|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-464 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 853.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPT 400
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-----GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 760079558 401 REAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAEEYPDGFQGAVLDEPTL 464
Cdd:COG4770 396 REEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEELAL 459
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-480 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 661.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGqKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPT 400
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP-----GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 401 REAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAEEypdgfqgAVLDEPTLRRVAAAAAAMNRVAEI 480
Cdd:PRK08654 395 REEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEE-------TTILEEMKRYALEEEEREKTLSEK 467
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-450 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 659.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPpvesvtPTSV-VRNDTGVYEGGEISMYYDPMIAKLCTWAP 399
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHP------PGGPgVRVDSAVYTGYTIPPYYDSMIGKLIVHGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 760079558 400 TREAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIaEEY 450
Cdd:PRK08591 395 TREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL-EKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 649.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPyRNFLPSIGRLTRYrppveSVTPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPT 400
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDL-----TLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGET 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 760079558 401 REAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFI 446
Cdd:PRK06111 395 REEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-455 |
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 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPAN-QSYIVIDKIMEAIKQSGAEAVH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 80 PGYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKA 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 160 SAGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVI 239
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 240 EEAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGE 319
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 320 KLPF------QQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRppvesvTPTSV-VRNDTG-VYEGGEISMYYDPMI 391
Cdd:PRK12999 324 TLHDleigipSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYR------SPGGFgVRLDGGnAFAGAEITPYYDSLL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 760079558 392 AKLCTWAPTREAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIaEEYPDGFQ 455
Cdd:PRK12999 398 VKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFI-DETPELFD 460
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-455 |
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: 592.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPP--PAnQSYIVIDKIMEAIKQSGAEAV 78
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGkgPV-DAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 79 HPGYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIK 158
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 159 ASAGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKV 238
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 239 IEEAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAG 318
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 319 EKL-------PfQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRppvesvTPTSV-VRNDTG-VYEGGEISMYYDP 389
Cdd:COG1038 322 YSLddpeigiP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYR------SAGGFgIRLDGGnAYTGAVITPYYDS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 760079558 390 MIAKLCTWAPTREAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIaEEYPDGFQ 455
Cdd:COG1038 395 LLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFI-DETPELFD 459
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
2-447 |
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: 570.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 2 FKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHPG 81
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 82 YGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGyMGLIADADEAVKISNEIGYPVMIKASA 161
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 162 GGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIEE 241
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 242 APSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKN-FYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQS--DLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPPvesvtptSVVRNDTGVYEGGEISMYYDPMIAKLCTWA 398
Cdd:TIGR02712 320 PDFASLniSLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFP-------DDVRVDTWVETGTEVSPEYDPMLAKIIVHG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 760079558 399 PTREAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIA 447
Cdd:TIGR02712 393 SDREDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLN 441
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-448 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 569.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPT 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPP-----GGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 760079558 401 REAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAE 448
Cdd:TIGR00514 396 REVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-450 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 560.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTryrppvESVTPTSV-VRNDTGVYEGGEISMYYDPMIAKLCTWAP 399
Cdd:PRK05586 321 LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIE------ELYIPGGLgVRVDSAVYSGYTIPPYYDSMIGKLIVYGK 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 760079558 400 TREAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAEEY 450
Cdd:PRK05586 395 DREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKL 445
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-452 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 521.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPAnQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKAS 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 161 AGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIE 240
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 241 EAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 321 LPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPT 400
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAP-----GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 760079558 401 REAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIaEEYPD 452
Cdd:PRK07178 395 WEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFV-ESHPE 445
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
3-446 |
5.52e-172 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 498.90 E-value: 5.52e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 3 KKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHPGY 82
Cdd:PRK12833 6 RKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 83 GFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKASAG 162
Cdd:PRK12833 86 GFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 163 GGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHgNCVYLHERECSIQRRNQKVIEEA 242
Cdd:PRK12833 166 GGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 243 PSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKN-FYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEKL 321
Cdd:PRK12833 245 PSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGeFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 322 PFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPTR 401
Cdd:PRK12833 325 RFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWP-----QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 760079558 402 EAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFI 446
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-450 |
6.96e-166 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 482.71 E-value: 6.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 3 KKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHPGY 82
Cdd:PRK08462 5 KRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 83 GFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKASAG 162
Cdd:PRK08462 85 GFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 163 GGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIEEA 242
Cdd:PRK08462 165 GGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 243 PSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEKLP 322
Cdd:PRK08462 245 PAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 323 fQQSDLKINGWAMESRLYAEDPyRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPTRE 402
Cdd:PRK08462 325 -SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAP-----GGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRN 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 760079558 403 AAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAEEY 450
Cdd:PRK08462 398 RAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEHF 445
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-448 |
6.70e-156 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 458.51 E-value: 6.70e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 1 MFKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPAnQSYIVIDKIMEAIKQSGAEAVHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 81 GYGFLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKI-SNEIGYPVMIKA 159
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 160 SAGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVI 239
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 240 EEAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGE 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 320 KLPFQQSDLKINGWAMESRLYAEDPYRNFLPSIGRLTRYRPpveSVTPTsvVRNDTGVYEGGEISMYYDPMIAKLCTWAP 399
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYP---ALGPS--VRVDSHIYKDYTIPPYYDSMLAKLIVKAT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 760079558 400 TREAAIEEMRLALDTFEVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAE 448
Cdd:PRK08463 395 SYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
1.64e-91 |
|
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: 282.66 E-value: 1.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 115 DKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKASAGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGD 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 195 DRIFIEKFVTQPRHIEIQVLADKHGNCVYLHERECSIQRRNQKVIEEAPSPFLDEATRKAMGEQACALAKAVGYASAGTV 274
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 760079558 275 EFIVD-GQKNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEKLP 322
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
1.14e-60 |
|
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: 198.09 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 2 FKKILIANRGEIACRVIKTARKMGIQTVAVYSDADRNALHVSMADEAIHIGPPPANQSYIVIDKIMEAIKQSGAEAVHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 760079558 82 YGFLSERMDFAAALEAAGVVFIGPPSGA 109
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-320 |
2.73e-56 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 192.01 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 62 VIDKIMEAIKQSGAEAVHPGYGFLSERmdFAAALEAAGvvFIGPPSGAIEAMGDKITSKKLAKEAGVStVPGYMgLIADA 141
Cdd:COG0439 5 IIAAAAELARETGIDAVLSESEFAVET--AAELAEELG--LPGPSPEAIRAMRDKVLMREALAAAGVP-VPGFA-LVDSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 142 DEAVKISNEIGYPVMIKASAGGGGKGMRIAWSEAEVKEGFESSKNEAANSFGDDRIFIEKFVtQPRHIEIQVLADkHGNC 221
Cdd:COG0439 79 EEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFL-EGREYSVEGLVR-DGEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 222 VYlhereCSIQRRNQK---VIE---EAPSPfLDEATRKAMGEQACALAKAVGYA-SAGTVEFIVDGQKNFYFLEMNTRLQ 294
Cdd:COG0439 157 VV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLG 230
|
250 260
....*....|....*....|....*...
gi 760079558 295 VEH--PVTELITGIDLVEQMIRVAAGEK 320
Cdd:COG0439 231 GEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-447 |
6.01e-50 |
|
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: 169.13 E-value: 6.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 336 ESRLYAEDPYRNFLPSIGRLTRYRPPVESVtptsvVRNDTGVYEGGEISMYYDPMIAKLCTWAPTREAAIEEMRLALDTF 415
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPG-----VRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEF 75
|
90 100 110
....*....|....*....|....*....|..
gi 760079558 416 EVEGIGHNLPFVGAVMDHPRFVKGDITTAFIA 447
Cdd:smart00878 76 RIRGVKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-448 |
2.95e-48 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 164.59 E-value: 2.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 336 ESRLYAEDPYRNFLPSIGRLTRYRPPvesvtPTSVVRNDTGVYEGGEISMYYDPMIAKLCTWAPTREAAIEEMRLALDTF 415
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-----GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEF 75
|
90 100 110
....*....|....*....|....*....|...
gi 760079558 416 EVEGIGHNLPFVGAVMDHPRFVKGDITTAFIAE 448
Cdd:pfam02785 76 RIEGVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| PCC_BT |
pfam18140 |
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ... |
474-591 |
3.88e-41 |
|
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.
Pssm-ID: 465666 [Multi-domain] Cd Length: 126 Bit Score: 145.85 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 474 MNRVAEIRRTRISGTMNNHERHVGVDWVVALQGESYHVSIAADREGSTVSF-SDGSSLRVTSDWTPGQPLASLMVDGRPL 552
Cdd:pfam18140 8 IHAVRELRARRISGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVtVDGETVTVSSDWRPGDPLFRGTVDGEPV 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 760079558 553 VMKVGKIPMGFRLRLRGSDLKVNVRTPRQAELALLMPEK 591
Cdd:pfam18140 88 TVQVERRAGGYRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
600-665 |
1.04e-23 |
|
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: 94.79 E-value: 1.04e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 760079558 600 LLCPMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEF 665
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
547-666 |
1.66e-19 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 92.60 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 547 VDGRPLVMKVG----KIPMGFRLRLRGSDLKVNVRTPRQAELAllmpEKLPPDTSKYLLCPMPGLVVKINVAEGDEVQEG 622
Cdd:PRK09282 472 VDGEKYEVKIEgvkaEGKRPFYLRVDGMPEEVVVEPLKEIVVG----GRPRASAPGAVTSPMPGTVVKVKVKEGDKVKAG 547
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 760079558 623 QALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK09282 548 DTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
603-665 |
2.91e-19 |
|
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: 92.84 E-value: 2.91e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760079558 603 PMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEF 665
Cdd:COG1038 1082 PMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
603-666 |
4.78e-18 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 88.66 E-value: 4.78e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 760079558 603 PMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK12999 1082 PMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
92-321 |
1.11e-16 |
|
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: 84.28 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 92 AAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGymGLIADADEAVKISNEIGYPVMIKASAGGGGKGMRIA 171
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 172 WSEAEVKEGFEssknEAANSFGDDRIFIEKFVTQPRHIEIQVLADkhGNCVYLhereCSIQRRnqkvIEEA--------- 242
Cdd:TIGR01369 724 YNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEEVLI----PGIMEH----IEEAgvhsgdstc 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 243 --PSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQkNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRVAAGEK 320
Cdd:TIGR01369 790 vlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDG-EVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKK 868
|
.
gi 760079558 321 L 321
Cdd:TIGR01369 869 L 869
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
603-666 |
3.35e-15 |
|
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: 72.62 E-value: 3.35e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760079558 603 PMPGLV-------VKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:COG0511 66 PMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-321 |
3.71e-14 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 76.16 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 92 AAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMGliADADEAVKISNEIGYPVMIKASAGGGGKGMRIA 171
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 172 WSEAEVKEGFESskneaaNSFGDDRIFIEKFVTQpRHIEIQVLADkhGNCVYL-----HerecsiqrrnqkvIEEA---- 242
Cdd:PRK12815 725 YDEPALEAYLAE------NASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIpgiieH-------------IEQAgvhs 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 243 -------PSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQkNFYFLEMNTRLQVEHPVTELITGIDLVEQMIRV 315
Cdd:PRK12815 783 gdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861
|
....*.
gi 760079558 316 AAGEKL 321
Cdd:PRK12815 862 LLGKSL 867
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
603-665 |
1.70e-13 |
|
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: 65.70 E-value: 1.70e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 760079558 603 PMPG-----LVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEF 665
Cdd:pfam00364 6 PMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
93-291 |
2.66e-13 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 70.91 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 93 AALEAAGVVFIGPPSGAIeAMG-DKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIKASAGGGGKGMRIA 171
Cdd:COG1181 73 GLLELLGIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 172 WSEAEVKEGFessknEAANSFgDDRIFIEKFVTqPRHIEIQVLADKHGNCVYLHErecsIQRRN-----------QKVIE 240
Cdd:COG1181 152 KNAEELAAAL-----EEAFKY-DDKVLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEY 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 760079558 241 EAPSPfLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNT 291
Cdd:COG1181 221 ICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
92-292 |
9.64e-13 |
|
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: 71.06 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 92 AAALEAAGVV----FIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMglIADADEAVKISNEIGYPVMIKASAGGGGKG 167
Cdd:COG0458 87 AVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGT--ATSVEEALAIAEEIGYPVIVRPSYVLGGRG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 168 MRIAWSEAE----VKEGFESSkneaansfGDDRIFIEKFVTQPRHIEIQVLADKHGNCVYLhereCSIQrrNqkvIEEA- 242
Cdd:COG0458 165 MGIVYNEEEleeyLERALKVS--------PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAg 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 243 ----------PSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKnFYFLEMNTR 292
Cdd:COG0458 228 vhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
545-664 |
1.52e-12 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 65.65 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 545 LMVDGRPLVMKVGKIPMG-FRLRLRGSDLKVN------------------VRTPRQAELALLMPEKLPPDT-------SK 598
Cdd:PRK05641 6 VIVDGVEYEVEVEELGPGkFRVSFEGKTYEVEakglgidlsavqeqvptpAPAPAPAVPSAPTPVAPAAPApapasagEN 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 760079558 599 YLLCPMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIME 664
Cdd:PRK05641 86 VVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIE 151
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
3-293 |
1.07e-11 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 68.49 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 3 KKILIANRGEI----AC-------RVIKTARKMGIQTVAVYSdadrNALHVsMADEAIhigpppANQSYIV------IDK 65
Cdd:TIGR01369 7 KKILVIGSGPIvigqAAefdysgsQACKALKEEGYRVILVNS----NPATI-MTDPEM------ADKVYIEpltpeaVEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 66 ImeaIKQSGAEAVHPGYG-----FLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMglIAD 140
Cdd:TIGR01369 76 I---IEKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEI--AHS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 141 ADEAVKISNEIGYPVMIKASAGGGGKGMRIAWSEAEVKEgfessknEAANSFGD---DRIFIEKFVTQPRHIEIQVLADK 217
Cdd:TIGR01369 151 VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKE-------IAERALSAspiNQVLVEKSLAGWKEIEYEVMRDS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 218 HGNCVYLhereCSIQR------RNQKVIEEAPSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQ-KNFYFLEMN 290
Cdd:TIGR01369 224 NDNCITV----CNMENfdpmgvHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVN 299
|
...
gi 760079558 291 TRL 293
Cdd:TIGR01369 300 PRV 302
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
603-663 |
2.22e-11 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 66.88 E-value: 2.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760079558 603 PMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIM 663
Cdd:PRK14040 530 PLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
25-362 |
3.03e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 65.72 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 25 GIQTVAVYSDADRNALHVSMADEAiHIGPPPANQSYIVIDKIMEAIKQSGAEAVHPGY----GFLSERmdfAAALEAaGV 100
Cdd:COG3919 28 GVRVIVVDRDPLGPAARSRYVDEV-VVVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRH---RDELEE-HY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 101 VFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYmgLIADADEAVKISNEIGYPVMIKAS--------AGGGGKGMRIAW 172
Cdd:COG3919 103 RLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 173 SEAEVKEGFesskneAANSFGDDRIFIEKFVTQPRHIE--IQVLADKHGNCVYLhereCSIQRRNQKVIEEAPSPFLDEA 250
Cdd:COG3919 181 DREELLALL------RRIAAAGYELIVQEYIPGDDGEMrgLTAYVDRDGEVVAT----FTGRKLRHYPPAGGNSAARESV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 251 TRKAMGEQACALAKAVGYASAGTVEFIVD---GQknFYFLEMNTRLQVEHPVTeLITGIDLVEQMIRVAAGEKLPFQQSD 327
Cdd:COG3919 251 DDPELEEAARRLLEALGYHGFANVEFKRDprdGE--YKLIEINPRFWRSLYLA-TAAGVNFPYLLYDDAVGRPLEPVPAY 327
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 760079558 328 LKINGW-----AMESRLYAEDPYRNFLPSIGRLTRYRPPV 362
Cdd:COG3919 328 REGVLWrvlpgDLLLRYLRDGELRKRLRELLRRGKVVDAV 367
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
604-666 |
3.47e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 59.03 E-value: 3.47e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760079558 604 MPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK08225 8 MAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
603-660 |
4.24e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 60.98 E-value: 4.24e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 760079558 603 PMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDD 660
Cdd:PRK06549 67 PMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGD 124
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
603-666 |
8.05e-11 |
|
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: 65.62 E-value: 8.05e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 760079558 603 PMPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:TIGR01235 1080 PMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
90-291 |
4.93e-10 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 61.28 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 90 DFAAALEAAG--VVFI---GPP------SGAIEAMG---------------DKITSKKLAKEAGVSTVPGYMglIADADE 143
Cdd:PRK01372 47 DIAAQLKELGfdRVFNalhGRGgedgtiQGLLELLGipytgsgvlasalamDKLRTKLVWQAAGLPTPPWIV--LTREED 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 144 AVKISNEIGYPVMIKASAGGGGKGMRIAWSEAEVKEGFEssknEAANSfgDDRIFIEKFVTQPrhiEIQ--VLADK---- 217
Cdd:PRK01372 125 LLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALE----LAFKY--DDEVLVEKYIKGR---ELTvaVLGGKalpv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 218 ------HGNCVYlherecsiqrrNQKVIEEA-----PSPFLDEATRKAMgEQACALAKAVGYASAGTVEFIVDGQKNFYF 286
Cdd:PRK01372 196 ieivpaGEFYDY-----------EAKYLAGGtqyicPAGLPAEIEAELQ-ELALKAYRALGCRGWGRVDFMLDEDGKPYL 263
|
....*
gi 760079558 287 LEMNT 291
Cdd:PRK01372 264 LEVNT 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
34-335 |
5.72e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 61.05 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 34 DADRNALHVSMADEAIhIGPPPANQSYIviDKIMEAIKQSGAEAVHPGY----GFLSERMDfaaALEAAGVVFIGPPSGA 109
Cdd:PRK12767 32 DISELAPALYFADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 110 IEAMGDKITSKKLAKEAGVSTVPGYMGLIADADEAVKISNEIGYPVMIK-----ASaggggkgmrIAWSEAEVKEGFESS 184
Cdd:PRK12767 106 IEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKprdgsAS---------IGVFKVNDKEELEFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 185 KNEAANsfgddrIFIEKFVTQPRhIEIQVLADKHGNCVylhereCSIQRRNQKVI-------EEAPSPFLDEATRKamge 257
Cdd:PRK12767 177 LEYVPN------LIIQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKRIEVRagetskgVTVKDPELFKLAER---- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 760079558 258 qacaLAKAVGYASAGTVEFIVDGQKnFYFLEMNTRLQVEHPVTeLITGIDLVEQMIRVAAGEKLPFQQSDLKiNGWAM 335
Cdd:PRK12767 240 ----LAEALGARGPLNIQCFVTDGE-PYLFEINPRFGGGYPLS-YMAGANEPDWIIRNLLGGENEPIIGEYK-EGLYM 310
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
92-321 |
7.01e-09 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 59.34 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 92 AAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGymGLIADADEAVKISNEIGYPVMIKAS------Agggg 165
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSyvlggrA---- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 166 kgMRIAWSEAEVKEGFEssknEAANSFGDDRIFIEKFVTqpRHIEIQV--LADkhGNCVYL-----Herecsiqrrnqkv 238
Cdd:PRK05294 720 --MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLE--GAIEVDVdaICD--GEDVLIggimeH------------- 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 239 IEEA-----------PSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQKnFYFLEMNTRLQVEHPVTELITGID 307
Cdd:PRK05294 777 IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDE-VYVIEVNPRASRTVPFVSKATGVP 855
|
250
....*....|....
gi 760079558 308 LVEQMIRVAAGEKL 321
Cdd:PRK05294 856 LAKIAARVMLGKKL 869
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
95-291 |
7.49e-09 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 57.82 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 95 LEAAGVVFIGPPSGAiEAMG-DKITSKKLAKEAGVSTVPgYMGLIADADEAV---KISNEIGYPVMIKASaggggkgmR- 169
Cdd:PRK01966 103 LELLGIPYVGCGVLA-SALSmDKILTKRLLAAAGIPVAP-YVVLTRGDWEEAslaEIEAKLGLPVFVKPA--------Nl 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 170 ---IAWSEAEVKEGFESSKNEAansFG-DDRIFIEKFVtQPRHIEIQVLadkhGNcvylhERECSiqrrnqkVIEE--AP 243
Cdd:PRK01966 173 gssVGISKVKNEEELAAALDLA---FEyDRKVLVEQGI-KGREIECAVL----GN-----DPKAS-------VPGEivKP 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 760079558 244 SPFLD-------------------EATRKAMGEQACALAKAVGYASAGTVEFIVDGQKNFYFLEMNT 291
Cdd:PRK01966 233 DDFYDyeakyldgsaeliipadlsEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
606-665 |
2.53e-08 |
|
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: 51.25 E-value: 2.53e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 606 GLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEF 665
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
606-665 |
2.14e-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: 2.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 760079558 606 GLVVKINVAEGDEVQEGQALATVEAMK--MEniLRAERRGTVKKIAAAPGASLRVDDVIMEF 665
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
585-659 |
2.19e-07 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 52.92 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 585 ALLMPEKLPPDTSKYLLCPMPGLV-----------VKInvaeGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPG 653
Cdd:PLN02983 185 ASPPPAKAPKSSHPPLKSPMAGTFyrspapgeppfVKV----GDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDG 260
|
....*.
gi 760079558 654 ASLRVD 659
Cdd:PLN02983 261 KPVSVD 266
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
94-222 |
1.57e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 51.70 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 94 ALEAAGVVFI-GPPSGAIEAMGDKITSKKLAKEAGVSTVPGymGLIADADEAVKISNEIGYPVMIKASAGGGGKGMRIAW 172
Cdd:PLN02735 680 SASGNGNVKIwGTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVY 757
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 760079558 173 SEAEVKEGFESskneAANSFGDDRIFIEKFVTQPRHIEIQVLADKHGNCV 222
Cdd:PLN02735 758 SDDKLKTYLET----AVEVDPERPVLVDKYLSDATEIDVDALADSEGNVV 803
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-321 |
2.06e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 51.32 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 3 KKILIANRGEI----AC-------RVIKTARKMGIQTVAVYSDAdrnalhvsmadEAIHIGPPPANQSYI------VIDK 65
Cdd:PLN02735 24 KKIMILGAGPIvigqACefdysgtQACKALKEEGYEVVLINSNP-----------ATIMTDPETADRTYIapmtpeLVEQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 66 IMEAIKqsgAEAVHPGYG-----FLSERMDFAAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGymGLIAD 140
Cdd:PLN02735 93 VIAKER---PDALLPTMGgqtalNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPS--GIATT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 141 ADEAVKISNEIG-YPVMIKASAGGGGKGMRIAWSEAEVKEGFESSKNEAANSfgddRIFIEKFVTQPRHIEIQVLADKHG 219
Cdd:PLN02735 168 LDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELEVMRDLAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 220 NCVYLhereCSIQR------RNQKVIEEAPSPFLDEATRKAMGEQACALAKAVGYASAGT-VEFIV---DGQknFYFLEM 289
Cdd:PLN02735 244 NVVII----CSIENidpmgvHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVnpvDGE--VMIIEM 317
|
330 340 350
....*....|....*....|....*....|..
gi 760079558 290 NTRLQVEHPVTELITGIDLVEQMIRVAAGEKL 321
Cdd:PLN02735 318 NPRVSRSSALASKATGFPIAKMAAKLSVGYTL 349
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
122-291 |
2.08e-06 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 122 LAKEAGVSTVPgYMGLIADADE------AVKISNEIGYPVMIKASAGGGGKGMRIAWSEAEVKEGFEsskneAANSFgDD 195
Cdd:pfam07478 1 LLKAAGLPVVP-FVTFTRADWKlnpkewCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIE-----EAFQY-DE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 196 RIFIEKFVtQPRHIEIQVLADKHGNCVYLHER--ECSIQRRNQKVIEEA-----PSPfLDEATRKAMGEQACALAKAVGY 268
Cdd:pfam07478 74 KVLVEEGI-EGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKALGC 151
|
170 180
....*....|....*....|...
gi 760079558 269 ASAGTVEFIVDGQKNFYFLEMNT 291
Cdd:pfam07478 152 RGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
606-666 |
2.38e-06 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 50.17 E-value: 2.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760079558 606 GLVVKINVAEGDEVQEGQALATVEAMK--MEniLRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKatVE--IPSPVAGTVAKLLVEEGDVVPVGSVIAVIE 77
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
604-666 |
3.93e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 50.10 E-value: 3.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760079558 604 MPGLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-293 |
7.48e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 49.20 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 92 AAALEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTvpGYMGLIADADEAVKISNEIGYPVMIKASAGGGGKGMRIA 171
Cdd:PRK12815 105 DGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 172 WSEAEVKEGFESSKNEAANSfgddRIFIEKFVTQPRHIEIQVLADKHGNCVYLhereCSIQRrnqkvIEE---------- 241
Cdd:PRK12815 183 ENLEELEQLFKQGLQASPIH----QCLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDPvgihtgdsiv 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 760079558 242 -APSPFLDEATRKAMGEQACALAKAVGYASAGTVEFIVDGQ-KNFYFLEMNTRL 293
Cdd:PRK12815 250 vAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKsKQYYLIEVNPRV 303
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
608-662 |
1.42e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 43.26 E-value: 1.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 760079558 608 VVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVI 662
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
606-648 |
1.60e-05 |
|
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: 43.20 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 760079558 606 GLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKI 648
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKV 56
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
21-289 |
2.94e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 46.68 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 21 ARKMGIQtVAVYsDADRNALHVSMADEaiHIGPPPANQsyividkimEAIKQ--SGAEAVhpGYGFlsERMDFAAALEAA 98
Cdd:PRK06019 21 AAPLGYK-VIVL-DPDPDSPAAQVADE--VIVADYDDV---------AALRElaEQCDVI--TYEF--ENVPAEALDALA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 99 GVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPgYMgLIADADEAVKISNEIGYPVMIKASaggggkGM--------RI 170
Cdd:PRK06019 84 ARVPVPPGPDALAIAQDRLTEKQFLDKLGIPVAP-FA-VVDSAEDLEAALADLGLPAVLKTR------RGgydgkgqwVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 171 AwSEAEVKegfessknEAANSFGDDRIFIEKFVTQPRhiEIQVLA--DKHGNCVY------LHerecsiqrRNQ---KVI 239
Cdd:PRK06019 156 R-SAEDLE--------AAWALLGSVPCILEEFVPFER--EVSVIVarGRDGEVVFyplvenVH--------RNGilrTSI 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 760079558 240 eeAPSPfLDEATRKAMGEQACALAKAVGYasAGT--VEFIVDGQKNFYFLEM 289
Cdd:PRK06019 217 --APAR-ISAELQAQAEEIASRIAEELDY--VGVlaVEFFVTGDGELLVNEI 263
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
608-666 |
8.15e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.58 E-value: 8.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760079558 608 VVKINVAEGDEVQEGQALATVEAMK--MEniLRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
95-231 |
1.14e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 45.47 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 95 LEAAGVVFIGPPSGAIEAMGDKITSKKLAKEAGVSTVPGYMglIADADEAVKISNEIGYPVMIkasaggggkgmR----- 169
Cdd:PRK05294 108 LEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGI--AHSMEEALEVAEEIGYPVII-----------Rpsftl 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 760079558 170 ------IAWSEAEVKE----GFESSKNeaansfgdDRIFIEKFVTQPRHIEIQVLADKHGNCVYLhereCSI 231
Cdd:PRK05294 175 ggtgggIAYNEEELEEiverGLDLSPV--------TEVLIEESLLGWKEYEYEVMRDKNDNCIIV----CSI 234
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
606-666 |
1.44e-04 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 44.87 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760079558 606 GLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
603-635 |
1.66e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 39.73 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|...
gi 760079558 603 PMPGLVVKINVAEGDEVQEGQALATVEAMKMEN 635
Cdd:pfam13533 8 PVSGKVVAVNVKEGQQVKKGDVLATLDSPELQL 40
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
88-314 |
2.49e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 43.39 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 88 RMDFAAALEAAGVVFIGPPSgAIEAMGDKITSKKLAKEAGVSTVPGYmgLIADADEAVKISNEIGYPVMIKASAGGGGKG 167
Cdd:COG0189 70 GLALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVLKPLDGSGGRG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 168 MRIAWSEAEVKegfesSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLA-DkhGNCVYLHER-----ECSIQRRNQKVIEE 241
Cdd:COG0189 147 VFLVEDEDALE-----SILEALTELGSEPVLVQEFIPEEDGRDIRVLVvG--GEPVAAIRRipaegEFRTNLARGGRAEP 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760079558 242 APspfLDEATRkamgEQACALAKAVGYASAGtVEFIVDGQKnFYFLEMNTRLQVEHpvTELITGIDLVEQMIR 314
Cdd:COG0189 220 VE---LTDEER----ELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEAIAD 281
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
92-289 |
2.57e-04 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 43.91 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 92 AAALEAAGVVFigPPSGAIEAMGDKITSKKLAKEAGVSTVPgYMgLIADADEAVKISNEIGYPVMIKASaggggkGM--- 168
Cdd:COG0026 68 LEALEAEVPVR--PGPEALEIAQDRLLEKAFLAELGIPVAP-FA-AVDSLEDLEAAIAELGLPAVLKTR------RGgyd 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 169 -----RIAwSEAEVKegfessknEAANSFGDDRIFIEKFVTQPRhiEIQVLA--DKHGNCVY--LHErecSIQRRNQ--K 237
Cdd:COG0026 138 gkgqvVIK-SAADLE--------AAWAALGGGPCILEEFVPFER--ELSVIVarSPDGEVATypVVE---NVHRNGIldE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 760079558 238 VIeeAPSPfLDEATRKAMGEQACALAKAVGYasAGT--VEFIVDGQKNFYFLEM 289
Cdd:COG0026 204 SI--APAR-ISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGELLVNEI 252
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
606-666 |
2.80e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.22 E-value: 2.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760079558 606 GLVVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
608-666 |
4.93e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 43.27 E-value: 4.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760079558 608 VVKINVAEGDEVQEGQALATVEAMK--MEniLRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK11855 18 VIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
115-204 |
5.54e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.22 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 115 DKITSKKLAKEAGVStVP-GYMglIADADEAVKISNEIGYPVMIK---------ASAGGGgkgmriawSEAEVKEGFess 184
Cdd:PRK14016 214 DKELTKRLLAAAGVP-VPeGRV--VTSAEDAWEAAEEIGYPVVVKpldgnhgrgVTVNIT--------TREEIEAAY--- 279
|
90 100
....*....|....*....|
gi 760079558 185 knEAANSFGDDrIFIEKFVT 204
Cdd:PRK14016 280 --AVASKESSD-VIVERYIP 296
|
|
| BCCP |
TIGR00531 |
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ... |
613-666 |
9.14e-04 |
|
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273123 [Multi-domain] Cd Length: 155 Bit Score: 40.21 E-value: 9.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 760079558 613 VAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:TIGR00531 102 VEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
124-278 |
1.48e-03 |
|
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: 39.93 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 124 KEAGVSTvPGYMgLIADADEAVKISNEIGYPVMIKASaggggkGM-------RIAWSEAEVkegfesskNEAANSFGDDR 196
Cdd:pfam02222 1 QKLGLPT-PRFM-AAESLEELIEAGQELGYPCVVKAR------RGgydgkgqYVVRSEADL--------PQAWEELGDGP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760079558 197 IFIEKFVTQPRHIEIQVLADKHGNcVYLHERECSIQRRNQKVIEEAPSPFLDEATRKAMgEQACALAKAVGYASAGTVEF 276
Cdd:pfam02222 65 VIVEEFVPFDRELSVLVVRSVDGE-TAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQ-DIAKRLVDELGGVGVFGVEL 142
|
..
gi 760079558 277 IV 278
Cdd:pfam02222 143 FV 144
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
613-666 |
1.81e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.68 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 760079558 613 VAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
608-666 |
1.89e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.53 E-value: 1.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 760079558 608 VVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK11854 120 VTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
119-159 |
1.98e-03 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 41.26 E-value: 1.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 760079558 119 SKKLAKEAGVSTVPGYmgLIADADEAVKISNEIGYPVMIKA 159
Cdd:COG1042 493 AKALLAAYGIPVVPTR--LARSAEEAVAAAEEIGYPVVLKI 531
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
608-666 |
3.20e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 3.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 760079558 608 VVKINVAEGDEVQEGQALATVEAMKMENILRAERRGTVKKIAAAPGASLRVDDVIMEFE 666
Cdd:PRK11854 221 VTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| |
