|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
11-466 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 846.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 170
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 250
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 331 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 410
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 767927177 411 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAA 466
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEE 456
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
11-454 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 679.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 170
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 250
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 331 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 410
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 767927177 411 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 454
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
11-457 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 644.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 170
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 250
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 331 PLSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHLSTPRAdPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 410
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 767927177 411 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQ 457
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVK 446
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
9-454 |
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: 620.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 9 RNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLSMEKIIQVAKTSAAQAI 87
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 88 HPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIK 167
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 168 AVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKI 247
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 248 IEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAG 327
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 328 EK-------IPlSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhlstpradpstRIET-------GVR-------QGD 386
Cdd:COG1038 322 YSlddpeigIP-SQEDIRLNGYAIQCRITTEDPANNFMPDTG--------------RITAyrsaggfGIRldggnayTGA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927177 387 EVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 454
Cdd:COG1038 387 VITPYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
13-456 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 615.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 13 KVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCG 92
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 93 FLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGG 172
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 173 GGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAP 252
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 253 APGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMdSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPL 332
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 333 SQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTK 412
Cdd:PRK08654 323 KQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 767927177 413 LRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHK 456
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETT 445
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
9-465 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 601.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 9 RNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLSMEKIIQVAKTSAAQAI 87
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 88 HPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIK 167
Cdd:PRK12999 83 HPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 168 AVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKI 247
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 248 IEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAG 327
Cdd:PRK12999 243 VEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 328 EKI------PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhlstpradpstRIET-------GVR-------QGDE 387
Cdd:PRK12999 323 ATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTG--------------RITAyrspggfGVRldggnafAGAE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927177 388 VSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQhHKQLLLSRKAA 465
Cdd:PRK12999 389 ITPYYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE-TPELFDFPKRR 465
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
12-451 |
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: 589.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 12 TKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGC 91
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 92 GFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGyHGEDQSDQCLKEHARRIGYPVMIKAVRG 171
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 172 GGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEA 251
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 252 PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 331 PLSQ--EEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRAdpsTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQA 408
Cdd:TIGR02712 321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDD---VRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 767927177 409 ALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 451
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
11-456 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 577.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 170
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 250
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 331 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 410
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIP-GGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 767927177 411 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHK 456
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
11-454 |
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: 570.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 170
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 250
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 331 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 410
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPP-GGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 767927177 411 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 454
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
11-463 |
2.39e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 521.20 E-value: 2.39e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPsQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQS-DQCLKEhARRIGYPVMIKAV 169
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADlDEALAE-AERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 170 RGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 249
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 250 EAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 329
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 330 IPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAA 409
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 767927177 410 LTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRK 463
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIK 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
11-451 |
1.53e-175 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 508.91 E-value: 1.53e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 170
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKIIEE 250
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMD-SKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 329
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 330 IPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRAdPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAA 409
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQG-PGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767927177 410 LTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 451
Cdd:PRK12833 403 LARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
9-454 |
7.97e-175 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 506.20 E-value: 7.97e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 9 RNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIH 88
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 89 PGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKA 168
Cdd:PRK08462 82 PGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 169 VRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKII 248
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 249 EEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGE 328
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 329 KIPlSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQA 408
Cdd:PRK08462 322 ELP-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAP-GGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 767927177 409 ALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 454
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
11-459 |
1.62e-168 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 491.25 E-value: 1.62e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQqSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHG-EDQSDQCLKEHARRIGYPVMIKAV 169
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 170 RGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 249
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 250 EAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 329
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 330 IPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLsTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAA 409
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEY-YPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 767927177 410 LTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLL 459
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELL 449
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
13-454 |
5.33e-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: 503.98 E-value: 5.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 13 KVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQ---QSYLSMEKIIQVAKTSAAQAIHP 89
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 90 GCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAV 169
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 170 RGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 249
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 250 EAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 329
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 330 IPL------SQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADpSTRIETGVR-QGDEVSVHYDPMIAKLVVW 402
Cdd:TIGR01235 321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGF-GIRLDGGNSyAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 767927177 403 AADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 454
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
125-331 |
3.54e-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: 277.26 E-value: 3.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 125 KSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDD 204
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 205 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVE 284
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767927177 285 FIMDSKH-NFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIP 331
Cdd:pfam02786 162 FALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-334 |
5.28e-67 |
|
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: 220.90 E-value: 5.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 72 MEKIIQVAKTSAAQaiHPGCGFLSEN----MEFAELCKQEGIIfiGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGED 147
Cdd:COG0439 2 IDAIIAAAAELARE--TGIDAVLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 148 QSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHH 227
Cdd:COG0439 78 PEE--ALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 228 GNAVYlferdCSVQRRHQK---IIE---EAPAPgIKSEVRKKLGEAAVRAAKAVNYV-GAGTVEFIMDSKHNFCFMEMNT 300
Cdd:COG0439 154 GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINA 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 767927177 301 RLQVEH--PVTEMITGTDLVEWQLRIAAGEKIPLSQ 334
Cdd:COG0439 228 RLGGEHipPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
11-118 |
1.99e-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: 1.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 90
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 767927177 91 CGFLSENMEFAELCKQEGIIFIGPPPSA 118
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
345-451 |
2.66e-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: 167.59 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 345 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 424
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 767927177 425 LHTNIDFLLNLSGHPEFEAGNVHTDFI 451
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
345-453 |
2.90e-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: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 345 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 424
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 767927177 425 LHTNIDFLLNLSGHPEFEAGNVHTDFIPQ 453
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
613-676 |
2.46e-24 |
|
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: 96.33 E-value: 2.46e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 676
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
610-676 |
3.24e-23 |
|
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: 93.66 E-value: 3.24e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927177 610 GPLAPM------TGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 676
Cdd:cd06663 1 TILIPDlaqhlgDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
125-300 |
3.70e-22 |
|
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: 97.48 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 125 KSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnDD 204
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 205 AMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAK 273
Cdd:COG1181 170 KVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243
|
170 180
....*....|....*....|....*..
gi 767927177 274 AVNYVGAGTVEFIMDSKHNFCFMEMNT 300
Cdd:COG1181 244 ALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
594-675 |
4.83e-19 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 84.53 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 594 PVPKYLSSVSSQETQGGP---LAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 670
Cdd:PRK05641 67 PTPVAPAAPAPAPASAGEnvvTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
....*
gi 767927177 671 TPLVE 675
Cdd:PRK05641 147 QPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
613-666 |
1.45e-17 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 87.44 E-value: 1.45e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 666
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
594-677 |
1.71e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 86.43 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 594 PVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTP 672
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 767927177 673 LVEFE 677
Cdd:PRK09282 587 LMEIE 591
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
613-666 |
3.50e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 85.96 E-value: 3.50e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 666
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
131-300 |
2.37e-16 |
|
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: 78.13 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 131 IMAAAGVPVV-------EGYHgEDQSDQCLKEHARrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnD 203
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWK-LNPKEWCAQVEEA-LGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 204 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIKSEVRKKLGEAAVRAAKAVN 276
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 767927177 277 YVGAGTVEFIMDSKHNFCFMEMNT 300
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
93-331 |
5.44e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 80.36 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 93 FLSENMEfaELckQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRG- 171
Cdd:COG3919 90 LLSRHRD--EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 172 -------GGGKGMRIVRSEQEFQEQLESARREakksfnDDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcsVQR 242
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF-----TGR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 243 RHQkiieEAPAPG-----IKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRL--QVEHPVtemITG 314
Cdd:COG3919 233 KLR----HYPPAGgnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRFwrSLYLAT---AAG 305
|
250
....*....|....*..
gi 767927177 315 TDLVEWQLRIAAGEKIP 331
Cdd:COG3919 306 VNFPYLLYDDAVGRPLE 322
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
128-300 |
1.44e-15 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 77.84 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 128 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHarRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARReakksfNDDAML 207
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLTREEDLLAAID--KLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 208 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIKSEVRKKLGEAAVRAAK 273
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 767927177 274 AVNYVGAGTVEFIMDSKHNFCFMEMNT 300
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
613-677 |
1.32e-14 |
|
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: 71.08 E-value: 1.32e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927177 613 APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 677
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
613-676 |
1.79e-14 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 68.78 E-value: 1.79e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927177 613 APMTGT-----IEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 676
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
592-664 |
2.49e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 76.51 E-value: 2.49e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927177 592 DIPVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 664
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
125-300 |
4.30e-14 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 74.00 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 125 KSTSKSIMAAAGVPVVEGY--HGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfn 202
Cdd:PRK01966 124 KILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 203 DDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIKSEVRKKL 264
Cdd:PRK01966 198 DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKI 263
|
170 180 190
....*....|....*....|....*....|....*.
gi 767927177 265 GEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNT 300
Cdd:PRK01966 264 RELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
114-285 |
3.89e-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: 71.26 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 114 PPPSAIR---DmgiKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQeq 189
Cdd:COG0026 79 PGPEALEiaqD---RLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 190 lesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkIIEE--APApGIKSEVRKKLG 265
Cdd:COG0026 152 ------AAWAALGGGPCILEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--ILDEsiAPA-RISEALAAEAE 219
|
170 180
....*....|....*....|
gi 767927177 266 EAAVRAAKAVNYVGAGTVEF 285
Cdd:COG0026 220 EIAKRIAEALDYVGVLAVEF 239
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
25-299 |
3.41e-12 |
|
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: 67.66 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 25 RVMRTAKKLGVQTVavyseadrnsmHVDMADEAYSIGPAPSqqsylsmekIIQVAKTSAAQAIHPGCGFLSENMEFAELC 104
Cdd:COG0189 18 ALIEAAQRRGHEVE-----------VIDPDDLTLDLGRAPE---------LYRGEDLSEFDAVLPRIDPPFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 105 KQEGIIFIgPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQ 184
Cdd:COG0189 78 EAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 185 EFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFERDcsVQRRHQKIIEEAPAPGIKSEVRK 262
Cdd:COG0189 155 ALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRI--PAEGEFRTNLARGGRAEPVELTD 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 767927177 263 KLGEAAVRAAKAV--NYVGagtVEFIMDsKHNFCFMEMN 299
Cdd:COG0189 225 EERELALRAAPALglDFAG---VDLIED-DDGPLVLEVN 259
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
29-330 |
1.77e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 67.69 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 29 TAKKLGVQTVAVYSEADRNSMHVDMADEAYsIGPapsqqsyLSMEKIIQVAKT----------SAAQAIHpgcgfLSENM 98
Cdd:PRK12815 584 ALKKEGYETIMINNNPETVSTDYDTADRLY-FEP-------LTLEDVLNVAEAenikgvivqfGGQTAIN-----LAKGL 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 99 EFAelckqeGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMR 178
Cdd:PRK12815 651 EEA------GLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMA 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 179 IVRSEQEFQEQLESArreakkSFNDDAMLIEKFVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA---- 251
Cdd:PRK12815 723 VVYDEPALEAYLAEN------ASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhs 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 252 -------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKhNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 324
Cdd:PRK12815 783 gdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861
|
....*.
gi 767927177 325 AAGEKI 330
Cdd:PRK12815 862 LLGKSL 867
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
78-417 |
2.02e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 67.56 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 78 VAKTSAAQAIH------PGCGFLSENMEF-----AELCKQEGIIfiGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGE 146
Cdd:PRK02186 52 SADTSDPDRIHrfvsslDGVAGIMSSSEYfievaSEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 147 DQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFnddamLIEKFVDTPRHvEVQVFGDH 226
Cdd:PRK02186 130 LRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 227 HGNAVYlferdcSVQRRHQ-------KIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNY-VGAGTVEFIMdSKHNFCFMEM 298
Cdd:PRK02186 202 RGHQVL------GITRKHLgppphfvEIGHDFPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 299 NTRLQVEH-PVT-EMITGTDLVEWQLRIAAGE--------------KIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAG 362
Cdd:PRK02186 274 NPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVaafadptakrygaiRFVLPARSGVLRGLLFLPDDIAARPELRFHPLKQ 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927177 363 PlVHLSTPRADPSTRIETGVRQGDE---VSVHYDPMIAKLVV-------WAADRQAALTKLRYSL 417
Cdd:PRK02186 354 P-GDALRLEGDFRDRIAAVVCAGDHrdsVAAAAERAVAGLSIdigdaarAAALNDAGAGAARPGL 417
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
98-289 |
9.77e-11 |
|
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: 64.90 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 98 MEFAELCKQEGIIFIGPPPSAI-----RDMgikstSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKA--VR 170
Cdd:COG0458 88 VELEEAGILEGVKILGTSPDAIdlaedREL-----FKELLDKLGIPQPKSGTATSVEE--ALAIAEEIGYPVIVRPsyVL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 171 GGggKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEE 250
Cdd:COG0458 161 GG--RGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767927177 251 A-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDS 289
Cdd:COG0458 226 AgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD 275
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
133-285 |
1.20e-10 |
|
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: 60.73 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 133 AAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEqefqEQLESARREAKksfnDDAMLIEKF 211
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927177 212 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 285
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
114-285 |
2.59e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 62.86 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 114 PPPSAIR---DmgiKSTSKSIMAAAGVPVVEgYHG-EDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQe 188
Cdd:PRK06019 90 PGPDALAiaqD---RLTEKQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 189 qlesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGE 266
Cdd:PRK06019 163 -------AAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEE 231
|
170
....*....|....*....
gi 767927177 267 AAVRAAKAVNYVGAGTVEF 285
Cdd:PRK06019 232 IASRIAEELDYVGVLAVEF 250
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
613-677 |
2.99e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 56.72 E-value: 2.99e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 677
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
613-674 |
3.59e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 58.28 E-value: 3.59e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLV 674
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
154-330 |
4.06e-10 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 63.09 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 154 KEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY- 232
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPg 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 233 LFErdcsvqrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSkHNFCFMEMNTR 301
Cdd:TIGR01369 773 IME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPR 840
|
170 180
....*....|....*....|....*....
gi 767927177 302 LQVEHPVTEMITGTDLVEWQLRIAAGEKI 330
Cdd:TIGR01369 841 ASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
115-319 |
2.43e-09 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 58.90 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 115 PPSAIRDMGIKSTSKSIMAAAGVPVVEG--YHGEDQSDQCLKEharrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLES 192
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTglAGSPEEALKLIEE----IGFPVVLKPVFGSWGRGVSLARDRQAAESLLEH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 193 ARREAKKSfndDAMLIEKFVDTPRHVEVQVF--GDHHGNAVYL-----FERDCSVQRRHQKIieeapapgiksEVRKKLG 265
Cdd:TIGR00768 155 FEQLNGPQ---NLFLVQEYIKKPGGRDIRVFvvGDEVVAAIYRitsghWRSNLARGGKAEPC-----------SLTEEIE 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767927177 266 EAAVRAAKAVNyVGAGTVEFIMdSKHNFCFMEMNTRLQVEHpvTEMITGTDLVE 319
Cdd:TIGR00768 221 ELAIKAAKALG-LDVAGVDLLE-SEDGLLVNEVNANPEFKN--SVKTTGVNIAG 270
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
591-676 |
2.90e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 53.95 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 591 IDIPVPKYLSSVSSqetqggplapmtGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 670
Cdd:cd06849 1 TEIKMPDLGESMTE------------GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVG 68
|
....*.
gi 767927177 671 TPLVEF 676
Cdd:cd06849 69 QVIAVI 74
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
53-331 |
4.06e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 58.74 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 53 MADEAYsIGPAPSQQSYLsmEKIIQVAKTSAAQAIHPG----CGFLSENM-EFAElckqEGIIFIGPPPSAIRDMGIKST 127
Cdd:PRK12767 42 FADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLidpeLPLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKWL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 128 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKsfnddaML 207
Cdd:PRK12767 115 TYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 208 IEKFVDTPRhVEVQVFGDHHGNAVYLFERdcsvqRRHQKIIEEApapgIKSEVRK--KLGEAAVRAAKAVNYVGAGTVEF 285
Cdd:PRK12767 185 IQEFIEGQE-YTVDVLCDLNGEVISIVPR-----KRIEVRAGET----SKGVTVKdpELFKLAERLAEALGARGPLNIQC 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767927177 286 IMDSKhNFCFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIAAGEKIP 331
Cdd:PRK12767 255 FVTDG-EPYLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGGENE 298
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
615-687 |
1.26e-07 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 54.41 E-value: 1.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927177 615 MT-GTIEKVFVKAGDKVKAGDSLMVM----IAMKMEhtikSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE 687
Cdd:PRK11856 14 MTeGEIVEWLVKVGDTVKEGQPLAEVetdkATVEIP----SPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAA 87
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
129-212 |
2.16e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 54.39 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 129 KSIMAAAGVPVVEGY--HGEDQsdqcLKEHARRIGYPVMIKAVRGGGGKGMRI-VRSEqefqEQLESARREAKKSFNDda 205
Cdd:PRK14016 219 KRLLAAAGVPVPEGRvvTSAED----AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD-- 288
|
....*..
gi 767927177 206 MLIEKFV 212
Cdd:PRK14016 289 VIVERYI 295
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
617-676 |
2.35e-07 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 48.52 E-value: 2.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927177 617 GTIEKVFVKAGDKVKAGDSLMVMIAMK--MEhtIKSPKDGTVKKVFYREGAQANRHTPLVEF 676
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
617-681 |
4.31e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 52.90 E-value: 4.31e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927177 617 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 681
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
617-680 |
1.07e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 51.75 E-value: 1.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927177 617 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEE 680
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
594-673 |
1.19e-06 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 50.61 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 594 PVPKYLSSVSSQETqggPL-APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGA 665
Cdd:PLN02983 185 ASPPPAKAPKSSHP---PLkSPMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGK 261
|
....*...
gi 767927177 666 QANRHTPL 673
Cdd:PLN02983 262 PVSVDTPL 269
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
600-677 |
1.52e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 51.26 E-value: 1.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927177 600 SSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 677
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
157-279 |
4.80e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.10 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 157 ARRIGYPVMikaVRGG---GGKGMRIVRSEQEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNAVYL 233
Cdd:PRK05294 700 AEEIGYPVL---VRPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLI 770
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927177 234 ---FErdcsvqrrHqkiIEEApapGIKS--------------EVRKKLGEAAVRAAKAVNYVG 279
Cdd:PRK05294 771 ggiME--------H---IEEA---GVHSgdsacslppqtlseEIIEEIREYTKKLALELNVVG 819
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
68-281 |
1.44e-05 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 48.13 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 68 SYLSMEKIIQVAKtsaaqaihpGCGFLSENME------FAELCKQEgiIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVE 141
Cdd:PLN02948 70 SFDDRAAVREFAK---------RCDVLTVEIEhvdvdtLEALEKQG--VDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 142 gyHGEDQSDQCLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEfqeqLESArrEAKKSFNDDAMLIEKFVDTPRHVEV 220
Cdd:PLN02948 139 --FMEIDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEED----LSSA--VAALGGFERGLYAEKWAPFVKELAV 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927177 221 QVFGDHHGNAV-Y-LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNyvGAG 281
Cdd:PLN02948 211 MVARSRDGSTRcYpVVE---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEKAVGSLE--GAG 267
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
11-302 |
1.93e-05 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 48.07 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 11 ITKVLIANRGEI--------------ACRVMrtaKKLGVQTVAVYSEADRNSMHVDMADEAYsIGPAPSQqsylSMEKII 76
Cdd:TIGR01369 6 IKKILVIGSGPIvigqaaefdysgsqACKAL---KEEGYRVILVNSNPATIMTDPEMADKVY-IEPLTPE----AVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 77 QVAKtsaAQAIHPGCG---FLSENMEFAEL--CKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQsDQ 151
Cdd:TIGR01369 78 EKER---PDAILPTFGgqtALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSV-EE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 152 CLkEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKsfndDAMLIEKFVDTPRHVEVQVFGDHHGNAV 231
Cdd:TIGR01369 154 AL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDSNDNCI 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927177 232 YLferdCSVQR-----RHQ-KIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSK-HNFCFMEMNTRL 302
Cdd:TIGR01369 229 TV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVNPRV 302
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
125-317 |
2.34e-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: 42.49 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 125 KSTSKSIMAAAG--VPVVEGYHGEDQSDQCLKEHARRigYPVMIKAVRGGGGKGMRIVRSEQEFqEQLESARREakksfn 202
Cdd:pfam08443 4 KAKSHQLLAKHGigPPNTRLAWYPEDAEQFIEQIKRQ--FPVIVKSIYGSQGIGVFLAEDEQKL-RQTLSATNE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 203 ddAMLIEKFVDTP--RHVEVQVFGDHHGNAVYLFERDCSVQRRHQKiieeaPAPGIKSEVRKKLGEAAVRAAKAVNYVGA 280
Cdd:pfam08443 75 --QILVQEFIAEAnnEDIRCLVVGDQVVGALHRQSNEGDFRSNLHR-----GGVGEKYQLSQEETELAIKAAQAMQLDVA 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 767927177 281 GtVEfIMDSKHNFCFMEMNTRLQVEhpVTEMITGTDL 317
Cdd:pfam08443 148 G-VD-LLRQKRGLLVCEVNSSPGLE--GIEKTLGINI 180
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
101-213 |
2.50e-04 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 43.85 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 101 AELCKQEGI--IFIGP--PPSA-----IRDMGI---------------KSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEH 156
Cdd:COG0151 55 VAFAKEENIdlVVVGPeaPLVAgivdaFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAAYRVFTDLEE--ALAY 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927177 157 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEfqeqlesARREAKKSFNDDAM-------LIEKFVD 213
Cdd:COG0151 133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLE 189
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
617-681 |
9.52e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 42.30 E-value: 9.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927177 617 GTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 681
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
157-301 |
1.32e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.07 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 157 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYlfer 236
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVVI---- 804
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927177 237 dCSVQRRhqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTR 301
Cdd:PLN02735 805 -GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
613-664 |
1.44e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.87 E-value: 1.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 664
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
160-233 |
1.54e-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: 39.57 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 160 IGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 231
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 767927177 232 YL 233
Cdd:pfam13535 80 IL 81
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
153-213 |
1.79e-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: 41.26 E-value: 1.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927177 153 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKS--FNDDAMLIEKFVD 213
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
613-639 |
2.14e-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: 41.60 E-value: 2.14e-03
10 20
....*....|....*....|....*..
gi 767927177 613 APMTGTIEKVFVKAGDKVKAGDSLMVM 639
Cdd:COG1038 1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
125-225 |
2.84e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 39.57 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927177 125 KSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVM-IKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFND 203
Cdd:pfam01071 3 KSFAKDFMKRYGIPTAEYETFTDPEE--AKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100
....*....|....*....|..
gi 767927177 204 DAMLIEKFVDTPrHVEVQVFGD 225
Cdd:pfam01071 81 ETVVIEEFLEGE-EVSVLAFVD 101
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
612-639 |
2.87e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 2.87e-03
10 20
....*....|....*....|....*...
gi 767927177 612 LAPMTGTIEKVFVKAGDKVKAGDSLMVM 639
Cdd:PRK12999 1117 TAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
153-199 |
5.47e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 39.74 E-value: 5.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767927177 153 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKK 199
Cdd:PRK09288 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
|
|
| |
