|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
45-494 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 844.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLStPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLR-PPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQHHKDLLP 494
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLA 450
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
45-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 669.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLStPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYH-PPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
45-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 645.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PLSQEEIPLQGHAFEARIYAEDPdNNFMPGAGPLVHLSTpPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTL-PGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
47-503 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 612.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 47 KVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYG 126
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 127 FLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGG 206
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 207 GGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAP 286
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 287 APGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMdSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPL 366
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 367 SQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTP--PpdmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK08654 323 KQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPggP---GVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIpQHHKDLLPTHSTIAKES 503
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFI-EEETTILEEMKRYALEE 457
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
45-488 |
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: 610.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 124 GYGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:COG1038 84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:COG1038 164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:COG1038 244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 364 -------IPlSQEEIPLQGHAFEARIYAEDPDNNFMPGAGplvhlstpppdmstRIET-------GVR-------QGDEV 422
Cdd:COG1038 324 lddpeigIP-SQEDIRLNGYAIQCRITTEDPANNFMPDTG--------------RITAyrsaggfGIRldggnayTGAVI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57528264 423 SVHYDPMIAKLVVWASDRQSALSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:COG1038 389 TPYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
45-488 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 596.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 124 GYGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK12999 165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 364 I------PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGplvhlstpppdmstRIET-------GVR-------QGDEVS 423
Cdd:PRK12999 325 LhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTG--------------RITAyrspggfGVRldggnafAGAEIT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57528264 424 VHYDPMIAKLVVWASDRQSALSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:PRK12999 391 PYYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDET 455
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
46-485 |
0e+00 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 592.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 46 TKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGY 125
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 126 GFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGyHGNDQSDECLKEHAGKIGYPVMIKAIRG 205
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 206 GGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEA 285
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 286 PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PLSQ--EEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPPpdmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQS 442
Cdd:TIGR02712 321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPD---DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 57528264 443 ALSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFI 485
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-491 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 580.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTpPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYI-PGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQHHKD 491
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLVD 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
45-488 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 569.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLsTPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRY-LPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 534.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPsQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQS-DECLKEhAGKIGYPVMIKAI 203
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADlDEALAE-AERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 364 IPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTP--PpdmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQ 441
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPggP---GVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 57528264 442 SALSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:PRK07178 397 EALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH 443
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-488 |
2.39e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 516.22 E-value: 2.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 365 PlSQEEIPLQGHAFEARIYAEDPdNNFMPGAGPLVHLsTPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK08462 324 P-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKW-IAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 57528264 445 SKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:PRK08462 401 AKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
43-485 |
4.15e-174 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 506.21 E-value: 4.15e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 43 GSITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIH 122
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 123 PGYGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKA 202
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 203 IRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKII 282
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 283 EEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMD-SKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAG 361
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 362 EKIPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPPPDmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQ 441
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGP-GVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 57528264 442 SALSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFI 485
Cdd:PRK12833 401 AALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
45-517 |
5.55e-172 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 501.27 E-value: 5.55e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQqSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHG-NDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 364 IPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLsTPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSA 443
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEY-YPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57528264 444 LSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQHHKDLLPT---HSTIAKESVCQAALGLILKEKE 517
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedRHQENKEEVIAAIAAALKKIRE 476
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
47-488 |
2.99e-165 |
|
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: 505.52 E-value: 2.99e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 47 KVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ---QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 124 GYGFLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 364 IPL------SQEEIPLQGHAFEARIYAEDPDNNFMPGAGPL-VHLSTppPDMSTRIETGVR-QGDEVSVHYDPMIAKLVV 435
Cdd:TIGR01235 321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIeAYRSA--GGFGIRLDGGNSyAGAIITPYYDSLLVKVSA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 57528264 436 WASDRQSALSKLRYSLHQYNIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQH 488
Cdd:TIGR01235 399 WASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
159-365 |
2.91e-89 |
|
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: 278.03 E-value: 2.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 159 KSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDD 238
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 239 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVE 318
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 57528264 319 FIMDSKH-NFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIP 365
Cdd:pfam02786 162 FALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
116-368 |
1.47e-64 |
|
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: 215.12 E-value: 1.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 116 SAAQAIHPGYGF---LSEN----MEFAEFCKQEGIIfiGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLK 188
Cdd:COG0439 7 AAAAELARETGIdavLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEE--AL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 189 EHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHHGNAVYlf 268
Cdd:COG0439 83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVVV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 269 erdCSVQRRHQK---IIE---EAPAPgIDPEVRRRLGEAAVRAAKAVNYV-GAGTVEFIMDSKHNFYFMEMNTRLQVEH- 340
Cdd:COG0439 159 ---CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHi 234
|
250 260
....*....|....*....|....*....
gi 57528264 341 -PVTEMITGTDLVEWQLRIAAGEKIPLSQ 368
Cdd:COG0439 235 pPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
45-152 |
1.03e-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: 204.26 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 57528264 125 YGFLSENMEFAEFCKQEGIIFIGPPSTA 152
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
379-487 |
1.69e-48 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 165.74 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 379 EARIYAEDPDNNFMPGAGPLVHLStPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYSLHQYNIVG 458
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYR-FPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 57528264 459 LRTNVDFLLRLSGHSEFEAGNVHTDFIPQ 487
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
379-485 |
2.22e-46 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 159.89 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 379 EARIYAEDPDNNFMPGAGPLVHLStPPPDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYSLHQYNIVG 458
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYR-FPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 57528264 459 LRTNVDFLLRLSGHSEFEAGNVHTDFI 485
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
647-710 |
5.74e-25 |
|
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: 98.26 E-value: 5.74e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57528264 647 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
159-334 |
9.96e-24 |
|
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: 102.11 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 159 KSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfnDD 238
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 239 AMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVRAAK 307
Cdd:COG1181 170 KVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243
|
170 180
....*....|....*....|....*..
gi 57528264 308 AVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:COG1181 244 ALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
650-710 |
3.91e-19 |
|
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: 82.10 E-value: 3.91e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57528264 650 TGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
634-709 |
2.16e-18 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 82.60 E-value: 2.16e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57528264 634 SPVSAEGTQGGTIAPMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVE 709
Cdd:PRK05641 76 APAPASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
647-700 |
7.75e-18 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 88.21 E-value: 7.75e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 57528264 647 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQ 700
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
162-334 |
1.49e-17 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 84.01 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 162 SKSIMAAAGVPVVEGYHGNdqSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARReakksfNDDAML 241
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLT--REEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 242 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIDPEVRRRLGEAAVRAAK 307
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 57528264 308 AVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
647-700 |
2.27e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 86.73 E-value: 2.27e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 57528264 647 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQ 700
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
628-711 |
2.81e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 85.66 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 628 PVPKYLSPVSAEGTQGGTI-APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAP 706
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 57528264 707 LVEFE 711
Cdd:PRK09282 587 LMEIE 591
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
165-334 |
6.13e-17 |
|
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: 80.05 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 165 IMAAAGVPVV-------EGYHGNDqsDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfnD 237
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWKLNP--KEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 238 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIDPEVRRRLGEAAVRAAKAVN 310
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 57528264 311 YVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
634-711 |
9.51e-17 |
|
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: 77.24 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 634 SPVSAEGTQGGTI-APMTGTI-------EKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHA 705
Cdd:COG0511 51 AAAAAAASGGGAVkSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQ 130
|
....*.
gi 57528264 706 PLVEFE 711
Cdd:COG0511 131 PLFVIE 136
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
159-334 |
1.09e-15 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 79.01 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 159 KSTSKSIMAAAGVPVVEGY--HGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfn 236
Cdd:PRK01966 124 KILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 237 DDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIDPEVRRRL 298
Cdd:PRK01966 198 DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKI 263
|
170 180 190
....*....|....*....|....*....|....*.
gi 57528264 299 GEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:PRK01966 264 RELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
127-365 |
2.79e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 75.35 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 127 FLSENMEfaEFckQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRG- 205
Cdd:COG3919 90 LLSRHRD--EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 206 -------GGGKGMRIIRSEKEFQEQLESARREakksfnDDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcsVQR 276
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF-----TGR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 277 RHQkiieEAPAPG-----IDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FYFMEMNTRL--QVEHPVtemITG 348
Cdd:COG3919 233 KLR----HYPPAGgnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRFwrSLYLAT---AAG 305
|
250
....*....|....*..
gi 57528264 349 TDLVEWQLRIAAGEKIP 365
Cdd:COG3919 306 VNFPYLLYDDAVGRPLE 322
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
626-698 |
6.77e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 74.97 E-value: 6.77e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57528264 626 GIPVPKYLSPVSAEGTQGGTI-APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEG 698
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
130-319 |
8.58e-13 |
|
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: 70.10 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 130 ENM--EFAEFCKQEGIIFigPPSTAIR---DmgiKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIR 204
Cdd:COG0026 61 ENVpaEALEALEAEVPVR--PGPEALEiaqD---RLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 205 GG-GGKGMRIIRSEKEFQEqlesarreAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkI 281
Cdd:COG0026 134 GGyDGKGQVVIKSAADLEA--------AWAALGGGPCILEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--I 200
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 57528264 282 IEE--APApGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEF 319
Cdd:COG0026 201 LDEsiAPA-RISEALAAEAEEIAKRIAEALDYVGVLAVEF 239
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
647-710 |
1.49e-12 |
|
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: 63.39 E-value: 1.49e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57528264 647 APMTGT-----IEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
165-364 |
4.07e-12 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 70.00 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 165 IMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESArreakkSFNDDAMLIEK 244
Cdd:PRK12815 677 LLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN------ASQLYPILIDQ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 245 FVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVN 310
Cdd:PRK12815 749 FIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLG 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57528264 311 YVGAGTVEFIMDSKhNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK12815 815 FRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
182-364 |
7.40e-12 |
|
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: 68.87 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 182 QSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHH 261
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 262 GNAVY-LFErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSkHNFYF 329
Cdd:TIGR01369 767 EVLIPgIME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYV 834
|
170 180 190
....*....|....*....|....*....|....*
gi 57528264 330 MEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:TIGR01369 835 IEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
132-333 |
1.58e-11 |
|
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: 65.73 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 132 MEFAEFCKQEGIIFIGPPStAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGM 211
Cdd:COG0189 71 LALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 212 RIIRSEKEFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFER-----DCSVQRRHQKIIEE 284
Cdd:COG0189 148 FLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRipaegEFRTNLARGGRAEP 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57528264 285 APapgIDPEVRrrlgEAAVRAAKAV--NYVGagtVEFIMDsKHNFYFMEMN 333
Cdd:COG0189 220 VE---LTDEER----ELALRAAPALglDFAG---VDLIED-DDGPLVLEVN 259
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
606-708 |
4.01e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 60.98 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 606 KF-ILLDNTIYLFSME---GSIEVGIPVPKYLSPVSAEGTQGGTI-----------------APMTGTIEKVFVKAGDRV 664
Cdd:PRK06549 4 KFkITIDGKEYLVEMEeigAPAQAAAPAQPASTPVPVPTEASPQVeaqapqpaaaagadampSPMPGTILKVLVAVGDQV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 57528264 665 KAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLV 708
Cdd:PRK06549 84 TENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
163-335 |
2.12e-10 |
|
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: 63.74 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 163 KSIMAAAGVPVVEGYHGNDQsDECLKEhAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLEsarrEAKKSFNDDAMLI 242
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSV-EEALAI-AEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLE----RALKVSPDHPVLI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 243 EKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNY 311
Cdd:COG0458 193 DESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGV 263
|
170 180
....*....|....*....|....
gi 57528264 312 VGAGTVEFIMDSKhNFYFMEMNTR 335
Cdd:COG0458 264 VGLCNIQFAVDDG-RVYVIEVNPR 286
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
163-319 |
5.90e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 61.71 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 163 KSIMAAAGVPVVEgYHG-NDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEFQEqlesarreAKKSFNDDAM 240
Cdd:PRK06019 105 KQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEA--------AWALLGSVPC 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 241 LIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVRAAKAVNYVGAGTVE 318
Cdd:PRK06019 174 ILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEEIASRIAEELDYVGVLAVE 249
|
.
gi 57528264 319 F 319
Cdd:PRK06019 250 F 250
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
167-319 |
1.15e-09 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 58.03 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 167 AAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEkefqEQLESARREAKksfnDDAMLIEKF 245
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57528264 246 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIDPEVRRRLGEAAVRAAKAVNYVGAGTVEF 319
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
147-452 |
2.90e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 60.63 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 147 GPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLES 226
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 227 ARREAKKSFnddamLIEKFVDTPRHvEVQVFGDHHGNAVYlferdcSVQRRHQ-------KIIEEAPAPgIDPEVRRRLG 299
Cdd:PRK02186 174 LRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVL------GITRKHLgppphfvEIGHDFPAP-LSAPQRERIV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 300 EAAVRAAKAVNY-VGAGTVEFIMdSKHNFYFMEMNTRLQVEH-PVT-EMITGTDLVEWQLRIAAGE-------------- 362
Cdd:PRK02186 241 RTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEINPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVaafadptakrygai 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 363 KIPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPlVHLSTPPPDMSTRIETGVRQGDE---VSVHYDPMIAKLVV---- 435
Cdd:PRK02186 320 RFVLPARSGVLRGLLFLPDDIAARPELRFHPLKQP-GDALRLEGDFRDRIAAVVCAGDHrdsVAAAAERAVAGLSIdigd 398
|
330 340
....*....|....*....|
gi 57528264 436 ---WASDRQSALSKLRYSLH 452
Cdd:PRK02186 399 aarAAALNDAGAGAARPGLP 418
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
646-711 |
5.31e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 53.25 E-value: 5.31e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57528264 646 IAPMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 711
Cdd:PRK08225 5 YASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
87-365 |
3.19e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 56.05 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 87 MADEAYSIgpaPSQQSYLAMEKIIQVAKSSAAQAIHPGY----GFLSENMEfaEFcKQEGIIFIGPPSTAIRDMGIKSTS 162
Cdd:PRK12767 42 FADKFYVV---PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQNRD--RF-EEIGVKVLVSSKEVIEICNDKWLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 163 KSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKKsfnddaMLI 242
Cdd:PRK12767 116 YEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LII 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 243 EKFVDTPRhVEVQVFGDHHGNAVylferdCSVQRRHQKIIEEAPAPGI---DPEVRrrlgEAAVRAAKAVNYVGAGTVEF 319
Cdd:PRK12767 186 QEFIEGQE-YTVDVLCDLNGEVI------SIVPRKRIEVRAGETSKGVtvkDPELF----KLAERLAEALGARGPLNIQC 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 57528264 320 IMDSKhNFYFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIAAGEKIP 365
Cdd:PRK12767 255 FVTDG-EPYLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGGENE 298
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
163-246 |
3.17e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 53.62 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 163 KSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRI-IRSEkefqEQLESARREAKKSFNDdaML 241
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAED--AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD--VI 290
|
....*
gi 57528264 242 IEKFV 246
Cdd:PRK14016 291 VERYI 295
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
651-710 |
6.70e-07 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 47.37 E-value: 6.70e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57528264 651 GTIEKVFVKAGDRVKAGDALMVMIAMK--MEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
87-336 |
7.39e-06 |
|
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: 49.61 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 87 MADEAYsIGPAPSQqsylAMEKIIQVAKssaAQAIHPGYG-----FLSENMEFAEFCKQEGIIFIGPPSTAIRDMGIKST 161
Cdd:TIGR01369 59 MADKVY-IEPLTPE----AVEKIIEKER---PDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDREL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 162 SKSIMAAAGVPVVEGYHGNDQsDECLkEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKsfndDAML 241
Cdd:TIGR01369 131 FREAMKEIGEPVPESEIAHSV-EEAL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 242 IEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQR-----RHQ-KIIEEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:TIGR01369 205 VEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGC 280
|
250 260
....*....|....*....|..
gi 57528264 316 TVEFIMDSK-HNFYFMEMNTRL 336
Cdd:TIGR01369 281 NVQFALNPDsGRYYVIEVNPRV 302
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
634-711 |
7.97e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 49.33 E-value: 7.97e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57528264 634 SPVSAEGTQGGTIAPMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 711
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
135-371 |
1.74e-05 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 47.70 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 135 AEFCKQEGI--IFIGP--P-----STAIRDMGI---------------KSTSKSIMAAAGVPVVEgYHGNDQSDEClKEH 190
Cdd:COG0151 55 VAFAKEENIdlVVVGPeaPlvagiVDAFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAA-YRVFTDLEEA-LAY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 191 AGKIGYPVMIKAIRGGGGKGMRIIRSEKEfqeqlesARREAKKSFNDDAM-------LIEKFVDTPRhVEVQVFGDhhGN 263
Cdd:COG0151 133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLEGEE-ASLFALTD--GK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 264 AVYLFE--RDcsvqrrHqKIIEE-------------APAPGIDPEVRRRLGEAAVR------AAKAVNYVG---AGtvef 319
Cdd:COG0151 203 TVLPLPtaQD------H-KRAGDgdtgpntggmgaySPAPVVTEELLEKIMEEIIEptvagmAAEGIPYRGvlyAG---- 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 57528264 320 IMDSKHNFYFMEMNTRL-----QVehpVTEMITgTDLVEWQLRIAAGEkipLSQEEI 371
Cdd:COG0151 272 LMITADGPKVLEFNVRFgdpetQV---VLPRLE-SDLLELLLAAAEGR---LDEVEL 321
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
191-364 |
6.65e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.24 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 191 AGKIGYPVMIkaiRGG---GGKGMRIIRSEKEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNAVYL 267
Cdd:PRK05294 700 AEEIGYPVLV---RPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLI 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 268 ---FErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKhNFYFMEMN 333
Cdd:PRK05294 771 ggiME--------H---IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDD-EVYVIEVN 838
|
170 180 190
....*....|....*....|....*....|.
gi 57528264 334 TRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK05294 839 PRASRTVPFVSKATGVPLAKIAARVMLGKKL 869
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
651-714 |
1.02e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.58 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57528264 651 GTIEKVFVKAGDRVKAGDALM-VMI--AMkMEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEE 714
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
148-315 |
1.90e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 44.67 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 148 PPSTAIRDMGIKSTSKSIMAAAGVPVVEgyHGNDQSDECLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEfqeqLES 226
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPE--FMEIDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEED----LSS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 227 ArrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV-Y-LFErdcSVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVR 304
Cdd:PLN02948 185 A--VAALGGFERGLYAEKWAPFVKELAVMVARSRDGSTRcYpVVE---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEK 258
|
170
....*....|.
gi 57528264 305 AAKAVNyvGAG 315
Cdd:PLN02948 259 AVGSLE--GAG 267
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
651-711 |
2.91e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 44.04 E-value: 2.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57528264 651 GTIEKVFVKAGDRVKAGDALM-VMI--AMkMEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 711
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
159-351 |
3.39e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 42.10 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 159 KSTSKSIMAAAGVPV-VEGYHGNDQSDECLKEHAGKiGYPVMIKAIRGGGGKGMRIIRSEKEFqEQLESARREAkksfnd 237
Cdd:pfam08443 4 KAKSHQLLAKHGIGPpNTRLAWYPEDAEQFIEQIKR-QFPVIVKSIYGSQGIGVFLAEDEQKL-RQTLSATNEQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 238 daMLIEKFVDTP--RHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPApGIDPEVRrrlgEAAVRAAKAVNYVGAG 315
Cdd:pfam08443 76 --ILVQEFIAEAnnEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKY-QLSQEET----ELAIKAAQAMQLDVAG 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 57528264 316 tVEfIMDSKHNFYFMEMNTRLQVEHpvTEMITGTDL 351
Cdd:pfam08443 149 -VD-LLRQKRGLLVCEVNSSPGLEG--IEKTLGINI 180
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
648-707 |
3.83e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 42.90 E-value: 3.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57528264 648 PMTGTI-------EKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPL 707
Cdd:PLN02983 203 PMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPL 269
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
635-673 |
5.73e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 5.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 57528264 635 PVSAEGTQGGTI----APMTGTIEKVFVKAGDRVKAGDALMVM 673
Cdd:COG1566 34 PVTADGRVEARVvtvaAKVSGRVTEVLVKEGDRVKKGQVLARL 76
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
191-372 |
1.03e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 191 AGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYlfer 270
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVVI---- 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 271 dCSVQRRhqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVE 339
Cdd:PLN02735 805 -GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPRASRT 879
|
170 180 190
....*....|....*....|....*....|....*.
gi 57528264 340 HPVTEMITGTDLVEWQLRIAAGEKIP---LSQEEIP 372
Cdd:PLN02735 880 VPFVSKAIGHPLAKYASLVMSGKSLKdlgFTEEVIP 915
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
645-673 |
1.55e-03 |
|
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: 41.99 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|
gi 57528264 645 TI-APMTGTIEKVFVKAGDRVKAGDALMVM 673
Cdd:COG1038 1115 TItAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
647-698 |
2.65e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.10 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 57528264 647 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEG 698
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
647-673 |
2.94e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 2.94e-03
10 20
....*....|....*....|....*..
gi 57528264 647 APMTGTIEKVFVKAGDRVKAGDALMVM 673
Cdd:PRK12999 1118 APVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
647-673 |
3.15e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 3.15e-03
10 20
....*....|....*....|....*..
gi 57528264 647 APMTGTIEKVFVKAGDRVKAGDALMVM 673
Cdd:COG0845 28 ARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
191-334 |
3.69e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 40.04 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 191 AGKIGYPVMIKAIRGGGGKGMRIIRSekefQEQLESARREAKKSfndDAMLIEKFVdTPRHVEVQVFGDHHGNAVYLFER 270
Cdd:PRK14569 126 EDEISFPVAVKPSSGGSSIATFKVKS----IQELKHAYEEASKY---GEVMIEQWV-TGKEITVAIVNDEVYSSVWIEPQ 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57528264 271 DCSVQRRHQ---KIIEEAPApGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:PRK14569 198 NEFYDYESKysgKSIYHSPS-GLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINS 263
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
187-247 |
4.90e-03 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 39.72 E-value: 4.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57528264 187 LKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKKS--FNDDAMLIEKFVD 247
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
645-673 |
8.83e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 34.73 E-value: 8.83e-03
10 20 30
....*....|....*....|....*....|
gi 57528264 645 TIAPMT-GTIEKVFVKAGDRVKAGDALMVM 673
Cdd:pfam13533 4 KIASPVsGKVVAVNVKEGQQVKKGDVLATL 33
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
194-267 |
9.64e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 37.65 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528264 194 IGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 265
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 57528264 266 YL 267
Cdd:pfam13535 80 IL 81
|
|
| |
