|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
37-486 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 800.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 357 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 436
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 189095269 437 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 486
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
36-478 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 677.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 36 TFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHP 115
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 116 GYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAS 195
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 196 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 275
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 276 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 355
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 356 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSD 432
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGET 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 189095269 433 RTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 478
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
37-496 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 651.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 357 RHKQADIRINGWAVECRVYAEDPyKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 436
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTF-FPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 437 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDvypdgfkgHMLTKSEK 496
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK--------QLVKKSTK 450
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
37-480 |
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 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVdSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 357 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 436
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDF-APSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 189095269 437 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 480
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
37-478 |
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: 570.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 357 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 436
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 189095269 437 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 478
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
37-480 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 570.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 357 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQyqepLHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDR 433
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGF-MPCPGKIEE----LYIPGglgVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 189095269 434 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 480
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
33-480 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 565.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 33 TLKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVG--PAPtSKSYLNMDAIMEAIKKTRA 110
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGegKHP-VRAYLDIDEIIRVAKQAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 111 QAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPV 190
Cdd:PRK12999 80 DAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 191 MIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRN 270
Cdd:PRK12999 160 MLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 271 QKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRV 350
Cdd:PRK12999 240 QKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 351 AKGYPLR------HKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQ-PGSDISIYYDPMI 423
Cdd:PRK12999 320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPANNF-MPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 189095269 424 SKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 480
Cdd:PRK12999 398 VKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
34-477 |
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: 556.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 34 LKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPA--PTsKSYLNMDAIMEAIKKTRAQ 111
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGkgPV-DAYLDIEEIIRVAKEKGVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 112 AVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVM 191
Cdd:COG1038 80 AIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 192 IKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQ 271
Cdd:COG1038 160 LKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 272 KVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVA 351
Cdd:COG1038 240 KVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 352 KGYPLRHK------QADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSG-IQPGSDISIYYDPMIS 424
Cdd:COG1038 320 EGYSLDDPeigipsQEDIRLNGYAIQCRITTEDPANNF-MPDTGRITAYRSAGG-FGIRLDGGnAYTGAVITPYYDSLLV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 189095269 425 KLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKF 477
Cdd:COG1038 398 KVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
37-483 |
2.99e-179 |
|
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: 543.09 E-value: 2.99e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 355
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 356 LRHKQ--ADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlhlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDR 433
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPAKNF-QPSPGLLTDVQFP---DDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 189095269 434 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD-VYP 483
Cdd:TIGR02712 396 EDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSfVYT 446
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
35-478 |
1.73e-175 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 509.30 E-value: 1.73e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 35 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVH 114
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 115 PGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKA 194
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 195 SAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHgNALWLNERECSIQRRNQKVV 274
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 275 EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKG 353
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 354 YPLRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDR 433
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDF-FPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 189095269 434 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 478
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
37-478 |
6.45e-170 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 495.39 E-value: 6.45e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSkSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 196
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 197 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 276
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 357 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 436
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDF-LPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 189095269 437 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 478
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFV 440
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-479 |
3.46e-167 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 487.33 E-value: 3.46e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 39 KILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYG 118
Cdd:PRK08462 6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 119 FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGG 198
Cdd:PRK08462 86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 199 GGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAP 278
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 279 SIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLrH 358
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL-P 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 359 KQADIRINGWAVECRVYAEDPyKSFgLPSIGRLSQYqeplHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTE 435
Cdd:PRK08462 325 SQESIKLKGHAIECRITAEDP-KKF-YPSPGKITKW----IAPGgrnVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 189095269 436 ALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLS 479
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
37-478 |
8.19e-145 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 431.16 E-value: 8.19e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTsKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRI-AREIGYPVMIKAS 195
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 196 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 275
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 276 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 355
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 356 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTE 435
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNF-IPSPGKITEYYPALG-PSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 189095269 436 ALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 478
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYI 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
150-357 |
1.18e-100 |
|
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: 307.31 E-value: 1.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 150 DKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGD 229
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 230 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTV 309
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 189095269 310 EFLVDSK-KNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLR 357
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
37-144 |
5.68e-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: 5.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 37 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 116
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 189095269 117 YGFLSENKEFARCLAAEDVVFIGPDTHA 144
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
97-351 |
1.07e-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: 193.55 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 97 NMDAIMEAIKKTRAQavHPGYGFLSENkEFARCLAAEdVV----FIGPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgV 172
Cdd:COG0439 1 DIDAIIAAAAELARE--TGIDAVLSES-EFAVETAAE-LAeelgLPGPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 173 VKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDk 252
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 253 HGNALWlnereCSIQRRNQK---VVE---EAPSIfLDAETRRAMGEQAVALARAVKYS-SAGTVEFLVDSKKNFYFLEMN 325
Cdd:COG0439 153 DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEIN 226
|
250 260
....*....|....*....|....*...
gi 189095269 326 TRLQVEH--PVTECITGLDLVQEMIRVA 351
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLA 254
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
371-478 |
1.34e-49 |
|
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: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 371 ECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 450
Cdd:smart00878 1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78
|
90 100
....*....|....*....|....*...
gi 189095269 451 GVTHNIALLREVIINSRFVKGDISTKFL 478
Cdd:smart00878 79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
371-480 |
3.69e-49 |
|
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: 167.67 E-value: 3.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 371 ECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 450
Cdd:pfam02785 1 EARIYAEDPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIE 78
|
90 100 110
....*....|....*....|....*....|
gi 189095269 451 GVTHNIALLREVIINSRFVKGDISTKFLSD 480
Cdd:pfam02785 79 GVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| PCC_BT |
pfam18140 |
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ... |
499-627 |
4.23e-35 |
|
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: 129.28 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 499 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 578
Cdd:pfam18140 1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 189095269 579 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 627
Cdd:pfam18140 80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
635-701 |
2.33e-28 |
|
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: 107.89 E-value: 2.33e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189095269 635 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
638-702 |
4.15e-21 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 98.67 E-value: 4.15e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189095269 638 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
638-701 |
2.25e-20 |
|
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: 96.30 E-value: 2.25e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189095269 638 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
635-701 |
5.64e-20 |
|
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: 84.19 E-value: 5.64e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189095269 635 VLRSPMPGVVVA-----VSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
635-702 |
2.87e-19 |
|
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: 84.56 E-value: 2.87e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189095269 635 VLRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:COG0511 62 AVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
555-702 |
1.39e-18 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 89.90 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 555 FSVEVDGSKLNV--TSTWNLASPLLSVSVDGTQRTVQclsreaggnmsiqflgtvykvniltrlAAELNKF-MLEKVTED 631
Cdd:PRK09282 468 FKVEVDGEKYEVkiEGVKAEGKRPFYLRVDGMPEEVV---------------------------VEPLKEIvVGGRPRAS 520
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 632 TSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK09282 521 APGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
634-702 |
9.82e-18 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 77.91 E-value: 9.82e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189095269 634 SVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
49-327 |
2.00e-17 |
|
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: 86.09 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 49 ACRVIRtckKMGIKTVAIHS-------DVDassvhvkMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG--- 118
Cdd:COG0458 21 ACKALR---EEGYEVILVNSnpetvstDYD-------TAD-RLYFEP-------LTVEDVLDIIEKEKPDGVIVQFGgqt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 119 ------FLSENKEFarclaaEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIG 187
Cdd:COG0458 83 alnlavELEEAGIL------EGVKILGTSPDAI----DLAEdrelfKELL-DKLGIPQPKS--GTATSVEEALAIAEEIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 188 YPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSsqeaassfGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnere 263
Cdd:COG0458 150 YPVIVRPSYVLGGRGMGIVYNEEEleeyLERALKVS--------PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV---- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189095269 264 CSIQrrNqkvVEEA-----------PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 327
Cdd:COG0458 218 GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
635-699 |
7.11e-17 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 77.54 E-value: 7.11e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189095269 635 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLV 699
Cdd:PRK06549 63 AMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
635-701 |
3.68e-15 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 73.36 E-value: 3.68e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189095269 635 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:PRK05641 86 VVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
52-357 |
1.84e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 77.35 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 52 VIRTCKKMGIKTVAIHSDVDASSVHVKMADeavcvgpaptsKSY---LNMDAIMEAIKKTRAQAVHPGYGFLSENKeFAR 128
Cdd:TIGR01369 580 AVLALRELGYETIMINYNPETVSTDYDTSD-----------RLYfepLTFEDVMNIIELEKPEGVIVQFGGQTPLN-LAK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 129 CLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGM 203
Cdd:TIGR01369 648 ALEEAGVPILGTSPESI----DRAEdrekfSELL-DELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 204 RIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPRHIEIQVLGDkHGNALwlnerECSIQRRnqkvVEEA------ 277
Cdd:TIGR01369 721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVL-----IPGIMEH----IEEAgvhsgd 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 278 -----PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAK 352
Cdd:TIGR01369 787 stcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865
|
....*
gi 189095269 353 GYPLR 357
Cdd:TIGR01369 866 GKKLE 870
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
638-702 |
2.97e-14 |
|
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: 76.79 E-value: 2.97e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189095269 638 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:TIGR01235 1079 APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
100-326 |
1.95e-13 |
|
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: 71.68 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 100 AIMEAIKKTRAQAVhpgyGFLSENKEFARCLAAE--DVVFI--------------------------GPDTHAIqAMgDK 151
Cdd:COG1181 23 AVAAALDKAGYDVV----PIGIDVEDLPAALKELkpDVVFPalhgrggedgtiqgllellgipytgsGVLASAL-AM-DK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 152 IESKLLAKKAEVNTIPGFdgVVKDAEEAV--RIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgD 229
Cdd:COG1181 97 ALTKRVLAAAGLPTPPYV--VLRRGELADleAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAAL-----EEAFKY-D 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 230 DRLLIEKFIDnPRHIEIQVLGDKHGNALWLNErecsIQRRN-----------QKVVEEAPSIfLDAETRRAMGEQAVALA 298
Cdd:COG1181 169 DKVLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEELEERIQELALKAF 242
|
250 260
....*....|....*....|....*...
gi 189095269 299 RAVKYSSAGTVEFLVDSKKNFYFLEMNT 326
Cdd:COG1181 243 RALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
52-328 |
1.84e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 69.57 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 52 VIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVcVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGY----GFLSENKEFA 127
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVV-VVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 128 rclaAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKASaggggkgMRIAW 207
Cdd:COG3919 99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPA-------DSVGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 208 DD---EETRDGFRLSSQEA------ASSFGDDRLLIEKFIDNPRHIEIQVLG--DKHGNALWLnereCSIQRRNQKVVEE 276
Cdd:COG3919 166 DElsfPGKKKVFYVDDREEllallrRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 189095269 277 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRL 328
Cdd:COG3919 242 GNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRF 294
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
638-701 |
4.25e-12 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 69.19 E-value: 4.25e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189095269 638 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:PRK14040 529 APLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
147-326 |
5.80e-12 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 67.06 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 147 AMgDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEaass 226
Cdd:PRK01372 96 AM-DKLRTKLVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 227 fgDDRLLIEKFIDNPrhiEIQ--VLGDKhgnALwlnerecsiqrrnqKVVE-EAPSIF-------------------LDA 284
Cdd:PRK01372 169 --DDEVLVEKYIKGR---ELTvaVLGGK---AL--------------PVIEiVPAGEFydyeakylaggtqyicpagLPA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 189095269 285 ETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 326
Cdd:PRK01372 227 EIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
642-701 |
2.40e-11 |
|
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: 59.73 E-value: 2.40e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
642-701 |
2.09e-09 |
|
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: 54.30 E-value: 2.09e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
640-702 |
2.23e-09 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 60.51 E-value: 2.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189095269 640 MPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
127-248 |
5.14e-09 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 59.73 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 127 ARCLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKAS------ 195
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAI----DLAEdrerfSKLL-EKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSyvlggr 718
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 189095269 196 AggggkgMRIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPrhIEIQV 248
Cdd:PRK05294 719 A------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGA--IEVDV 759
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
642-701 |
5.73e-09 |
|
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: 53.21 E-value: 5.73e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
138-353 |
6.26e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 59.60 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 138 IGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEEtrdgfr 217
Cdd:PRK12815 658 LGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA------ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 218 LSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDkhGNALWLN---ERecsiqrrnqkvVEEA-----------PSIFLD 283
Cdd:PRK12815 730 LEAYLAENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiEH-----------IEQAgvhsgdsiavlPPQSLS 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 284 AETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKG 353
Cdd:PRK12815 796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
46-328 |
3.64e-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: 56.93 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 46 GEIACRVIrtcKKMGIKTVAIHSDVDASSVHVKMADEaVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG-----FL 120
Cdd:TIGR01369 29 GSQACKAL---KEEGYRVILVNSNPATIMTDPEMADK-VYIEP-------LTPEAVEKIIEKERPDAILPTFGgqtalNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 121 SENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKASAGGGG 200
Cdd:TIGR01369 98 AVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESE--IAHSVEEALAAAKEIGYPVIVRPAFTLGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 201 KGMRIAWDDEE----TRDGFRLSSQeaassfgdDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnereCSIQrrN------ 270
Cdd:TIGR01369 176 TGGGIAYNREElkeiAERALSASPI--------NQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNME--Nfdpmgv 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189095269 271 ----QKVVeeAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSK-KNFYFLEMNTRL 328
Cdd:TIGR01369 242 htgdSIVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVNPRV 302
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
637-681 |
1.30e-07 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 53.69 E-value: 1.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 189095269 637 RSPMPGVvvAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTV 681
Cdd:PLN02983 210 RSPAPGE--PPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTI 252
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
642-702 |
2.09e-07 |
|
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: 54.11 E-value: 2.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
636-702 |
5.93e-07 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 47.70 E-value: 5.93e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189095269 636 LRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK07051 6 IVSPLPGTFyrrpspdAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
137-326 |
1.08e-06 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 51.27 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 137 FIGPDTHAiQAMG-DKIESKLLAKKAEVNTIPGfdgVV---KDAEEAV--RIAREIGYPVMIKASaggggkgmriawdde 210
Cdd:PRK01966 110 YVGCGVLA-SALSmDKILTKRLLAAAGIPVAPY---VVltrGDWEEASlaEIEAKLGLPVFVKPA--------------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 211 etRDGfrlssqeaaSSFG--------------------DDRLLIEKFIdNPRHIEIQVLGdkhgnalwlNERECSiqrrn 270
Cdd:PRK01966 171 --NLG---------SSVGiskvkneeelaaaldlafeyDRKVLVEQGI-KGREIECAVLG---------NDPKAS----- 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189095269 271 qkVVEE--APSIFLD-------------------AETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 326
Cdd:PRK01966 225 --VPGEivKPDDFYDyeakyldgsaeliipadlsEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
642-702 |
2.00e-06 |
|
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: 51.03 E-value: 2.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
644-702 |
2.13e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 50.98 E-value: 2.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 644 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
140-255 |
2.52e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 50.93 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 140 PDThaIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRdgfrlS 219
Cdd:PLN02735 694 PDS--IDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK-----T 764
|
90 100 110
....*....|....*....|....*....|....*..
gi 189095269 220 SQEAASSFGDDR-LLIEKFIDNPRHIEIQVLGDKHGN 255
Cdd:PLN02735 765 YLETAVEVDPERpVLVDKYLSDATEIDVDALADSEGN 801
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
636-698 |
3.00e-06 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 45.18 E-value: 3.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189095269 636 LRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 698
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
130-356 |
3.83e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 50.35 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 130 LAAEDVVFIGPDTHAIQAMGDKIESKLLAKKaevNTIP-GFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWD 208
Cdd:PRK12815 108 LEQYGVELLGTNIEAIQKGEDRERFRALMKE---LGEPvPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 209 DEETRDGFRlsSQEAASSFGDdrLLIEKFIDNPRHIEIQVLGDKHGNALWLNERE----CSIQRRNQKVVeeAPSIFL-D 283
Cdd:PRK12815 185 LEELEQLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVCNMEnidpVGIHTGDSIVV--APSQTLtD 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189095269 284 AETRRaMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 356
Cdd:PRK12815 259 DEYQM-LRSASLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTL 331
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
79-327 |
4.05e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.50 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 79 MADEAVcVGPAPTSKSYLnmDAIMEAIKKTRAQAVHPGY----GFLSENKEFarcLAAEDVVFIGPDTHAIQAMGDKIES 154
Cdd:PRK12767 42 FADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRDR---FEEIGVKVLVSSKEVIEICNDKWLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 155 KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG------FRLSSQEAASSFG 228
Cdd:PRK12767 116 YEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKP------------------RDGsasigvFKVNDKEELEFLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 229 DDR--LLIEKFIDNPRhIEIQVLGDKHGNALwlnereCSIQRR---------NQKVVEEAPSIFldaetrramgEQAVAL 297
Cdd:PRK12767 178 EYVpnLIIQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKrievragetSKGVTVKDPELF----------KLAERL 240
|
250 260 270
....*....|....*....|....*....|
gi 189095269 298 ARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 327
Cdd:PRK12767 241 AEALGARGPLNIQCFVTDGE-PYLFEINPR 269
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
185-326 |
4.99e-06 |
|
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: 48.08 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 185 EIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgDDRLLIEKFIDNpRHIEIQVLGDKHGNALWLNER-- 262
Cdd:pfam07478 34 ALGYPVFVKPARLGSSVGVSKVESREELQAAI-----EEAFQY-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvp 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189095269 263 ECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALA----RAVKYSSAGTVEFLVDSKKNFYFLEMNT 326
Cdd:pfam07478 107 SGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELAlkayKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
644-702 |
1.50e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 48.28 E-value: 1.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 644 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK11855 18 VIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
49-256 |
4.27e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.01 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 49 ACRVIRtckKMGIKTVAIHSDV-----DAssvhvKMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG----- 118
Cdd:PRK05294 33 ACKALR---EEGYRVVLVNSNPatimtDP-----EMAD-ATYIEP-------ITPEFVEKIIEKERPDAILPTMGgqtal 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 119 ----FLSENKEFARClaaeDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIka 194
Cdd:PRK05294 97 nlavELAESGVLEKY----GVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVII-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189095269 195 saggggkgmR-----------IAWDDEETRD----GFRLS--SQeaassfgddrLLIEKFIDNPRHIEIQVLGDKHGNA 256
Cdd:PRK05294 169 ---------RpsftlggtgggIAYNEEELEEiverGLDLSpvTE----------VLIEESLLGWKEYEYEVMRDKNDNC 228
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
57-324 |
1.10e-04 |
|
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: 45.07 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 57 KKMGIKTVAIHSDVDASSVHVkmADEAVcVGPaptsksYLNMDAIMEAIKktRAQAVhpgyGFLSEN--KEFARCLAAED 134
Cdd:COG0026 11 KRLGYRVHVLDPDPDSPAAQV--ADEHI-VAD------YDDEEALREFAE--RCDVV----TFEFENvpAEALEALEAEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 135 VVFigPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeeTRD 214
Cdd:COG0026 76 PVR--PGPEALEIAQDRLLEKAFLAELGIPV-APFA-AVDSLEDLEAAIAELGLPAVLKT-----------------RRG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 215 G------FRLSSQE----AASSFGDDRLLIEKFIDNPRhiEIQVLG--DKHGN-ALW---LNerecsIQRRNQKVVEEAP 278
Cdd:COG0026 135 GydgkgqVVIKSAAdleaAWAALGGGPCILEEFVPFER--ELSVIVarSPDGEvATYpvvEN-----VHRNGILDESIAP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 189095269 279 SiFLDAETRRAMGEQAVALARAVKYssAGT--VEFLVDSKKNFYFLEM 324
Cdd:COG0026 208 A-RISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGELLVNEI 252
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
126-349 |
2.08e-04 |
|
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: 43.78 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 126 FARCLAAEDVVFIgPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKasaggggkgmri 205
Cdd:COG0189 73 LLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVLK------------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 206 awddeeTRDG------FRLSSQEAASSF-------GDDRLLIEKFIDNPRHIEIQ--VLGDKHGNALW--LNERECSIQR 268
Cdd:COG0189 138 ------PLDGsggrgvFLVEDEDALESIlealtelGSEPVLVQEFIPEEDGRDIRvlVVGGEPVAAIRriPAEGEFRTNL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 269 RNQKVVEEAPsifLDAETRramgEQAVALARAVKYSSAGtVEFLVDsKKNFYFLEMNtrlqvehpVTECI------TGLD 342
Cdd:COG0189 212 ARGGRAEPVE---LTDEER----ELALRAAPALGLDFAG-VDLIED-DDGPLVLEVN--------VTPGFrgleraTGVD 274
|
....*..
gi 189095269 343 LVQEMIR 349
Cdd:COG0189 275 IAEAIAD 281
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
57-239 |
4.07e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.22 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 57 KKMGIKTVAIhsDVDASSVHVKMADEAVCVgpaptskSYLNMDAIMEAIKktRAQAVhpGYGFlsEN--KEFARCLAAED 134
Cdd:PRK06019 22 APLGYKVIVL--DPDPDSPAAQVADEVIVA-------DYDDVAALRELAE--QCDVI--TYEF--ENvpAEALDALAARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 135 VVFIGPDthAIQAMGDKIESKLLAKKAEVNTiPGFdGVVKDAEEAVRIAREIGYPVMIKasaggggkgmriawddeeTR- 213
Cdd:PRK06019 87 PVPPGPD--ALAIAQDRLTEKQFLDKLGIPV-APF-AVVDSAEDLEAALADLGLPAVLK------------------TRr 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 189095269 214 ---DG---FRLSS----QEAASSFGDDRLLIEKFID 239
Cdd:PRK06019 145 ggyDGkgqWVIRSaedlEAAWALLGSVPCILEEFVP 180
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
642-701 |
5.30e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 43.13 E-value: 5.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 701
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
20-363 |
5.89e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 43.23 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 20 WPPQQLMLSAALRTlkTFDKILVANRGEI----ACRV----IRTCKKM---GIKTVAIHSDVDASSVHVKMADEAVcVGP 88
Cdd:PLN02735 8 TRAWSAATKAGKRT--DLKKIMILGAGPIvigqACEFdysgTQACKALkeeGYEVVLINSNPATIMTDPETADRTY-IAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 89 aptsksyLNMDAIMEAIKKTRAQAVHPGYG---FLSENKEFAR--CLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEV 163
Cdd:PLN02735 85 -------MTPELVEQVIAKERPDALLPTMGgqtALNLAVALAEsgILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 164 NTIPgfDGVVKDAEEAVRIAREIG-YPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSfgddRLLIEKFIDNPR 242
Cdd:PLN02735 158 KTPP--SGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 243 HIEIQVLGDKHGNALWLnereCSIQRRNQKVVEEAPSI-------FLDAETRRaMGEQAVALARAVKYSSAGT-VEFLVD 314
Cdd:PLN02735 232 EYELEVMRDLADNVVII----CSIENIDPMGVHTGDSItvapaqtLTDKEYQR-LRDYSVAIIREIGVECGGSnVQFAVN 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 189095269 315 SKK-NFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADI 363
Cdd:PLN02735 307 PVDgEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDI 356
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
153-194 |
6.79e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 42.80 E-value: 6.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 189095269 153 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKA 194
Cdd:COG1042 492 EAKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
642-698 |
9.71e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 42.24 E-value: 9.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 698
Cdd:PRK14875 17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
153-193 |
1.42e-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: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 189095269 153 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIK 193
Cdd:pfam13549 14 EAKALLAAYGIPVVPT--RLARSPEEAVAAAEEIGYPVVLK 52
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
171-238 |
2.84e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.91 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095269 171 GVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG-------FRLSSQE-------AASSFGDDrLLIEK 236
Cdd:PRK14016 233 RVVTSAEDAWEAAEEIGYPVVVKP------------------LDGnhgrgvtVNITTREeieaayaVASKESSD-VIVER 293
|
..
gi 189095269 237 FI 238
Cdd:PRK14016 294 YI 295
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
642-702 |
3.03e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 3.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
642-702 |
5.39e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 39.99 E-value: 5.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
642-702 |
6.61e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 39.60 E-value: 6.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189095269 642 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 702
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| |
