|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-449 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 912.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIKA 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKLGLQEK 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
|
|
| 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: 807.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGpLTDDMDANRAHAKRIGYPVIIKA 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKLGLQE 448
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMGE 449
|
|
| 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: 779.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTDDMDAnRAHAKRIGYPVIIKA 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEA-LAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SgggggrgmrvvRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:COG4770 160 SaggggkgmrvvRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDPaRGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKL 444
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
|
|
| 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: 689.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTDDMDAnRAHAKRIGYPVIIKA 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEA-IAIARQIGYPVMLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGE-FYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVAI 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1943962720 400 ARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKL 444
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQL 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-449 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 668.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTDDMDANRAhAKRIGYPVIIKA 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEI-AEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 321 LSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVAI 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943962720 400 ARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKLGLQEK 449
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEE 449
|
|
| 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: 614.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTDDMDANRAhAKRIGYPVIIKA 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEI-AKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPkNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKLG 445
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-433 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 575.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 80 PGYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIK 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPI-DDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 160 ASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 240 VEEAPAPGITPELRRYIgerCAKA---CVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:PRK12999 243 VEIAPAPGLSEELRERI---CEAAvklARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 316 AAGQPLS------IKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGK 387
Cdd:PRK12999 320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPaNNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1943962720 388 LICYGESRDVAIARMKNALQELIIDGIKTNVDLQMRIMSDENFQHG 433
Cdd:PRK12999 400 LTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG 445
|
|
| 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: 564.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 2 LDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 82 YGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIKAS 161
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVV-ASLDAALEVAARIGYPLMIKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 162 GGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQgNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 242 EAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPlRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLE 441
Cdd:PRK12833 403 LARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-433 |
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: 559.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAIH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGpVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 80 PGYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIK 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPV-DDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 160 ASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 240 VEEAPAPGITPELRRYIGE---RCAKAcvdIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:COG1038 242 VEIAPAPNLDEELREAICEaavKLAKA---VGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 316 AAGQPLS------IKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRW-ESHIYAGYTVPPYYDSMIGK 387
Cdd:COG1038 319 AEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPaNNFMPDTGRITAYRSAGGFGIRLdGGNAYTGAVITPYYDSLLVK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1943962720 388 LICYGESRDVAIARMKNALQELIIDGIKTNVDLQMRIMSDENFQHG 433
Cdd:COG1038 399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAG 444
|
|
| 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: 550.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 2 LDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 82 YGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTdDMDANRAHAKRIGYPVIIKAS 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALK-SYEEAKKIAKEIGYPVILKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 162 GGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 242 EAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 321 LSiKQDEVVVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVAIA 400
Cdd:PRK08462 323 LP-SQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1943962720 401 RMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKK 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: 546.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIKA 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNL-ADLDEALAEAERIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPkNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLE 441
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-445 |
6.83e-176 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 500.88 E-value: 6.83e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP-IKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTDDMDANRAHAKRIGYPVIIKA 160
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIKQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVA 398
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVwKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1943962720 399 IARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEKKLG 445
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-442 |
2.33e-164 |
|
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: 494.55 E-value: 2.33e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 3 DKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGY 82
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 83 GFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSdgPLTDDMDANRAHAKRIGYPVIIKASG 162
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT--GLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 163 GGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVVEE 242
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 243 APAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdeARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 321 LSIKQ--DEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGgfGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDV 397
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPaKNFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1943962720 398 AIARMKNALQELIIDGIKTNVDLQMRIMSDENFQHGGTNIHYLEK 442
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-433 |
5.76e-161 |
|
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: 483.95 E-value: 5.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 4 KIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPS---VKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDlgpIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIKA 160
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPP-ETMEEVLDFAAAIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 320 PLSIK------QDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGKLICY 391
Cdd:TIGR01235 320 SLPTPqlgvpnQEDIRTNGYAIQCRVTTEDPaNNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1943962720 392 GESRDVAIARMKNALQELIIDGIKTNVDLQMRIMSDENFQHG 433
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
2.51e-97 |
|
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: 290.75 E-value: 2.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 115 DKVSAITAMKKAGVPTVPGSDGPLtDDMDANRAHAKRIGYPVIIKASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFN 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPV-ETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 195 NDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGT 274
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1943962720 275 FEFLFE--NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLS 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-320 |
1.43e-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: 221.67 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 62 NIPAIISA-AEITGAVAIHpgyGFLSENAN----FAEQVERSGFIfiGPKADTIRLMGDKVSAITAMKKAGVPtVPGSDg 136
Cdd:COG0439 1 DIDAIIAAaAELARETGID---AVLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGFA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 137 pLTDDMDANRAHAKRIGYPVIIKASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFNNDMVYMEKYLENpRHIEIQVLA 216
Cdd:COG0439 74 -LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 217 DgQGNAIYlaerdCSMQRRHQK---VVE---EAPAPgITPELRRYIGERCAKACVDIGY-RGAGTFEFLF-ENGEFYFIE 288
Cdd:COG0439 152 R-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIE 224
|
250 260 270
....*....|....*....|....*....|....
gi 1943962720 289 MNTRIQVEH--PVTEMITGVDLIKEQLRIAAGQP 320
Cdd:COG0439 225 INARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
1.03e-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: 193.09 E-value: 1.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 2 LDKIVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1943962720 82 YGFLSENANFAEQVERSGFIFIGPKADT 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 |
4.19e-58 |
|
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: 186.08 E-value: 4.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVAIARMKNALQELIIDGI 414
Cdd:smart00878 1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 1943962720 415 KTNVDLQMRIMSDENFQHGGTNIHYLE 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 |
8.23e-56 |
|
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: 180.38 E-value: 8.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGESRDVAIARMKNALQELIIDGI 414
Cdd:pfam02785 1 EARIYAEDPdNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 1943962720 415 KTNVDLQMRIMSDENFQHGGTNIHYLEK 442
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
90-322 |
4.50e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 71.54 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 90 NFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSdgpLTDDMDANRAHAKRIGYPVIIKASGGGGGRGM 169
Cdd:PRK12815 645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL---TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGM 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 170 RVVRSDAELAQSIsmtkaeAKAAFNNDMVYMEKYLENpRHIEIQVLADgqGNAIYLA---ErdcsmqrrHqkvVEEA--- 243
Cdd:PRK12815 722 AVVYDEPALEAYL------AENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiE--------H---IEQAgvh 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 244 --------PAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:PRK12815 782 sgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861
|
....*..
gi 1943962720 316 AAGQPLS 322
Cdd:PRK12815 862 LLGKSLA 868
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
90-321 |
9.40e-13 |
|
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: 70.41 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 90 NFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGsdGPLTDDMDANRAhAKRIGYPVIIKASGGGGGRGM 169
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEF-ASEIGYPVLVRPSYVLGGRAM 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 170 RVVRSDAELAQSISmtkaEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIY-LAErdcsmqrrHqkvVEEA----- 243
Cdd:TIGR01369 721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPgIME--------H---IEEAgvhsg 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 244 ------PAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAA 317
Cdd:TIGR01369 786 dstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865
|
....
gi 1943962720 318 GQPL 321
Cdd:TIGR01369 866 GKKL 869
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
84-321 |
3.53e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 55.32 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 84 FLSENANFAEQversGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTvpgsdgPLT---DDMDANRAHAKRIGYPVIIKA 160
Cdd:COG3919 90 LLSRHRDELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVPV------PKTvvlDSADDLDALAEDLGFPVVVKP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 161 SGGGGGRGMRVVR--------SDAELAQSIsmtkAEAKAAFNNDMVymEKYLENPRHIE--IQVLADGQGNAIYLaerdC 230
Cdd:COG3919 160 ADSVGYDELSFPGkkkvfyvdDREELLALL----RRIAAAGYELIV--QEYIPGDDGEMrgLTAYVDRDGEVVAT----F 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 231 SMQRRHQK--------VVEEAPAPGITPELRRYIGErcakacvdIGYRGAGTFEFLF--ENGEFYFIEMNTRI--QVEHP 298
Cdd:COG3919 230 TGRKLRHYppaggnsaARESVDDPELEEAARRLLEA--------LGYHGFANVEFKRdpRDGEYKLIEINPRFwrSLYLA 301
|
250 260
....*....|....*....|...
gi 1943962720 299 VtemITGVDLIKEQLRIAAGQPL 321
Cdd:COG3919 302 T---AAGVNFPYLLYDDAVGRPL 321
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
90-292 |
1.59e-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: 53.34 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 90 NFAEQVERSGFI----FIGPKADTIRLMGDKVSAITAMKKAGVPTVPGsdGPLTDDMDANRAhAKRIGYPVIIKASGGGG 165
Cdd:COG0458 85 NLAVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAI-AEEIGYPVIVRPSYVLG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 166 GRGMRVVRSDAELAQSIsmtkAEAKAAFNNDMVYMEKYLENPRHIEIQVLADGQGNAIYLaerdCSMQrrHqkvVEEA-- 243
Cdd:COG0458 162 GRGMGIVYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgv 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943962720 244 ---------PAPGITPE----LRRYiGERCAKAcvdIGYRGAGTFEFLFENGEFYFIEMNTR 292
Cdd:COG0458 229 hsgdsicvaPPQTLSDKeyqrLRDA-TLKIARA---LGVVGLCNIQFAVDDGRVYVIEVNPR 286
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-290 |
2.06e-05 |
|
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: 46.09 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 16 RILRACKELGIktvavhstadrDLKHVLLADETVCIGPAPSVKSYLNIP---AIISAAeitgavaIHPGYGFlsenaNFA 92
Cdd:COG0189 18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSefdAVLPRI-------DPPFYGL-----ALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 93 EQVERSGFIFIGPkADTIRLMGDKVSAITAMKKAGVPTvpgsdgP---LTDDMDANRAHAKRIGYPVIIKAsgggggrgm 169
Cdd:COG0189 75 RQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV------PptlVTRDPDDLRAFLEELGGPVVLKP--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 170 rvvrsdAELAQSISMTKAEAKAAFN----------NDMVYMEKYLENPRHIEIQVLA-DGQgnaiYLAerdcSMQRRHQK 238
Cdd:COG0189 139 ------LDGSGGRGVFLVEDEDALEsilealtelgSEPVLVQEFIPEEDGRDIRVLVvGGE----PVA----AIRRIPAE 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943962720 239 -----------VVEEAPapgITPELRRyIGERCAKAcVDIGYrgAGtFEFLFENGEFYFIEMN 290
Cdd:COG0189 205 gefrtnlarggRAEPVE---LTDEERE-LALRAAPA-LGLDF--AG-VDLIEDDDGPLVLEVN 259
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
5-321 |
1.22e-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: 44.60 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 5 IVIANRGEIALRILRACK---ELGIKTVAVHS---TADRDLKhvlLADET--VCIGPApsvksylNIPAIISAAEITGav 76
Cdd:TIGR01369 17 IVIGQAAEFDYSGSQACKalkEEGYRVILVNSnpaTIMTDPE---MADKVyiEPLTPE-------AVEKIIEKERPDA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 77 aIHPGYGflSENA-NFAEQVERSGFIfigpKADTIRLMGDKVSAI----------TAMKKAGVPtVPGSDgpLTDDMDAN 145
Cdd:TIGR01369 85 -ILPTFG--GQTAlNLAVELEESGVL----EKYGVEVLGTPVEAIkkaedrelfrEAMKEIGEP-VPESE--IAHSVEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 146 RAHAKRIGYPVIIKASGGGGGRGMRVVRSDAELaqsismtKAEAKAAFNNDM---VYMEKYLENPRHIEIQVLADGQGNA 222
Cdd:TIGR01369 155 LAAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL-------KEIAERALSASPinqVLVEKSLAGWKEIEYEVMRDSNDNC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 223 IYLaerdCSMQR-----RHQK---VVeeAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTR 292
Cdd:TIGR01369 228 ITV----CNMENfdpmgVHTGdsiVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPR 301
|
330 340
....*....|....*....|....*....
gi 1943962720 293 IQVEHPVTEMITGVDLIKEQLRIAAGQPL 321
Cdd:TIGR01369 302 VSRSSALASKATGYPIAKVAAKLAVGYTL 330
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-291 |
1.28e-04 |
|
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: 43.07 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 123 MKKAGVPTVP----GSDGPLTDDMDANRAHAKRIGYPVIIKAsgggggrgmrvvrsdAELAQSISMTKAEA--------K 190
Cdd:pfam07478 2 LKAAGLPVVPfvtfTRADWKLNPKEWCAQVEEALGYPVFVKP---------------ARLGSSVGVSKVESreelqaaiE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 191 AAFNND-MVYMEKYLENpRHIEIQVLADGQGNAIYLAER--DCSMQRRHQKVVEEA-----PApGITPELRRYIGERCAK 262
Cdd:pfam07478 67 EAFQYDeKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALK 144
|
170 180 190
....*....|....*....|....*....|
gi 1943962720 263 ACVDIGYRGAGTFE-FLFENGEFYFIEMNT 291
Cdd:pfam07478 145 AYKALGCRGLARVDfFLTEDGEIVLNEVNT 174
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
152-291 |
1.68e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 43.27 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 152 IGYPVIIKASGGGGGRGMRVVRSDAELAQSIsmtKAEAKaafNNDMVYMEKYLENpRHIEIQVLADGQGNAIyLAERDCS 231
Cdd:PRK14571 124 LGYPCVVKPRREGSSIGVFICESDEEFQHAL---KEDLP---RYGSVIVQEYIPG-REMTVSILETEKGFEV-LPILELR 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943962720 232 MQRRHQKVVEE---------APAPgITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNT 291
Cdd:PRK14571 196 PKRRFYDYVAKytkgetefiLPAP-LNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINT 263
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
115-291 |
2.57e-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: 42.79 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 115 DKVSAITAMKKAGVPTVPGSDGPLTDDMDANRAHAKrIGYPVIIKASgggggrgmrvvRSDAELAQSISMTKAEAKAAFN 194
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEE-LGLPLFVKPA-----------REGSSVGVSKVKNAEELAAALE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 195 NDMVY-----MEKYLEnPRHIEIQVLADGQGNA-----I------------YLAErdcsmqrrhqKVVEEAPAPgITPEL 252
Cdd:COG1181 163 EAFKYddkvlVEEFID-GREVTVGVLGNGGPRAlppieIvpengfydyeakYTDG----------GTEYICPAR-LPEEL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1943962720 253 RRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:COG1181 231 EERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
68-412 |
1.06e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 41.37 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 68 SAAEITGAVAIHPGY-GFLSENANFAEQVERSGFIFIGPKADT--IRLMGDKVSAITAMKKAGVPtVPGSDGpLTDDMDA 144
Cdd:PRK02186 57 DPDRIHRFVSSLDGVaGIMSSSEYFIEVASEVARRLGLPAANTeaIRTCRDKKRLARTLRDHGID-VPRTHA-LALRAVA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 145 NRAHAKrIGYPVIIKASGGGGGRGMRVVRSDAE-LAQSISMTKAEAKAAFnndmvyMEKYLENPRHiEIQVLADGQGNAI 223
Cdd:PRK02186 135 LDALDG-LTYPVVVKPRMGSGSVGVRLCASVAEaAAHCAALRRAGTRAAL------VQAYVEGDEY-SVETLTVARGHQV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 224 ------YLAERDCSMQRRHqkvveEAPAPGITPELRRYigERCAKACVD-IGYR-GAGTFEFLFENGEFYFIEMNTR--- 292
Cdd:PRK02186 207 lgitrkHLGPPPHFVEIGH-----DFPAPLSAPQRERI--VRTVLRALDaVGYAfGPAHTELRVRGDTVVIIEINPRlag 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 293 --IQVehpVTEMITGVDLIKEQLRIAAGQ-----PLSIKQDEVVVRGHAVECRINAEDpntFLPSP---GKITRFH---A 359
Cdd:PRK02186 280 gmIPV---LLEEAFGVDLLDHVIDLHLGVaafadPTAKRYGAIRFVLPARSGVLRGLL---FLPDDiaaRPELRFHplkQ 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1943962720 360 PGGfGVRWESHiyagytvppyYDSMIGKLICYGESRDVAIARMKNALQELIID 412
Cdd:PRK02186 354 PGD-ALRLEGD----------FRDRIAAVVCAGDHRDSVAAAAERAVAGLSID 395
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
101-292 |
1.31e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 40.77 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 101 IFiGPKADTIRLMGDKVSAITAMKKAGVPTvpgSDGPLTDDMDANRAHAKRIGYPVIIKASgggggrgmrvvrsdaELAQ 180
Cdd:COG0151 89 VF-GPSKAAAQLEGSKAFAKEFMARYGIPT---AAYRVFTDLEEALAYLEEQGAPIVVKAD---------------GLAA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 181 S----ISMTKAEAKAAFnNDM------------VYMEKYLENPrhiE--IQVLADGQgNAIYLAE-RDcsmqrrHqKVVE 241
Cdd:COG0151 150 GkgvvVAETLEEALAAV-DDMladgkfgdagarVVIEEFLEGE---EasLFALTDGK-TVLPLPTaQD------H-KRAG 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943962720 242 E-------------APAPGITPELRRYIGERCAKACVD------IGYRGagtfeFLF-----ENGEFYFIEMNTR 292
Cdd:COG0151 218 DgdtgpntggmgaySPAPVVTEELLEKIMEEIIEPTVAgmaaegIPYRG-----VLYaglmiTADGPKVLEFNVR 287
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
115-291 |
1.35e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.48 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 115 DKVSAITAMKKAGVPTVPGSdgpLTDDMDANRAHAKRIGYPVIIKASgggggrgmrvvrsdAElAQSISMTKAEAKAAFN 194
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWI---VLTREEDLLAAIDKLGLPLVVKPA--------------RE-GSSVGVSKVKEEDELQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 195 N---------DMVYMEKYLENPrhiEIQV-LADGQG---------------NAIYLAErdcsmqrrhqKVVEEAPApGIT 249
Cdd:PRK01372 160 AalelafkydDEVLVEKYIKGR---ELTVaVLGGKAlpvieivpagefydyEAKYLAG----------GTQYICPA-GLP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1943962720 250 PELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:PRK01372 226 AEIEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYLLEVNT 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
77-292 |
2.15e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 39.87 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 77 AIHPGY----GFLSENAN-FAEQversGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLTDDMDANRAhAKR 151
Cdd:PRK12767 72 LLIPLIdpelPLLAQNRDrFEEI----GVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALA-KGE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943962720 152 IGYPVIIK-----ASgggggrgmrvvrSDAELAQSISMtkAEAKAAFNNDMVYMEkYLENPRhIEIQVLADGQGNAIyla 226
Cdd:PRK12767 147 LQFPLFVKprdgsAS------------IGVFKVNDKEE--LEFLLEYVPNLIIQE-FIEGQE-YTVDVLCDLNGEVI--- 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943962720 227 erdCSMQRRHQKVVEEAPAPGIT---PELRRYIgERCAKAcvdIGYRGAGTFEFLFENGEFYFIEMNTR 292
Cdd:PRK12767 208 ---SIVPRKRIEVRAGETSKGVTvkdPELFKLA-ERLAEA---LGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| |
