|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
49-504 |
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 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 208
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 288
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 369 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 448
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 116805327 449 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAA 504
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEE 456
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
49-492 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 681.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 208
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 288
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 369 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 448
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 116805327 449 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 492
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
49-495 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 646.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 208
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 288
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 369 PLSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHLSTPRAdPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 448
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 116805327 449 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQ 495
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVK 446
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
47-492 |
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: 622.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 47 RNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLSMEKIIQVAKTSAAQAI 125
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 126 HPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIK 205
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 206 AVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKI 285
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 286 IEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAG 365
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 366 EK-------IPlSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhlstpradpstRIET-------GVR-------QGD 424
Cdd:COG1038 322 YSlddpeigIP-SQEDIRLNGYAIQCRITTEDPANNFMPDTG--------------RITAyrsaggfGIRldggnayTGA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116805327 425 EVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 492
Cdd:COG1038 387 VITPYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
51-494 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 618.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 51 KVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCG 130
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 131 FLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGG 210
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 211 GGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAP 290
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 291 APGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMdSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPL 370
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 371 SQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTK 450
Cdd:PRK08654 323 KQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 116805327 451 LRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHK 494
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETT 445
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
47-503 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 601.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 47 RNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLSMEKIIQVAKTSAAQAI 125
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 126 HPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIK 205
Cdd:PRK12999 83 HPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 206 AVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKI 285
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 286 IEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAG 365
Cdd:PRK12999 243 VEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 366 EKI------PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhlstpradpstRIET-------GVR-------QGDE 425
Cdd:PRK12999 323 ATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTG--------------RITAyrspggfGVRldggnafAGAE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116805327 426 VSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQhHKQLLLSRKAA 503
Cdd:PRK12999 389 ITPYYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE-TPELFDFPKRR 465
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
50-489 |
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 116805327 50 TKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGC 129
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 130 GFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGyHGEDQSDQCLKEHARRIGYPVMIKAVRG 209
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 210 GGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEA 289
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 290 PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 369 PLSQ--EEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRAdpsTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQA 446
Cdd:TIGR02712 321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDD---VRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 116805327 447 ALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 489
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
49-494 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 582.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 208
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 288
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 369 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 448
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIP-GGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 116805327 449 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHK 494
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
49-492 |
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: 573.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 208
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 288
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 369 PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAAL 448
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPP-GGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 116805327 449 TKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 492
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
49-501 |
4.95e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 521.97 E-value: 4.95e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPsQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQS-DQCLKEhARRIGYPVMIKAV 207
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADlDEALAE-AERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 208 RGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 287
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 288 EAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 367
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 368 IPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAA 447
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 116805327 448 LTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRK 501
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIK 452
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
47-492 |
1.90e-175 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 509.29 E-value: 1.90e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 47 RNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIH 126
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 127 PGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKA 206
Cdd:PRK08462 82 PGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 207 VRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKII 286
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 287 EEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGE 366
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 367 KIPlSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQA 446
Cdd:PRK08462 322 ELP-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAP-GGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 116805327 447 ALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 492
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
49-489 |
6.52e-174 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 506.21 E-value: 6.52e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 208
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKIIEE 288
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 APAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMD-SKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 367
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 368 IPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRAdPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAA 447
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQG-PGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 116805327 448 LTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 489
Cdd:PRK12833 403 LARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
49-497 |
3.77e-169 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 494.33 E-value: 3.77e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQqSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHG-EDQSDQCLKEHARRIGYPVMIKAV 207
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 208 RGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 287
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 288 EAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 367
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 368 IPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLsTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAA 447
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEY-YPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 116805327 448 LTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLL 497
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELL 449
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
51-492 |
7.81e-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: 504.75 E-value: 7.81e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 51 KVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQ---QSYLSMEKIIQVAKTSAAQAIHP 127
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 128 GCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAV 207
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 208 RGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 287
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 288 EAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 367
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 368 IPL------SQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADpSTRIETGVR-QGDEVSVHYDPMIAKLVVW 440
Cdd:TIGR01235 321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGF-GIRLDGGNSyAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 116805327 441 AADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 492
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
163-369 |
4.25e-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: 4.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 163 KSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDD 242
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 243 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVE 322
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116805327 323 FIMDSKH-NFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIP 369
Cdd:pfam02786 162 FALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
110-372 |
1.34e-66 |
|
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: 220.51 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 110 MEKIIQVAKTSAAQaiHPGCGFLSEN----MEFAELCKQEGIIfiGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGED 185
Cdd:COG0439 2 IDAIIAAAAELARE--TGIDAVLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 186 QSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHH 265
Cdd:COG0439 78 PEE--ALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 266 GNAVYlferdCSVQRRHQK---IIE---EAPAPgIKSEVRKKLGEAAVRAAKAVNYV-GAGTVEFIMDSKHNFCFMEMNT 338
Cdd:COG0439 154 GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINA 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 116805327 339 RLQVEH--PVTEMITGTDLVEWQLRIAAGEKIPLSQ 372
Cdd:COG0439 228 RLGGEHipPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
49-156 |
4.90e-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: 202.72 E-value: 4.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPG 128
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 116805327 129 CGFLSENMEFAELCKQEGIIFIGPPPSA 156
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
383-489 |
3.81e-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: 3.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 383 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 462
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 116805327 463 LHTNIDFLLNLSGHPEFEAGNVHTDFI 489
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
383-491 |
4.16e-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: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 383 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 462
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 116805327 463 LHTNIDFLLNLSGHPEFEAGNVHTDFIPQ 491
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
651-714 |
2.00e-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: 96.72 E-value: 2.00e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 714
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
648-714 |
2.28e-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: 94.05 E-value: 2.28e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116805327 648 GPLAPM------TGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 714
Cdd:cd06663 1 TILIPDlaqhlgDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
163-338 |
3.96e-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: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 163 KSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnDD 242
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 243 AMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAK 311
Cdd:COG1181 170 KVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243
|
170 180
....*....|....*....|....*..
gi 116805327 312 AVNYVGAGTVEFIMDSKHNFCFMEMNT 338
Cdd:COG1181 244 ALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
632-713 |
4.16e-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: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 632 PVPKYLSSVSSQETQGGP---LAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 708
Cdd:PRK05641 67 PTPVAPAAPAPAPASAGEnvvTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
....*
gi 116805327 709 TPLVE 713
Cdd:PRK05641 147 QPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
651-704 |
1.57e-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: 1.57e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 704
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
632-715 |
1.70e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 86.43 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 632 PVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTP 710
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 116805327 711 LVEFE 715
Cdd:PRK09282 587 LMEIE 591
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
651-704 |
3.89e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 86.35 E-value: 3.89e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 704
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 ... |
169-338 |
2.24e-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: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 169 IMAAAGVPVV-------EGYHgEDQSDQCLKEHARrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnD 241
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWK-LNPKEWCAQVEEA-LGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 242 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIKSEVRKKLGEAAVRAAKAVN 314
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 116805327 315 YVGAGTVEFIMDSKHNFCFMEMNT 338
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
131-369 |
7.77e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 79.97 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 131 FLSENMEfaELckQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRG- 209
Cdd:COG3919 90 LLSRHRD--EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 210 -------GGGKGMRIVRSEQEFQEQLESARREakksfnDDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcsVQR 280
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF-----TGR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 281 RHQkiieEAPAPG-----IKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRL--QVEHPVtemITG 352
Cdd:COG3919 233 KLR----HYPPAGgnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRFwrSLYLAT---AAG 305
|
250
....*....|....*..
gi 116805327 353 TDLVEWQLRIAAGEKIP 369
Cdd:COG3919 306 VNFPYLLYDDAVGRPLE 322
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
166-338 |
1.48e-15 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 77.84 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 166 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHarRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARReakksfNDDAML 245
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLTREEDLLAAID--KLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 246 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIKSEVRKKLGEAAVRAAK 311
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 116805327 312 AVNYVGAGTVEFIMDSKHNFCFMEMNT 338
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
651-714 |
1.00e-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: 69.55 E-value: 1.00e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116805327 651 APMTGT-----IEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 714
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
651-715 |
1.06e-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: 71.46 E-value: 1.06e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116805327 651 APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 715
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
630-702 |
2.74e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 76.51 E-value: 2.74e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116805327 630 DIPVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 702
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
163-338 |
3.14e-14 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 74.39 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 163 KSTSKSIMAAAGVPVVEGY--HGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfn 240
Cdd:PRK01966 124 KILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 241 DDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIKSEVRKKL 302
Cdd:PRK01966 198 DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKI 263
|
170 180 190
....*....|....*....|....*....|....*.
gi 116805327 303 GEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNT 338
Cdd:PRK01966 264 RELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
152-323 |
5.23e-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: 70.87 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 152 PPPSAIR---DmgiKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQeq 227
Cdd:COG0026 79 PGPEALEiaqD---RLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 228 lesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkIIEE--APApGIKSEVRKKLG 303
Cdd:COG0026 152 ------AAWAALGGGPCILEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--ILDEsiAPA-RISEALAAEAE 219
|
170 180
....*....|....*....|
gi 116805327 304 EAAVRAAKAVNYVGAGTVEF 323
Cdd:COG0026 220 EIAKRIAEALDYVGVLAVEF 239
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
63-337 |
4.49e-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: 67.27 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 63 RVMRTAKKLGVQTVavyseadrnsmHVDMADEAYSIGPAPSqqsylsmekIIQVAKTSAAQAIHPGCGFLSENMEFAELC 142
Cdd:COG0189 18 ALIEAAQRRGHEVE-----------VIDPDDLTLDLGRAPE---------LYRGEDLSEFDAVLPRIDPPFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 143 KQEGIIFIgPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQ 222
Cdd:COG0189 78 EAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 223 EFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFERDcsVQRRHQKIIEEAPAPGIKSEVRK 300
Cdd:COG0189 155 ALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRI--PAEGEFRTNLARGGRAEPVELTD 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 116805327 301 KLGEAAVRAAKAV--NYVGagtVEFIMDsKHNFCFMEMN 337
Cdd:COG0189 225 EERELALRAAPALglDFAG---VDLIED-DDGPLVLEVN 259
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
67-368 |
1.30e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 68.07 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 67 TAKKLGVQTVAVYSEADRNSMHVDMADEAYsIGPapsqqsyLSMEKIIQVAKT----------SAAQAIHpgcgfLSENM 136
Cdd:PRK12815 584 ALKKEGYETIMINNNPETVSTDYDTADRLY-FEP-------LTLEDVLNVAEAenikgvivqfGGQTAIN-----LAKGL 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 137 EFAelckqeGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMR 216
Cdd:PRK12815 651 EEA------GLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMA 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 217 IVRSEQEFQEQLESArreakkSFNDDAMLIEKFVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA---- 289
Cdd:PRK12815 723 VVYDEPALEAYLAEN------ASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhs 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 290 -------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKhNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 362
Cdd:PRK12815 783 gdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861
|
....*.
gi 116805327 363 AAGEKI 368
Cdd:PRK12815 862 LLGKSL 867
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
116-455 |
3.66e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 66.79 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 116 VAKTSAAQAIH------PGCGFLSENMEF-----AELCKQEGIIfiGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGE 184
Cdd:PRK02186 52 SADTSDPDRIHrfvsslDGVAGIMSSSEYfievaSEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 185 DQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFnddamLIEKFVDTPRHvEVQVFGDH 264
Cdd:PRK02186 130 LRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 265 HGNAVYlferdcSVQRRHQ-------KIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNY-VGAGTVEFIMdSKHNFCFMEM 336
Cdd:PRK02186 202 RGHQVL------GITRKHLgppphfvEIGHDFPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 337 NTRLQVEH-PVT-EMITGTDLVEWQLRIAAGE--------------KIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAG 400
Cdd:PRK02186 274 NPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVaafadptakrygaiRFVLPARSGVLRGLLFLPDDIAARPELRFHPLKQ 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116805327 401 PlVHLSTPRADPSTRIETGVRQGDE---VSVHYDPMIAKLVV-------WAADRQAALTKLRYSL 455
Cdd:PRK02186 354 P-GDALRLEGDFRDRIAAVVCAGDHrdsVAAAAERAVAGLSIdigdaarAAALNDAGAGAARPGL 417
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
136-327 |
7.58e-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: 65.28 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 136 MEFAELCKQEGIIFIGPPPSAI-----RDMgikstSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKA--VR 208
Cdd:COG0458 88 VELEEAGILEGVKILGTSPDAIdlaedREL-----FKELLDKLGIPQPKSGTATSVEE--ALAIAEEIGYPVIVRPsyVL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 209 GGggKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEE 288
Cdd:COG0458 161 GG--RGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 116805327 289 A-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDS 327
Cdd:COG0458 226 AgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD 275
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
171-323 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 171 AAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEqefqEQLESARREAKksfnDDAMLIEKF 249
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116805327 250 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 323
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
651-715 |
2.29e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 57.10 E-value: 2.29e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 715
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
152-323 |
3.41e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 62.48 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 152 PPPSAIR---DmgiKSTSKSIMAAAGVPVVEgYHG-EDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQe 226
Cdd:PRK06019 90 PGPDALAiaqD---RLTEKQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 227 qlesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGE 304
Cdd:PRK06019 163 -------AAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEE 231
|
170
....*....|....*....
gi 116805327 305 AAVRAAKAVNYVGAGTVEF 323
Cdd:PRK06019 232 IASRIAEELDYVGVLAVEF 250
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
192-368 |
3.64e-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: 63.48 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 192 KEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY- 270
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPg 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 271 LFErdcsvqrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSkHNFCFMEMNTR 339
Cdd:TIGR01369 773 IME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPR 840
|
170 180
....*....|....*....|....*....
gi 116805327 340 LQVEHPVTEMITGTDLVEWQLRIAAGEKI 368
Cdd:TIGR01369 841 ASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
651-712 |
3.81e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 58.28 E-value: 3.81e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLV 712
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
629-714 |
2.31e-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: 54.33 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 629 IDIPVPKYLSSVSSqetqggplapmtGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 708
Cdd:cd06849 1 TEIKMPDLGESMTE------------GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVG 68
|
....*.
gi 116805327 709 TPLVEF 714
Cdd:cd06849 69 QVIAVI 74
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
153-357 |
2.39e-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: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 153 PPSAIRDMGIKSTSKSIMAAAGVPVVEG--YHGEDQSDQCLKEharrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLES 230
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTglAGSPEEALKLIEE----IGFPVVLKPVFGSWGRGVSLARDRQAAESLLEH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 231 ARREAKKSfndDAMLIEKFVDTPRHVEVQVF--GDHHGNAVYL-----FERDCSVQRRHQKIieeapapgiksEVRKKLG 303
Cdd:TIGR00768 155 FEQLNGPQ---NLFLVQEYIKKPGGRDIRVFvvGDEVVAAIYRitsghWRSNLARGGKAEPC-----------SLTEEIE 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116805327 304 EAAVRAAKAVNyVGAGTVEFIMdSKHNFCFMEMNTRLQVEHpvTEMITGTDLVE 357
Cdd:TIGR00768 221 ELAIKAAKALG-LDVAGVDLLE-SEDGLLVNEVNANPEFKN--SVKTTGVNIAG 270
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
91-369 |
3.11e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 59.13 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 91 MADEAYSIgPAPSQQSYLsmEKIIQVAKTSAAQAIHPG----CGFLSENM-EFAElckqEGIIFIGPPPSAIRDMGIKST 165
Cdd:PRK12767 42 FADKFYVV-PKVTDPNYI--DRLLDICKKEKIDLLIPLidpeLPLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKWL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 166 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKsfnddaML 245
Cdd:PRK12767 115 TYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 246 IEKFVDTPRhVEVQVFGDHHGNAVYLFERdcsvqRRHQKIIEEApapgIKSEVRK--KLGEAAVRAAKAVNYVGAGTVEF 323
Cdd:PRK12767 185 IQEFIEGQE-YTVDVLCDLNGEVISIVPR-----KRIEVRAGET----SKGVTVKdpELFKLAERLAEALGARGPLNIQC 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 116805327 324 IMDSKhNFCFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIAAGEKIP 369
Cdd:PRK12767 255 FVTDG-EPYLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGGENE 298
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
653-725 |
1.34e-07 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 54.41 E-value: 1.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116805327 653 MT-GTIEKVFVKAGDKVKAGDSLMVM----IAMKMEhtikSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE 725
Cdd:PRK11856 14 MTeGEIVEWLVKVGDTVKEGQPLAEVetdkATVEIP----SPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAA 87
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
655-714 |
2.04e-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: 48.91 E-value: 2.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116805327 655 GTIEKVFVKAGDKVKAGDSLMVMIAMK--MEhtIKSPKDGTVKKVFYREGAQANRHTPLVEF 714
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
167-250 |
2.33e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 54.39 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 167 KSIMAAAGVPVVEGY--HGEDQsdqcLKEHARRIGYPVMIKAVRGGGGKGMRI-VRSEqefqEQLESARREAKKSFNDda 243
Cdd:PRK14016 219 KRLLAAAGVPVPEGRvvTSAED----AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD-- 288
|
....*..
gi 116805327 244 MLIEKFV 250
Cdd:PRK14016 289 VIVERYI 295
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
655-719 |
4.60e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 53.29 E-value: 4.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116805327 655 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 719
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
655-718 |
1.11e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 51.75 E-value: 1.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116805327 655 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEE 718
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
632-711 |
1.28e-06 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 50.61 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 632 PVPKYLSSVSSQETqggPL-APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGA 703
Cdd:PLN02983 185 ASPPPAKAPKSSHP---PLkSPMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGK 261
|
....*...
gi 116805327 704 QANRHTPL 711
Cdd:PLN02983 262 PVSVDTPL 269
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
638-715 |
1.67e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 51.26 E-value: 1.67e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116805327 638 SSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 715
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
195-317 |
4.47e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.10 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 195 ARRIGYPVMikaVRGG---GGKGMRIVRSEQEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNAVYL 271
Cdd:PRK05294 700 AEEIGYPVL---VRPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLI 770
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116805327 272 ---FErdcsvqrrHqkiIEEApapGIKS--------------EVRKKLGEAAVRAAKAVNYVG 317
Cdd:PRK05294 771 ggiME--------H---IEEA---GVHSgdsacslppqtlseEIIEEIREYTKKLALELNVVG 819
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
106-319 |
1.58e-05 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 48.13 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 106 SYLSMEKIIQVAKtsaaqaihpGCGFLSENME------FAELCKQEgiIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVE 179
Cdd:PLN02948 70 SFDDRAAVREFAK---------RCDVLTVEIEhvdvdtLEALEKQG--VDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 180 gyHGEDQSDQCLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEfqeqLESArrEAKKSFNDDAMLIEKFVDTPRHVEV 258
Cdd:PLN02948 139 --FMEIDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEED----LSSA--VAALGGFERGLYAEKWAPFVKELAV 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116805327 259 QVFGDHHGNAV-Y-LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNyvGAG 319
Cdd:PLN02948 211 MVARSRDGSTRcYpVVE---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEKAVGSLE--GAG 267
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
49-340 |
1.60e-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: 48.46 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 49 ITKVLIANRGEI--------------ACRVMrtaKKLGVQTVAVYSEADRNSMHVDMADEAYsIGPAPSQqsylSMEKII 114
Cdd:TIGR01369 6 IKKILVIGSGPIvigqaaefdysgsqACKAL---KEEGYRVILVNSNPATIMTDPEMADKVY-IEPLTPE----AVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 115 QVAKtsaAQAIHPGCG---FLSENMEFAEL--CKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQsDQ 189
Cdd:TIGR01369 78 EKER---PDAILPTFGgqtALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSV-EE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 190 CLkEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKsfndDAMLIEKFVDTPRHVEVQVFGDHHGNAV 269
Cdd:TIGR01369 154 AL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDSNDNCI 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116805327 270 YLferdCSVQR-----RHQ-KIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSK-HNFCFMEMNTRL 340
Cdd:TIGR01369 229 TV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVNPRV 302
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
163-355 |
1.76e-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: 43.26 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 163 KSTSKSIMAAAG--VPVVEGYHGEDQSDQCLKEHARRigYPVMIKAVRGGGGKGMRIVRSEQEFqEQLESARREakksfn 240
Cdd:pfam08443 4 KAKSHQLLAKHGigPPNTRLAWYPEDAEQFIEQIKRQ--FPVIVKSIYGSQGIGVFLAEDEQKL-RQTLSATNE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 241 ddAMLIEKFVDTP--RHVEVQVFGDHHGNAVYLFERDCSVQRRHQKiieeaPAPGIKSEVRKKLGEAAVRAAKAVNYVGA 318
Cdd:pfam08443 75 --QILVQEFIAEAnnEDIRCLVVGDQVVGALHRQSNEGDFRSNLHR-----GGVGEKYQLSQEETELAIKAAQAMQLDVA 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 116805327 319 GtVEfIMDSKHNFCFMEMNTRLQVEHpvTEMITGTDL 355
Cdd:pfam08443 148 G-VD-LLRQKRGLLVCEVNSSPGLEG--IEKTLGINI 180
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
139-251 |
2.24e-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: 44.23 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 139 AELCKQEGI--IFIGP--PPSA-----IRDMGI---------------KSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEH 194
Cdd:COG0151 55 VAFAKEENIdlVVVGPeaPLVAgivdaFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAAYRVFTDLEE--ALAY 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116805327 195 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEfqeqlesARREAKKSFNDDAM-------LIEKFVD 251
Cdd:COG0151 133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLE 189
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
655-719 |
9.77e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 42.30 E-value: 9.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116805327 655 GTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 719
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
195-339 |
1.24e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 195 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYlfer 274
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVVI---- 804
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116805327 275 dCSVQRRhqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTR 339
Cdd:PLN02735 805 -GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
651-702 |
1.28e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.87 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 702
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
198-271 |
1.46e-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: 39.96 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 198 IGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 269
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 116805327 270 YL 271
Cdd:pfam13535 80 IL 81
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
191-251 |
1.97e-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: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116805327 191 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKS--FNDDAMLIEKFVD 251
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
651-677 |
2.22e-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: 2.22e-03
10 20
....*....|....*....|....*..
gi 116805327 651 APMTGTIEKVFVKAGDKVKAGDSLMVM 677
Cdd:COG1038 1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
163-263 |
2.33e-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: 39.96 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805327 163 KSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVM-IKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFND 241
Cdd:pfam01071 3 KSFAKDFMKRYGIPTAEYETFTDPEE--AKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100
....*....|....*....|..
gi 116805327 242 DAMLIEKFVDTPrHVEVQVFGD 263
Cdd:pfam01071 81 ETVVIEEFLEGE-EVSVLAFVD 101
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
650-677 |
3.04e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 3.04e-03
10 20
....*....|....*....|....*...
gi 116805327 650 LAPMTGTIEKVFVKAGDKVKAGDSLMVM 677
Cdd:PRK12999 1117 TAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
191-237 |
6.17e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 39.74 E-value: 6.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 116805327 191 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKK 237
Cdd:PRK09288 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
|
|
| |
