|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 864.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKS 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEE-ALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYE-NGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAED-SETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDpAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKLGL 446
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLAL 447
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-444 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 776.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDnKKRTLELAREIGYPIMIKS 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQD-AEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:COG4770 160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY-ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAED-SETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDpARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKL 444
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-446 |
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: 727.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKS 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEE-NVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYE-NGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAED-SETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDpIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKLGL 446
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-444 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 700.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKS 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEE-AIAIARQIGYPVMLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYENG-HFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQkNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAEDSETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESAI 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1593250820 400 ARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKL 444
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQL 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 657.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKS 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEE-AKEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGEP 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 321 LRYRQQDIVLRGHAIECRINAEDS-ETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESAI 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1593250820 400 ARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKLGL 446
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 618.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKS 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEE-ALEIAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY-ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAED-SETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDpKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKLG 445
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-436 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 585.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIG-PASSLQSYLNVPAIISAAEVTDTVAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGeGKHPVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 80 PGYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIK 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEE-ALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 160 SSGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKV 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 240 VEEAPAPGITEAQRREIgerCAAA---CRSIGYRGAGTFEFLY-ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILV 315
Cdd:PRK12999 243 VEIAPAPGLSEELRERI---CEAAvklARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 316 AAGEPLR------YRQQDIVLRGHAIECRINAEDSET-FLPCPGKITEFHAPGGPGVRMET-HIYSGYTVPRYYDSMIGK 387
Cdd:PRK12999 320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPANnFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1593250820 388 LITHGEDRESAIARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGAN 436
Cdd:PRK12999 400 LTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYT 448
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-441 |
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: 573.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIG-PASSLQSYLNVPAIISAAEVTDTVAIH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGeGKGPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 80 PGYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDnKKRTLELAREIGYPIMIK 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDD-LEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 160 SSGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKV 239
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 240 VEEAPAPGITEAQRREIgerCAAA---CRSIGYRGAGTFEFLY-ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILV 315
Cdd:COG1038 242 VEIAPAPNLDEELREAI---CEAAvklAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 316 AAGEPLR------YRQQDIVLRGHAIECRINAEDSET-FLPCPGKITEFHAPGGPGVRMET-HIYSGYTVPRYYDSMIGK 387
Cdd:COG1038 319 AEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPANnFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1593250820 388 LITHGEDRESAIARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLE 441
Cdd:COG1038 399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
2-441 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 548.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 2 IEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 82 YGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDnKKRTLELAREIGYPIMIKSS 161
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVAS-LDAALEVAARIGYPLMIKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 162 GGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMgNAIHLGERDCSMQRRHQKVVE 241
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 242 EAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY--ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAEDSE-TFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPLrDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLE 441
Cdd:PRK12833 403 LARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 545.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 2 IEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 82 YGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKRTlELAREIGYPIMIKSS 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAK-KIAKEIGYPVILKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 162 GGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVVE 241
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 242 EAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYE-NGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGEP 320
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 321 LrYRQQDIVLRGHAIECRINAEDSETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESAIA 400
Cdd:PRK08462 323 L-PSQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1593250820 401 RMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKK 443
Cdd:PRK08462 402 KMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-441 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 536.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPaSSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA-DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKS 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDE-ALAEAERIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYE-NGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAEDSET-FLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPKNdFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLE 441
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-445 |
7.65e-171 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 488.17 E-value: 7.65e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 1 MIEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGpASSLQSYLNVPAIISAAEVTDTVAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIG-TDPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDNKKRTLELAREIGYPIMIKS 160
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY-ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYRQQDIVLRGHAIECRINAED-SETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESA 398
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENvWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1593250820 399 IARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEKKLG 445
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-442 |
4.51e-170 |
|
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: 509.19 E-value: 4.51e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 3 EKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHPGY 82
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 83 GFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSdgPIDDNKKRTLELAREIGYPIMIKSSG 162
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT--GLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 163 GGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVVEE 242
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 243 APAPGITEAQRREIgerCAAA---CRSIGYRGAGTFEFLY--ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAA 317
Cdd:TIGR02712 240 TPAPNLPPETRQAL---LAAAerlGEAVNYRSAGTVEFIYdeARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 318 GEPLRYRQ--QDIVLRGHAIECRINAED-SETFLPCPGKITEFHAPGgpGVRMETHIYSGYTVPRYYDSMIGKLITHGED 394
Cdd:TIGR02712 317 GELPDFASlnISLTPRGAAIEARVYAENpAKNFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1593250820 395 RESAIARMSNALRETVIDGINTNIKLQRSIMKDGAFLAGGANIHYLEK 442
Cdd:TIGR02712 395 REDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-433 |
5.92e-160 |
|
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: 481.25 E-value: 5.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 4 KVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSL---QSYLNVPAIISAAEVTDTVAIHP 80
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFLSENADFAERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSDGPIDDnKKRTLELAREIGYPIMIKS 160
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPET-MEEVLDFAAAIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 161 SGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVV 240
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 241 EEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY-ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGE 319
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 320 PLRYR------QQDIVLRGHAIECRINAEDSE-TFLPCPGKITEFHAPGGPGVRMET-HIYSGYTVPRYYDSMIGKLITH 391
Cdd:TIGR01235 320 SLPTPqlgvpnQEDIRTNGYAIQCRVTTEDPAnNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1593250820 392 GEDRESAIARMSNALRETVIDGINTNIKLQRSIMKDGAFLAG 433
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
2.26e-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: 275.34 E-value: 2.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 115 DKVSAIAAMKAAGVPCVPGSDGPIDDNKKrTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFN 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEE-ALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 195 NDMVYMEKYLENPRHIEFQLLADQMGNAIHLGERDCSMQRRHQKVVEEAPAPGITEAQRREIGERCAAACRSIGYRGAGT 274
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1593250820 275 FEFLYE--NGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGEPLR 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-320 |
1.94e-69 |
|
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: 221.28 E-value: 1.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 62 NVPAIISAAEvtdtvAIHPGYGF---LSENAD----FAERVERSGFIfiGPRPETIRLMGDKVSAIAAMKAAGVPcVPGS 134
Cdd:COG0439 1 DIDAIIAAAA-----ELARETGIdavLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 135 DgPIDDnKKRTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLLNAIALTKAEAAAAFNNDMVYMEKYLENpRHIEFQL 214
Cdd:COG0439 73 A-LVDS-PEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 215 LADQmGNAIHlgerdCSMQRRHQK---VVE---EAPAPgITEAQRREIGERCAAACRSIGY-RGAGTFEFLY-ENGHFYF 286
Cdd:COG0439 150 LVRD-GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYL 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 1593250820 287 IEMNTRVQVEH--PVTEMVTGVDIVKEQILVAAGEP 320
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
1.38e-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: 197.71 E-value: 1.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 2 IEKVLIANRGEIALRILRACRELGIKTVAVHSEADRDLKHVLLADESVCIGPASSLQSYLNVPAIISAAEVTDTVAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1593250820 82 YGFLSENADFAERVERSGFIFIGPRPET 109
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-441 |
3.66e-55 |
|
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: 178.38 E-value: 3.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 336 ECRINAED-SETFLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESAIARMSNALRETVIDGI 414
Cdd:smart00878 1 ECRINAEDpANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 1593250820 415 NTNIKLQRSIMKDGAFLAGGANIHYLE 441
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-442 |
1.69e-52 |
|
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: 171.52 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 336 ECRINAEDSET-FLPCPGKITEFHAPGGPGVRMETHIYSGYTVPRYYDSMIGKLITHGEDRESAIARMSNALRETVIDGI 414
Cdd:pfam02785 1 EARIYAEDPDNnFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 1593250820 415 NTNIKLQRSIMKDGAFLAGGANIHYLEK 442
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
92-322 |
2.00e-12 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 69.26 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 92 AERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSdgpIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRV 171
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWK---TATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEI 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 172 VHSEATLL----NAIALTKaeaaaafnNDMVYMEKYLENPRHIEFQLLAD-----------QMGNA-IHLGERDCSMqrr 235
Cdd:TIGR01369 723 VYNEEELRryleEAVAVSP--------EHPVLIDKYLEDAVEVDVDAVSDgeevlipgimeHIEEAgVHSGDSTCVL--- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 236 hqkvveeaPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILV 315
Cdd:TIGR01369 792 --------PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRV 863
|
....*..
gi 1593250820 316 AAGEPLR 322
Cdd:TIGR01369 864 MLGKKLE 870
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-321 |
1.19e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 66.92 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 92 AERVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSdgpIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRV 171
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL---TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 172 VHSEATLlnaialtkaeaaaafnndmvymEKYLENPRHIEFQLLADQM-------------GNAIHLG---Erdcsmqrr 235
Cdd:PRK12815 724 VYDEPAL----------------------EAYLAENASQLYPILIDQFidgkeyevdaisdGEDVTIPgiiE-------- 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 236 HqkvVEEA-----------PAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLYENGHFYFIEMNTRVQVEHPVTEMVT 304
Cdd:PRK12815 774 H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKAT 850
|
250
....*....|....*..
gi 1593250820 305 GVDIVKEQILVAAGEPL 321
Cdd:PRK12815 851 GVPLAKLATKVLLGKSL 867
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
4-321 |
6.86e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 60.33 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 4 KVLIANRGEIALRILRACRELGIKTVAVHSEAD------RDLKHVLladesVCIGPASSLQSYLNvpAIISAAE------ 71
Cdd:COG3919 7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLgpaarsRYVDEVV-----VVPDPGDDPEAFVD--ALLELAErhgpdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 72 ---VTDTVAIhpgygFLSENADFAERversGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPC----VPGSDGPIDdnkkr 144
Cdd:COG3919 80 lipTGDEYVE-----LLSRHRDELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVPVpktvVLDSADDLD----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 145 tlELAREIGYPIMIKSSGGGGGRG--------MRVVHSEATLLNAIAltkaeAAAAFNNDMVYMEkYLENPRHIEFQL-- 214
Cdd:COG3919 146 --ALAEDLGFPVVVKPADSVGYDElsfpgkkkVFYVDDREELLALLR-----RIAAAGYELIVQE-YIPGDDGEMRGLta 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 215 LADQMGNAIHLgerdCSMQRRHQKVVEEAPAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY--ENGHFYFIEMNTR 292
Cdd:COG3919 218 YVDRDGEVVAT----FTGRKLRHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPR 293
|
330 340 350
....*....|....*....|....*....|.
gi 1593250820 293 VQVEHPvteMVT--GVDIVKEQILVAAGEPL 321
Cdd:COG3919 294 FWRSLY---LATaaGVNFPYLLYDDAVGRPL 321
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
92-322 |
3.41e-07 |
|
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: 52.57 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 92 AERVERSGFI----FIGPRPETIRLMGDKVSAIAAMKAAGVPCVPGSdgpIDDNKKRTLELAREIGYPIMIKSSGGGGGR 167
Cdd:COG0458 87 AVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKSG---TATSVEEALAIAEEIGYPVIVRPSYVLGGR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 168 GMRVVHSEATLLNAIALTKAEAaaafNNDMVYMEKYLENPRHIEFQLLADQMGNAIhLGerdCSMQrrHqkvVEEA---- 243
Cdd:COG0458 164 GMGIVYNEEELEEYLERALKVS----PDHPVLIDESLLGAKEIEVDVVRDGEDNVI-IV---GIME--H---IEPAgvhs 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 244 -------PAPGITEAQR---REIGERCAaacRSIGYRGAGTFEFLYENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQI 313
Cdd:COG0458 231 gdsicvaPPQTLSDKEYqrlRDATLKIA---RALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAA 307
|
....*....
gi 1593250820 314 LVAAGEPLR 322
Cdd:COG0458 308 KLALGYTLD 316
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
77-337 |
5.06e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 48.34 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 77 AIHPGY----GFLSENADfaeRVERSGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCvPGSDGPIDDNKKRTLELAREI 152
Cdd:PRK12767 72 LLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPT-PKSYLPESLEDFKAALAKGEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 153 GYPIMIKSSGGGGGRGMRVVHSEATLLNAIAltkaeaaaaFNNDMVYMEkYLEnprHIEFQL--LADQMGNAIHlgerdc 230
Cdd:PRK12767 148 QFPLFVKPRDGSASIGVFKVNDKEELEFLLE---------YVPNLIIQE-FIE---GQEYTVdvLCDLNGEVIS------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 231 SMQRRHQKVVEEAPAPGITEAqRREIGERCAAACRSIGYRGAGTFEFLYENGHFYFIEMNTRVQVEHPVTEMVtGVD--- 307
Cdd:PRK12767 209 IVPRKRIEVRAGETSKGVTVK-DPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPLSYMA-GANepd 286
|
250 260 270
....*....|....*....|....*....|.
gi 1593250820 308 -IVKEQILVAAGEPLRYRQQDIVLRGHAIEC 337
Cdd:PRK12767 287 wIIRNLLGGENEPIIGEYKEGLYMRRYDEVV 317
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-291 |
8.84e-05 |
|
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: 43.46 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 123 MKAAGVPCVP----GSDGPIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLLNAIALtkaeaAAAFNNDmV 198
Cdd:pfam07478 2 LKAAGLPVVPfvtfTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEE-----AFQYDEK-V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 199 YMEKYLENpRHIEFQLLADQMGNAIHLGER--DCSMQRRHQKVVEEA-----PApGITEAQRREIGERCAAACRSIGYRG 271
Cdd:pfam07478 76 LVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALGCRG 153
|
170 180
....*....|....*....|.
gi 1593250820 272 AGTFE-FLYENGHFYFIEMNT 291
Cdd:pfam07478 154 LARVDfFLTEDGEIVLNEVNT 174
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
102-291 |
1.23e-04 |
|
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: 43.94 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 102 FIGPRPETIRLMGDKVSAIAAMKAAGVPCVPG---SDGPIDDnkkrTLELAREIGYPIMIK-----SSgggggRGMRVVH 173
Cdd:COG1181 82 YTGSGVLASALAMDKALTKRVLAAAGLPTPPYvvlRRGELAD----LEAIEEELGLPLFVKparegSS-----VGVSKVK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 174 SEATLLNAIALtkaeaaaAFNND---MVymEKYLEnPRHIEFQLLADQMGNAIHLGE-------RDcsmqrRHQK----- 238
Cdd:COG1181 153 NAEELAAALEE-------AFKYDdkvLV--EEFID-GREVTVGVLGNGGPRALPPIEivpengfYD-----YEAKytdgg 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1593250820 239 VVEEAPAPgITEAQRREIGERCAAACRSIGYRGAGTFEFLY-ENGHFYFIEMNT 291
Cdd:COG1181 218 TEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
110-321 |
1.80e-04 |
|
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: 44.22 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 110 IRLMGDKVSAI----------AAMKAAGVPcVPGSDgpIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLL 179
Cdd:TIGR01369 112 VEVLGTPVEAIkkaedrelfrEAMKEIGEP-VPESE--IAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 180 ----NAIALTKAeaaaafnnDMVYMEKYLENPRHIEFQLLADQMGNAI-------------HLGErdcSMqrrhqkVVee 242
Cdd:TIGR01369 189 eiaeRALSASPI--------NQVLVEKSLAGWKEIEYEVMRDSNDNCItvcnmenfdpmgvHTGD---SI------VV-- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 243 APAPGITEAQRREIGERCAAACRSIGYRGAGTFEFLY--ENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGEP 320
Cdd:TIGR01369 250 APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYT 329
|
.
gi 1593250820 321 L 321
Cdd:TIGR01369 330 L 330
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-311 |
2.21e-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: 43.01 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 16 RILRACRELGIktvavhseadrDLKHVLLADESVCIGPASSLQSYLNVPAIisaaevtDTV---AIHPGYGFlsenaDFA 92
Cdd:COG0189 18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSEF-------DAVlprIDPPFYGL-----ALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 93 ERVERSGFIFIgPRPETIRLMGDKVSAIAAMKAAGVPCVPGSdgpIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRVV 172
Cdd:COG0189 75 RQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTL---VTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 173 HSEATLLNAIALtkaeaAAAFNNDMVYMEKYLENPRHIEFQ-LLADqmGNAIHlgerdcSMQRRHQK-----------VV 240
Cdd:COG0189 151 EDEDALESILEA-----LTELGSEPVLVQEFIPEEDGRDIRvLVVG--GEPVA------AIRRIPAEgefrtnlarggRA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1593250820 241 EEAPAPgiteaqrREIGERCAAACRSIGYRGAGtFEFLYENGHFYFIEMNTRVQVEHpvTEMVTGVDIVKE 311
Cdd:COG0189 218 EPVELT-------DEERELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
104-321 |
2.67e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 43.61 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 104 GPRPETIRLMGDKVSAIAAMKAAGVPCVPGSdgpIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLL---- 179
Cdd:PLN02735 691 GTSPDSIDAAEDRERFNAILNELKIEQPKGG---IARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKtyle 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 180 NAIALTKAEAaaafnndmVYMEKYLENPRHIEFQLLADQMGN-------------AIHLGERDCSMqrrhqkvveeaPAP 246
Cdd:PLN02735 768 TAVEVDPERP--------VLVDKYLSDATEIDVDALADSEGNvviggimehieqaGVHSGDSACSL-----------PTQ 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593250820 247 GITEAQRREIGERCAAACRSIGYRGAGTFEF-LYENGHFYFIEMNTRVQVEHPVTEMVTGVDIVKEQILVAAGEPL 321
Cdd:PLN02735 829 TIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSL 904
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
110-293 |
2.96e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 43.42 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 110 IRLMGDKVSAI----------AAMKAAGVPcVPGSDgpIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLL 179
Cdd:PRK12815 113 VELLGTNIEAIqkgedrerfrALMKELGEP-VPESE--IVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 180 NAIalTKAEAAAAFNNDMVymEKYLENPRHIEFQLLADQMGN-------------AIHLGErdcSMqrrhqkVVeeAPAP 246
Cdd:PRK12815 190 QLF--KQGLQASPIHQCLL--EESIAGWKEIEYEVMRDRNGNcitvcnmenidpvGIHTGD---SI------VV--APSQ 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1593250820 247 GITEAQRREIGERCAAACRSIGYRGAGTFEFL--YENGHFYFIEMNTRV 293
Cdd:PRK12815 255 TLTDDEYQMLRSASLKIISALGVVGGCNIQFAldPKSKQYYLIEVNPRV 303
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
115-291 |
3.26e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 42.41 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 115 DKVSAIAAMKAAGVPCVPGSDGPIDDNkkrTLELAREIGYPIMIK-----SSgggggRGMRVVHSEATLLNAIALtkaea 189
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREED---LLAAIDKLGLPLVVKparegSS-----VGVSKVKEEDELQAALEL----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 190 AAAFNNDMVyMEKYLENPrhiEFQ--LLADQM---------------------GNAIHLgerdCsmqrrhqkvveeaPAp 246
Cdd:PRK01372 165 AFKYDDEVL-VEKYIKGR---ELTvaVLGGKAlpvieivpagefydyeakylaGGTQYI----C-------------PA- 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1593250820 247 GITEAQRREIGERCAAACRSIGYRGAGTFEFLY-ENGHFYFIEMNT 291
Cdd:PRK01372 223 GLPAEIEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYLLEVNT 268
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
3-360 |
4.91e-04 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 42.21 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 3 EKVLIAnrGeIALRIL-RACRELGIKTVAVHSEADRDLKHvlLADESVCIGPASSLQSYLNVPAIIS-AAEVTDTVAIHP 80
Cdd:COG2232 5 PDLLIA--G-FSARALaQSARRAGYRVYAVDLFADLDTRA--LAERWVRLDAESCGFDLEDLPAALLeLAAADDPDGLVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 81 GYGFlsenADFAERVER--SGFIFIGPRPETIRLMGDKVSAIAAMKAAGVPCVP-GSDGPIDDnkkrtlelareigYPIM 157
Cdd:COG2232 80 GSGF----ENFPELLERlaRRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPEtRFEPPPDP-------------GPWL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 158 IKSSGGGGGRGMRVVHSEAtllnaialtkaeaaaaFNNDMVYMEKYLENpRHIEFQLLADQmGNAIHLGerdCSMQrrhq 237
Cdd:COG2232 143 VKPIGGAGGWHIRPADSEA----------------PPAPGRYFQRYVEG-TPASVLFLADG-SDARVLG---FNRQ---- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 238 kVVEEAPAPG-----------ITEAQRREIGERCAAACRSIGYRGAGTFEFLYENGHFYFIEMNTRVQVEHPVTEMVTGV 306
Cdd:COG2232 198 -LIGPAGERPfryggnigplaLPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGG 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593250820 307 DIVKEQILVAAGE-PLRYRQQDIVLRGHAI-----ECRINAEDSETF----LPCPGKITEFHAP 360
Cdd:COG2232 277 NLFDAHLRACRGElPEVPRPKPRRVAAKAIlyaprDLTIPDDLSWPPwvadIPAPGTRIEKGEP 340
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
107-412 |
4.82e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 39.45 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 107 PETIRLMGDKVSAIAAMKAAGVPcVPgsDGPIDDNKKRTLELAREIGYPIMIKSSGGGGGRGMRVVHSEATLLNAIALTK 186
Cdd:PRK02186 99 TEAIRTCRDKKRLARTLRDHGID-VP--RTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 187 AEAAAAFnndmvYMEKYLENPrhiEF--QLLADQMGNAI------HLGERDCSMQRRHqkvveEAPAPgITEAQRREIGE 258
Cdd:PRK02186 176 RAGTRAA-----LVQAYVEGD---EYsvETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAP-LSAPQRERIVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 259 RCAAACRSIGYR-GAGTFEFLYENGHFYFIEMNTR-------VQVEHpvtemVTGVDIVKEQILVAAGEPlryrqQDIVL 330
Cdd:PRK02186 242 TVLRALDAVGYAfGPAHTELRVRGDTVVIIEINPRlaggmipVLLEE-----AFGVDLLDHVIDLHLGVA-----AFADP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593250820 331 ---RGHAIECRINAEDSE----TFLPCP---GKITEFHAPGGPG--VRMETHiysgytvpryYDSMIGKLITHGEDRESA 398
Cdd:PRK02186 312 takRYGAIRFVLPARSGVlrglLFLPDDiaaRPELRFHPLKQPGdaLRLEGD----------FRDRIAAVVCAGDHRDSV 381
|
330
....*....|....
gi 1593250820 399 IARMSNALRETVID 412
Cdd:PRK02186 382 AAAAERAVAGLSID 395
|
|
| |
