348 108 PAAGQSSGVQEVTVPDigDIEK-------VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSV 180
|
90
....*....|
gi 1229255125 658 AVDELIMEFE 667
Cdd:TIGR01348 181 PTGDLILTLS 190
|
|
| BCCP |
TIGR00531 |
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ... |
614-667 |
7.36e-04 |
|
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273123 [Multi-domain] Cd Length: 155 Bit Score: 40.59 E-value: 7.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1229255125 614 VKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:TIGR00531 102 VEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
119-158 |
1.71e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 40.54 E-value: 1.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1229255125 119 SKKLAAEAGVSTVPGHmgLIEDADEAVRIAGSIGYPVMIK 158
Cdd:pfam13549 15 AKALLAAYGIPVVPTR--LARSPEEAVAAAEEIGYPVVLK 52
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
109-158 |
1.75e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 41.68 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 109 AIDAMGDKITSKKLAAEAGVStVPghMG-LIEDADEAVRIAGSIGYPVMIK 158
Cdd:PRK14016 208 AVDIACDKELTKRLLAAAGVP-VP--EGrVVTSAEDAWEAAEEIGYPVVVK 255
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
604-662 |
1.80e-03 |
|
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: 41.08 E-value: 1.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVLrAERRATVKRitAEAGSSLAVDEL 662
Cdd:COG0845 29 RVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAAL-AQAQAQLAA--AQAQLELAKAEL 84
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
115-314 |
1.83e-03 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 39.79 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 115 DKITSKKLAAEAGVStvPGHMGLIEDADEAVRIAGSIG--YPVMIKASAGGGGKGMRIAWNDEEAREGFQLSRNEakssf 192
Cdd:pfam08443 3 DKAKSHQLLAKHGIG--PPNTRLAWYPEDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNEQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 193 gddrIFIEKFV--TQPRHIEIQVLGDQhgnVVylgereCSIQRRNQKvieeapSPFLDEATRKAMGEQ----------AV 260
Cdd:pfam08443 76 ----ILVQEFIaeANNEDIRCLVVGDQ---VV------GALHRQSNE------GDFRSNLHRGGVGEKyqlsqeetelAI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1229255125 261 ALAKAVGYYSAGtVEfIVDGNRNFYFLEMNTRLQVEHpvTELITGIDLVEEMIR 314
Cdd:pfam08443 137 KAAQAMQLDVAG-VD-LLRQKRGLLVCEVNSSPGLEG--IEKTLGINIAIKIIA 186
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
95-290 |
1.96e-03 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 41.34 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 95 LKAANVTFIGP-PVNAIDAMgDKITSKKLAAEAGVSTVPGH----MGLIEDADEAV-RIAGSIGYPVMIKASAGGGGKGM 168
Cdd:PRK14573 548 LEIIGKPYTGPsLAFSAIAM-DKVLTKRFASDVGVPVVPYQpltlAGWKREPELCLaHIVEAFSFPMFVKTAHLGSSIGV 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 169 RIAWNDEEAREGFqlsrNEAksSFGDDRIFIEKFVTQPRHIEIQVLGDQHGNVVYLGEREcsiqRRNQKV---------- 238
Cdd:PRK14573 627 FEVHNVEELRDKI----SEA--FLYDTDVFVEESRLGSREIEVSCLGDGSSAYVIAGPHE----RRGSGGfidyqekygl 696
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229255125 239 --IEEAPSPF---LDEATRKAMGEQAVALAKAVGYYSAGTVEFIVDGNRNFYFLEMN 290
Cdd:PRK14573 697 sgKSSAQIVFdldLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
604-638 |
3.13e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 35.88 E-value: 3.13e-03
10 20 30
....*....|....*....|....*....|....*
gi 1229255125 604 PMPGVITSILVKDGETVEAGQPLATVEAMKMENVL 638
Cdd:pfam13533 8 PVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQL 42
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
606-642 |
3.20e-03 |
|
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439927 [Multi-domain] Cd Length: 272 Bit Score: 40.00 E-value: 3.20e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1229255125 606 PGVITSILVKDGETVEAGQPLATVEAmKMENVLRAER 642
Cdd:COG0157 57 PGLEVEWLVADGDRVEAGDVLLEVEG-PARALLTAER 92
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
609-667 |
3.73e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 40.19 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229255125 609 ITSILVKDGETVEAGQPLATVEAMK--MEnvLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
607-667 |
3.85e-03 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 39.99 E-value: 3.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229255125 607 GVITSILVKDGETVEAGQPLATVEAMKME--------NVLRAERRATVKRITAEAGSSLAVDELIMEFE 667
Cdd:TIGR01843 52 GIVREILVREGDRVKAGQVLVELDATDVEadaaelesQVLRLEAEVARLRAEADSQAAIEFPDDLLSAE 120
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
603-629 |
3.89e-03 |
|
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: 36.61 E-value: 3.89e-03
10 20
....*....|....*....|....*..
gi 1229255125 603 CPMPGVITSILVKDGETVEAGQPLATV 629
Cdd:cd06849 48 APAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
603-629 |
6.84e-03 |
|
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: 35.81 E-value: 6.84e-03
10 20
....*....|....*....|....*..
gi 1229255125 603 CPMPGVITSILVKDGETVEAGQPLATV 629
Cdd:COG0508 50 APAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
124-278 |
7.11e-03 |
|
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: 38.00 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 124 AEAGVSTvPGHMgLIEDADEAVRIAGSIGYPVMIKASaggggkGM-------RIAWNDEEAREGFQLsrneakssFGDDR 196
Cdd:pfam02222 1 QKLGLPT-PRFM-AAESLEELIEAGQELGYPCVVKAR------RGgydgkgqYVVRSEADLPQAWEE--------LGDGP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 197 IFIEKFVtqPRHIEIQVLGDQHGNvvylGEREC-----SIQRRNQKVIEEAPSPFLDEATRKAMgEQAVALAKAVGYYSA 271
Cdd:pfam02222 65 VIVEEFV--PFDRELSVLVVRSVD----GETAFypvveTIQEDGICRLSVAPARVPQAIQAEAQ-DIAKRLVDELGGVGV 137
|
....*..
gi 1229255125 272 GTVEFIV 278
Cdd:pfam02222 138 FGVELFV 144
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
63-182 |
9.83e-03 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 38.45 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229255125 63 IDKILAAIKEIGADAVHPGYGFLSEN--PRFAEALKAANVTfigppVNAIDAMGDKITSKKLAAEAGvstvpghmglIED 140
Cdd:COG1082 15 LEEALRAAAELGYDGVELAGGDLDEAdlAELRAALADHGLE-----ISSLHAPGLNLAPDPEVREAA----------LER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1229255125 141 ADEAVRIAGSIGYPVMIKASAGGGGKGMRIAWNDEEAREGFQ 182
Cdd:COG1082 80 LKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDRLAERLR 121
|
|
| |
