|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
30-479 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 802.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 350 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 429
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1034584483 430 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 479
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
29-471 |
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 1034584483 29 TFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHP 108
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 109 GYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAS 188
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 189 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 268
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 269 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 348
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 349 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSD 425
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGET 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034584483 426 RTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 471
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
30-489 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 652.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 350 RHKQADIRINGWAVECRVYAEDPyKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 429
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTF-FPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 430 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDvypdgfkgHMLTKSEK 489
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK--------QLVKKSTK 450
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
30-473 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 627.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVdSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 350 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 429
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDF-APSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1034584483 430 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 473
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
30-471 |
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 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 350 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 429
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1034584483 430 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 471
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
30-473 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 567.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 350 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQyqepLHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDR 426
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGF-MPCPGKIEE----LYIPGglgVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034584483 427 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 473
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
27-473 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 566.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 27 EKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVG--PAPtSKSYLNMDAIMEAIKKTRAQ 104
Cdd:PRK12999 2 MKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGegKHP-VRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 105 AVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVM 184
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 185 IKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQ 264
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 265 KVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVA 344
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 345 KGYPLR------HKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQ-PGSDISIYYDPMIS 417
Cdd:PRK12999 321 EGATLHdleigiPSQEDIRLRGYAIQCRITTEDPANNF-MPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLLV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034584483 418 KLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 473
Cdd:PRK12999 399 KLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
28-470 |
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: 556.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 28 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPA--PTsKSYLNMDAIMEAIKKTRAQA 105
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGkgPV-DAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 106 VHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMI 185
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 186 KASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQK 265
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 266 VVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAK 345
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 346 GYPLRHK------QADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSG-IQPGSDISIYYDPMISK 418
Cdd:COG1038 321 GYSLDDPeigipsQEDIRLNGYAIQCRITTEDPANNF-MPDTGRITAYRSAGG-FGIRLDGGnAYTGAVITPYYDSLLVK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034584483 419 LITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKF 470
Cdd:COG1038 399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
30-476 |
2.32e-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: 2.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 348
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 349 LRHKQ--ADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlhlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDR 426
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPAKNF-QPSPGLLTDVQFP---DDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 427 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD-VYP 476
Cdd:TIGR02712 396 EDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSfVYT 446
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
28-471 |
2.88e-177 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 513.53 E-value: 2.88e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 28 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVH 107
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 108 PGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKA 187
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 188 SAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHgNALWLNERECSIQRRNQKVV 267
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 268 EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKG 346
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 347 YPLRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDR 426
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDF-FPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1034584483 427 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 471
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
30-471 |
3.33e-170 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 495.78 E-value: 3.33e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSkSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 189
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 190 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 269
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 350 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 429
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDF-LPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1034584483 430 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 471
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFV 440
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
32-472 |
1.25e-166 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 485.40 E-value: 1.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 32 KILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYG 111
Cdd:PRK08462 6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 112 FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGG 191
Cdd:PRK08462 86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 192 GGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAP 271
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 272 SIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLrH 351
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL-P 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 352 KQADIRINGWAVECRVYAEDPyKSFgLPSIGRLSQYqeplHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTE 428
Cdd:PRK08462 325 SQESIKLKGHAIECRITAEDP-KKF-YPSPGKITKW----IAPGgrnVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1034584483 429 ALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLS 472
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
30-471 |
3.42e-144 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 429.23 E-value: 3.42e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTsKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRI-AREIGYPVMIKAS 188
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 189 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 268
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 269 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 348
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 349 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTE 428
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNF-IPSPGKITEYYPALG-PSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1034584483 429 ALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 471
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYI 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
143-350 |
8.65e-101 |
|
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: 8.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 143 DKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGD 222
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 223 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTV 302
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034584483 303 EFLVDSK-KNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLR 350
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
30-137 |
2.29e-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: 203.10 E-value: 2.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 30 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 109
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1034584483 110 YGFLSENKEFARCLAAEDVVFIGPDTHA 137
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
90-344 |
5.03e-57 |
|
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: 194.32 E-value: 5.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 90 NMDAIMEAIKKTRAQavHPGYGFLSENkEFARCLAAEdVV----FIGPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgV 165
Cdd:COG0439 1 DIDAIIAAAAELARE--TGIDAVLSES-EFAVETAAE-LAeelgLPGPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 166 VKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDk 245
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 246 HGNALWlnereCSIQRRNQK---VVE---EAPSIfLDAETRRAMGEQAVALARAVKYS-SAGTVEFLVDSKKNFYFLEMN 318
Cdd:COG0439 153 DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEIN 226
|
250 260
....*....|....*....|....*...
gi 1034584483 319 TRLQVEH--PVTECITGLDLVQEMIRVA 344
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLA 254
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
364-471 |
1.13e-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: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 364 ECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 443
Cdd:smart00878 1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78
|
90 100
....*....|....*....|....*...
gi 1034584483 444 GVTHNIALLREVIINSRFVKGDISTKFL 471
Cdd:smart00878 79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
364-473 |
3.45e-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: 3.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 364 ECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 443
Cdd:pfam02785 1 EARIYAEDPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIE 78
|
90 100 110
....*....|....*....|....*....|
gi 1034584483 444 GVTHNIALLREVIINSRFVKGDISTKFLSD 473
Cdd:pfam02785 79 GVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| PCC_BT |
pfam18140 |
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ... |
492-620 |
2.05e-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: 130.05 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 492 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 571
Cdd:pfam18140 1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034584483 572 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 620
Cdd:pfam18140 80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
628-694 |
2.28e-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: 2.28e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034584483 628 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
631-695 |
3.46e-21 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 99.06 E-value: 3.46e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034584483 631 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
631-694 |
1.97e-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: 96.69 E-value: 1.97e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034584483 631 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
628-694 |
7.78e-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: 83.80 E-value: 7.78e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034584483 628 VLRSPMPGVVVA-----VSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
628-695 |
2.48e-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: 2.48e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034584483 628 VLRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:COG0511 62 AVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
548-695 |
1.45e-18 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 89.90 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 548 FSVEVDGSKLNV--TSTWNLASPLLSVSVDGTQRTVQclsreaggnmsiqflgtvykvniltrlAAELNKF-MLEKVTED 624
Cdd:PRK09282 468 FKVEVDGEKYEVkiEGVKAEGKRPFYLRVDGMPEEVV---------------------------VEPLKEIvVGGRPRAS 520
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 625 TSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK09282 521 APGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
627-695 |
1.14e-17 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 77.52 E-value: 1.14e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034584483 627 SVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
42-320 |
2.32e-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: 85.70 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 42 ACRVIRtckKMGIKTVAIHS-------DVDassvhvkMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG--- 111
Cdd:COG0458 21 ACKALR---EEGYEVILVNSnpetvstDYD-------TAD-RLYFEP-------LTVEDVLDIIEKEKPDGVIVQFGgqt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 112 ------FLSENKEFarclaaEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIG 180
Cdd:COG0458 83 alnlavELEEAGIL------EGVKILGTSPDAI----DLAEdrelfKELL-DKLGIPQPKS--GTATSVEEALAIAEEIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 181 YPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSsqeaassfGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnere 256
Cdd:COG0458 150 YPVIVRPSYVLGGRGMGIVYNEEEleeyLERALKVS--------PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV---- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034584483 257 CSIQrrNqkvVEEA-----------PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 320
Cdd:COG0458 218 GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
628-692 |
3.74e-17 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 78.32 E-value: 3.74e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034584483 628 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLV 692
Cdd:PRK06549 63 AMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
628-694 |
2.73e-15 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 73.74 E-value: 2.73e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034584483 628 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:PRK05641 86 VVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
45-350 |
2.40e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 76.96 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 45 VIRTCKKMGIKTVAIHSDVDASSVHVKMADeavcvgpaptsKSY---LNMDAIMEAIKKTRAQAVHPGYGFLSENKeFAR 121
Cdd:TIGR01369 580 AVLALRELGYETIMINYNPETVSTDYDTSD-----------RLYfepLTFEDVMNIIELEKPEGVIVQFGGQTPLN-LAK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 122 CLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGM 196
Cdd:TIGR01369 648 ALEEAGVPILGTSPESI----DRAEdrekfSELL-DELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 197 RIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPRHIEIQVLGDkHGNALwlnerECSIQRRnqkvVEEA------ 270
Cdd:TIGR01369 721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVL-----IPGIMEH----IEEAgvhsgd 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 271 -----PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAK 345
Cdd:TIGR01369 787 stcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865
|
....*
gi 1034584483 346 GYPLR 350
Cdd:TIGR01369 866 GKKLE 870
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
631-695 |
2.77e-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: 2.77e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034584483 631 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:TIGR01235 1079 APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
93-319 |
1.92e-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: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 93 AIMEAIKKTRAQAVhpgyGFLSENKEFARCLAAE--DVVFI--------------------------GPDTHAIqAMgDK 144
Cdd:COG1181 23 AVAAALDKAGYDVV----PIGIDVEDLPAALKELkpDVVFPalhgrggedgtiqgllellgipytgsGVLASAL-AM-DK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 145 IESKLLAKKAEVNTIPGFdgVVKDAEEAV--RIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgD 222
Cdd:COG1181 97 ALTKRVLAAAGLPTPPYV--VLRRGELADleAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAAL-----EEAFKY-D 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 223 DRLLIEKFIDnPRHIEIQVLGDKHGNALWLNErecsIQRRN-----------QKVVEEAPSIfLDAETRRAMGEQAVALA 291
Cdd:COG1181 169 DKVLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEELEERIQELALKAF 242
|
250 260
....*....|....*....|....*...
gi 1034584483 292 RAVKYSSAGTVEFLVDSKKNFYFLEMNT 319
Cdd:COG1181 243 RALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
45-321 |
1.40e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 69.96 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 45 VIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVcVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGY----GFLSENKEFA 120
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVV-VVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 121 rclaAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKASaggggkgMRIAW 200
Cdd:COG3919 99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPA-------DSVGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 201 DD---EETRDGFRLSSQEA------ASSFGDDRLLIEKFIDNPRHIEIQVLG--DKHGNALWLnereCSIQRRNQKVVEE 269
Cdd:COG3919 166 DElsfPGKKKVFYVDDREEllallrRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1034584483 270 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRL 321
Cdd:COG3919 242 GNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRF 294
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
631-694 |
3.52e-12 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 69.57 E-value: 3.52e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034584483 631 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:PRK14040 529 APLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
140-319 |
5.27e-12 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 67.44 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 140 AMgDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEaass 219
Cdd:PRK01372 96 AM-DKLRTKLVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 220 fgDDRLLIEKFIDNPrhiEIQ--VLGDKhgnALwlnerecsiqrrnqKVVE-EAPSIF-------------------LDA 277
Cdd:PRK01372 169 --DDEVLVEKYIKGR---ELTvaVLGGK---AL--------------PVIEiVPAGEFydyeakylaggtqyicpagLPA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034584483 278 ETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 319
Cdd:PRK01372 227 EIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
635-694 |
2.47e-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: 2.47e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
635-694 |
2.07e-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: 2.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
633-695 |
2.44e-09 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 60.51 E-value: 2.44e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034584483 633 MPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
635-694 |
5.35e-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: 5.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
120-241 |
5.51e-09 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 59.73 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 120 ARCLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKAS------ 188
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAI----DLAEdrerfSKLL-EKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSyvlggr 718
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034584483 189 AggggkgMRIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPrhIEIQV 241
Cdd:PRK05294 719 A------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGA--IEVDV 759
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
131-346 |
6.89e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 59.21 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 131 IGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEEtrdgfr 210
Cdd:PRK12815 658 LGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA------ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 211 LSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDkhGNALWLN---ERecsiqrrnqkvVEEA-----------PSIFLD 276
Cdd:PRK12815 730 LEAYLAENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiEH-----------IEQAgvhsgdsiavlPPQSLS 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 277 AETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKG 346
Cdd:PRK12815 796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
25-321 |
3.49e-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: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 25 PNEKTFDKILVANRGEI----AC-------RVIRTCKKMGIKTVAIHSDVDASSVHVKMADEaVCVGPaptsksyLNMDA 93
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIvigqAAefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADK-VYIEP-------LTPEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 94 IMEAIKKTRAQAVHPGYG-----FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKD 168
Cdd:TIGR01369 73 VEKIIEKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESE--IAHS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 169 AEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSSQeaassfgdDRLLIEKFIDNPRHIEIQVLGD 244
Cdd:TIGR01369 151 VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREElkeiAERALSASPI--------NQVLVEKSLAGWKEIEYEVMRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 245 KHGNALWLnereCSIQrrN----------QKVVeeAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSK-KNFY 313
Cdd:TIGR01369 223 SNDNCITV----CNME--NfdpmgvhtgdSIVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYY 294
|
....*...
gi 1034584483 314 FLEMNTRL 321
Cdd:TIGR01369 295 VIEVNPRV 302
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
630-674 |
1.28e-07 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 53.69 E-value: 1.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1034584483 630 RSPMPGVvvAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTV 674
Cdd:PLN02983 210 RSPAPGE--PPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTI 252
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
635-695 |
1.45e-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: 54.50 E-value: 1.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
629-695 |
4.97e-07 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 47.70 E-value: 4.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034584483 629 LRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK07051 6 IVSPLPGTFyrrpspdAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
635-695 |
1.44e-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: 51.41 E-value: 1.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
130-319 |
1.47e-06 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 50.89 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 130 FIGPDTHAiQAMG-DKIESKLLAKKAEVNTIPGfdgVV---KDAEEAV--RIAREIGYPVMIKASaggggkgmriawdde 203
Cdd:PRK01966 110 YVGCGVLA-SALSmDKILTKRLLAAAGIPVAPY---VVltrGDWEEASlaEIEAKLGLPVFVKPA--------------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 204 etRDGfrlssqeaaSSFG--------------------DDRLLIEKFIdNPRHIEIQVLGdkhgnalwlNERECSiqrrn 263
Cdd:PRK01966 171 --NLG---------SSVGiskvkneeelaaaldlafeyDRKVLVEQGI-KGREIECAVLG---------NDPKAS----- 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034584483 264 qkVVEE--APSIFLD-------------------AETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 319
Cdd:PRK01966 225 --VPGEivKPDDFYDyeakyldgsaeliipadlsEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
637-695 |
1.62e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 51.36 E-value: 1.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 637 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
133-248 |
2.29e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 51.32 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 133 PDThaIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRdgfrlS 212
Cdd:PLN02735 694 PDS--IDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK-----T 764
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034584483 213 SQEAASSFGDDR-LLIEKFIDNPRHIEIQVLGDKHGN 248
Cdd:PLN02735 765 YLETAVEVDPERpVLVDKYLSDATEIDVDALADSEGN 801
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
629-691 |
3.18e-06 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 45.18 E-value: 3.18e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034584483 629 LRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 691
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
123-349 |
4.29e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 50.35 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 123 LAAEDVVFIGPDTHAIQAMGDKIESKLLAKKaevNTIP-GFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWD 201
Cdd:PRK12815 108 LEQYGVELLGTNIEAIQKGEDRERFRALMKE---LGEPvPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 202 DEETRDGFRlsSQEAASSFGDdrLLIEKFIDNPRHIEIQVLGDKHGNALWLNERE----CSIQRRNQKVVeeAPSIFL-D 276
Cdd:PRK12815 185 LEELEQLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVCNMEnidpVGIHTGDSIVV--APSQTLtD 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034584483 277 AETRRaMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 349
Cdd:PRK12815 259 DEYQM-LRSASLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTL 331
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
178-319 |
4.84e-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: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 178 EIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgDDRLLIEKFIDNpRHIEIQVLGDKHGNALWLNER-- 255
Cdd:pfam07478 34 ALGYPVFVKPARLGSSVGVSKVESREELQAAI-----EEAFQY-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvp 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034584483 256 ECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALA----RAVKYSSAGTVEFLVDSKKNFYFLEMNT 319
Cdd:pfam07478 107 SGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELAlkayKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
72-320 |
5.35e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.11 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 72 MADEAVcVGPAPTSKSYLnmDAIMEAIKKTRAQAVHPGY----GFLSENKEfarCLAAEDVVFIGPDTHAIQAMGDKIES 147
Cdd:PRK12767 42 FADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 148 KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG------FRLSSQEAASSFG 221
Cdd:PRK12767 116 YEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKP------------------RDGsasigvFKVNDKEELEFLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 222 DDR--LLIEKFIDNPRhIEIQVLGDKHGNALwlnereCSIQRR---------NQKVVEEAPSIFldaetrramgEQAVAL 290
Cdd:PRK12767 178 EYVpnLIIQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKrievragetSKGVTVKDPELF----------KLAERL 240
|
250 260 270
....*....|....*....|....*....|
gi 1034584483 291 ARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 320
Cdd:PRK12767 241 AEALGARGPLNIQCFVTDGE-PYLFEINPR 269
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
637-695 |
1.12e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 48.67 E-value: 1.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 637 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK11855 18 VIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
42-249 |
4.63e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.01 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 42 ACRVIRtckKMGIKTVAIHSDV-----DAssvhvKMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG----- 111
Cdd:PRK05294 33 ACKALR---EEGYRVVLVNSNPatimtDP-----EMAD-ATYIEP-------ITPEFVEKIIEKERPDAILPTMGgqtal 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 112 ----FLSENKEFARClaaeDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIka 187
Cdd:PRK05294 97 nlavELAESGVLEKY----GVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVII-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034584483 188 saggggkgmR-----------IAWDDEETRD----GFRLS--SQeaassfgddrLLIEKFIDNPRHIEIQVLGDKHGNA 249
Cdd:PRK05294 169 ---------RpsftlggtgggIAYNEEELEEiverGLDLSpvTE----------VLIEESLLGWKEYEYEVMRDKNDNC 228
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
50-317 |
6.86e-05 |
|
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: 45.45 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 50 KKMGIKTVAIHSDVDASSVHVkmADEAVcVGPaptsksYLNMDAIMEAIKktRAQAVhpgyGFLSEN--KEFARCLAAED 127
Cdd:COG0026 11 KRLGYRVHVLDPDPDSPAAQV--ADEHI-VAD------YDDEEALREFAE--RCDVV----TFEFENvpAEALEALEAEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 128 VVFigPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeeTRD 207
Cdd:COG0026 76 PVR--PGPEALEIAQDRLLEKAFLAELGIPV-APFA-AVDSLEDLEAAIAELGLPAVLKT-----------------RRG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 208 G------FRLSSQE----AASSFGDDRLLIEKFIDNPRhiEIQVLG--DKHGN-ALW---LNerecsIQRRNQKVVEEAP 271
Cdd:COG0026 135 GydgkgqVVIKSAAdleaAWAALGGGPCILEEFVPFER--ELSVIVarSPDGEvATYpvvEN-----VHRNGILDESIAP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034584483 272 SiFLDAETRRAMGEQAVALARAVKYssAGT--VEFLVDSKKNFYFLEM 317
Cdd:COG0026 208 A-RISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGELLVNEI 252
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
119-342 |
1.59e-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: 44.16 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 119 FARCLAAEDVVFIgPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKasaggggkgmri 198
Cdd:COG0189 73 LLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVLK------------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 199 awddeeTRDG------FRLSSQEAASSF-------GDDRLLIEKFIDNPRHIEIQ--VLGDKHGNALW--LNERECSIQR 261
Cdd:COG0189 138 ------PLDGsggrgvFLVEDEDALESIlealtelGSEPVLVQEFIPEEDGRDIRvlVVGGEPVAAIRriPAEGEFRTNL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 262 RNQKVVEEAPsifLDAETRramgEQAVALARAVKYSSAGtVEFLVDsKKNFYFLEMNtrlqvehpVTECI------TGLD 335
Cdd:COG0189 212 ARGGRAEPVE---LTDEER----ELALRAAPALGLDFAG-VDLIED-DDGPLVLEVN--------VTPGFrgleraTGVD 274
|
....*..
gi 1034584483 336 LVQEMIR 342
Cdd:COG0189 275 IAEAIAD 281
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
50-232 |
2.91e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.60 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 50 KKMGIKTVAIhsDVDASSVHVKMADEAVCVgpaptskSYLNMDAIMEAIKktRAQAVhpGYGFlsEN--KEFARCLAAED 127
Cdd:PRK06019 22 APLGYKVIVL--DPDPDSPAAQVADEVIVA-------DYDDVAALRELAE--QCDVI--TYEF--ENvpAEALDALAARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 128 VVFIGPDthAIQAMGDKIESKLLAKKAEVNTiPGFdGVVKDAEEAVRIAREIGYPVMIKasaggggkgmriawddeeTR- 206
Cdd:PRK06019 87 PVPPGPD--ALAIAQDRLTEKQFLDKLGIPV-APF-AVVDSAEDLEAALADLGLPAVLK------------------TRr 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034584483 207 ---DG---FRLSS----QEAASSFGDDRLLIEKFID 232
Cdd:PRK06019 145 ggyDGkgqWVIRSaedlEAAWALLGSVPCILEEFVP 180
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
146-187 |
5.10e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 43.19 E-value: 5.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1034584483 146 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKA 187
Cdd:COG1042 492 EAKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
635-694 |
5.23e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 43.13 E-value: 5.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 694
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
96-356 |
6.83e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 43.23 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 96 EAIKKTRAQAVHPGYG---FLSENKEFAR--CLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPgfDGVVKDAE 170
Cdd:PLN02735 92 QVIAKERPDALLPTMGgqtALNLAVALAEsgILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 171 EAVRIAREIG-YPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSfgddRLLIEKFIDNPRHIEIQVLGDKHGNA 249
Cdd:PLN02735 170 ECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELEVMRDLADNV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 250 LWLnereCSIQRRNQKVVEEAPSI-------FLDAETRRaMGEQAVALARAVKYSSAGT-VEFLVDSKK-NFYFLEMNTR 320
Cdd:PLN02735 246 VII----CSIENIDPMGVHTGDSItvapaqtLTDKEYQR-LRDYSVAIIREIGVECGGSnVQFAVNPVDgEVMIIEMNPR 320
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034584483 321 LQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADI 356
Cdd:PLN02735 321 VSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDI 356
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
635-691 |
7.00e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 42.62 E-value: 7.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 691
Cdd:PRK14875 17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
146-186 |
1.15e-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: 40.92 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1034584483 146 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIK 186
Cdd:pfam13549 14 EAKALLAAYGIPVVPT--RLARSPEEAVAAAEEIGYPVVLK 52
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
164-231 |
2.47e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 41.30 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034584483 164 GVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG-------FRLSSQE-------AASSFGDDrLLIEK 229
Cdd:PRK14016 233 RVVTSAEDAWEAAEEIGYPVVVKP------------------LDGnhgrgvtVNITTREeieaayaVASKESSD-VIVER 293
|
..
gi 1034584483 230 FI 231
Cdd:PRK14016 294 YI 295
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
635-695 |
2.50e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.14 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
635-695 |
4.56e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.37 E-value: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
635-695 |
5.74e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 39.99 E-value: 5.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034584483 635 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 695
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| |
