|
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: 908.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLgDDMNANRAHAKRIGYPVIIKA 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446807371 399 IARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKLGLQEK 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: 804.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGpLGDDMNANRAHAKRIGYPVIIKA 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446807371 399 IARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKLGLQE 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: 777.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLGDDMNAnRAHAKRIGYPVIIKA 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEA-LAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SgggggrgmrvvRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:COG4770 160 SaggggkgmrvvRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDPaRGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446807371 399 IARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKL 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: 689.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLGDDMNAnRAHAKRIGYPVIIKA 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEA-IAIARQIGYPVMLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGE-FYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAI 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446807371 400 ARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKL 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 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLGDDMNANRAhAKRIGYPVIIKA 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEI-AEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 321 LSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAI 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446807371 400 ARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKLGLQEK 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: 613.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLGDDMNANRAhAKRIGYPVIIKA 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEI-AKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPkNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446807371 399 IARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKLG 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: 576.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 80 PGYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLgDDMNANRAHAKRIGYPVIIK 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPI-DDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 160 ASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 240 VEEAPAPGITPELRRYIgerCAKA---CVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:PRK12999 243 VEIAPAPGLSEELRERI---CEAAvklARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 316 AAGQPLS------ITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGK 387
Cdd:PRK12999 320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPaNNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446807371 388 LICYGENRDVAIARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHG 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: 560.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 2 LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 82 YGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLgDDMNANRAHAKRIGYPVIIKAS 161
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVV-ASLDAALEVAARIGYPLMIKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 162 GGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQgNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 242 EAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPlRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446807371 399 IARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLE 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: 558.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAIH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGpVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 80 PGYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLgDDMNANRAHAKRIGYPVIIK 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPV-DDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 160 ASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 240 VEEAPAPGITPELRRYIGE---RCAKAcvdIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:COG1038 242 VEIAPAPNLDEELREAICEaavKLAKA---VGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 316 AAGQPLS------ITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRW-ESHIYAGYTVPPYYDSMIGK 387
Cdd:COG1038 319 AEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPaNNFMPDTGRITAYRSAGGFGIRLdGGNAYTGAVITPYYDSLLVK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446807371 388 LICYGENRDVAIARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHG 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: 551.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 2 LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 82 YGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLgDDMNANRAHAKRIGYPVIIKAS 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAL-KSYEEAKKIAKEIGYPVILKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 162 GGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 242 EAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 321 LSiTQDEVVVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIA 400
Cdd:PRK08462 323 LP-SQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446807371 401 RMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKK 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: 545.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLGDdMNANRAHAKRIGYPVIIKA 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLAD-LDEALAEAERIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPkNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446807371 399 IARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLE 441
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-445 |
5.67e-175 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 498.57 E-value: 5.67e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP-IKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDgPLGDD-MNANRAHAKRIGYPVIIK 159
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNSEsMEEIKIFARKIGYPVILK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 160 ASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 240 VEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAG 318
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 319 QPLSITQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDV 397
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVwKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446807371 398 AIARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEKKLG 445
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-442 |
2.20e-163 |
|
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: 491.85 E-value: 2.20e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 3 DKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGY 82
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 83 GFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSdgPLGDDMNANRAHAKRIGYPVIIKASG 162
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT--GLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 163 GGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVVEE 242
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 243 APAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdeARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 321 LSITQ--DEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGgfGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDV 397
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPaKNFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446807371 398 AIARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHGGTNIHYLEK 442
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-433 |
3.52e-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: 484.72 E-value: 3.52e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 4 KIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPS---VKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDlgpIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 81 GYGFLSENANFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSDGPLgDDMNANRAHAKRIGYPVIIKA 160
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPP-ETMEEVLDFAAAIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 161 SGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 320 PLSI------TQDEVVVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGKLICY 391
Cdd:TIGR01235 320 SLPTpqlgvpNQEDIRTNGYAIQCRVTTEDPaNNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446807371 392 GENRDVAIARMKNALQELIIDGIKTNIDLQTRIMNDEHFQHG 433
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
3.19e-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: 290.36 E-value: 3.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 115 DKVSAITAMKKAGVPTVPGSDGPlGDDMNANRAHAKRIGYPVIIKASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFS 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGP-VETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 195 NDMVYMEKYLENPRHIEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGT 274
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446807371 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 |
8.79e-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: 219.36 E-value: 8.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 62 NIPAIISA-AEITGAVAIHpgyGFLSENAN----FAEQVERSGFIfiGPKADTIRLMGDKVSAITAMKKAGVPtVPGSDg 136
Cdd:COG0439 1 DIDAIIAAaAELARETGID---AVLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGFA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 137 pLGDDMNANRAHAKRIGYPVIIKASGGGGGRGMRVVRSDAELAQSISMTKAEAKAAFSNDMVYMEKYLENpRHIEIQVLA 216
Cdd:COG0439 74 -LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 217 DgQGNAIYlaerdCSMQRRHQK---VVE---EAPAPgITPELRRYIGERCAKACVDIGY-RGAGTFEFLF-ENGEFYFIE 288
Cdd:COG0439 152 R-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIE 224
|
250 260 270
....*....|....*....|....*....|....
gi 446807371 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 |
3.07e-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: 191.93 E-value: 3.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 2 LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 446807371 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 |
3.01e-59 |
|
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: 189.16 E-value: 3.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGI 414
Cdd:smart00878 1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 446807371 415 KTNIDLQTRIMNDEHFQHGGTNIHYLE 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 |
1.10e-55 |
|
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: 180.00 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGI 414
Cdd:pfam02785 1 EARIYAEDPdNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 446807371 415 KTNIDLQTRIMNDEHFQHGGTNIHYLEK 442
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
90-321 |
3.02e-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: 68.87 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 90 NFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSdgpLGDDMNANRAHAKRIGYPVIIKASGGGGGRGM 169
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWK---TATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 170 RVVRSDAELAQSISmtkaEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIY-LAErdcsmqrrHqkvVEEA----- 243
Cdd:TIGR01369 721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPgIME--------H---IEEAgvhsg 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 244 ------PAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAA 317
Cdd:TIGR01369 786 dstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865
|
....
gi 446807371 318 GQPL 321
Cdd:TIGR01369 866 GKKL 869
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
90-322 |
7.24e-12 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 67.69 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 90 NFAEQVERSGFIFIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSdgpLGDDMNANRAHAKRIGYPVIIKASGGGGGRGM 169
Cdd:PRK12815 645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL---TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGM 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 170 RVVRSDAELAQSIsmtkaeAKAAFSNDMVYMEKYLENpRHIEIQVLADgqGNAIYLA---ErdcsmqrrHqkvVEEA--- 243
Cdd:PRK12815 722 AVVYDEPALEAYL------AENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiE--------H---IEQAgvh 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 244 --------PAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:PRK12815 782 sgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861
|
....*..
gi 446807371 316 AAGQPLS 322
Cdd:PRK12815 862 LLGKSLA 868
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
84-335 |
3.50e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 52.24 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 84 FLSENANFAEQversGFIFIGPKADTIRLMGDKVSAITAMKKAGVPtVPGSDGPlgDDMNANRAHAKRIGYPVIIKASGG 163
Cdd:COG3919 90 LLSRHRDELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTVVL--DSADDLDALAEDLGFPVVVKPADS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 164 GGGRGMRVVR--------SDAELAQSIsmtkaEAKAAFSNDMVYMEkYLENPRHIE--IQVLADGQGNAIYLaerdCSMQ 233
Cdd:COG3919 163 VGYDELSFPGkkkvfyvdDREELLALL-----RRIAAAGYELIVQE-YIPGDDGEMrgLTAYVDRDGEVVAT----FTGR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 234 RRHQK--------VVEEAPAPGITPELRRYIGErcakacvdIGYRGAGTFEFLF--ENGEFYFIEMNTRI--QVEHPVte 301
Cdd:COG3919 233 KLRHYppaggnsaARESVDDPELEEAARRLLEA--------LGYHGFANVEFKRdpRDGEYKLIEINPRFwrSLYLAT-- 302
|
250 260 270
....*....|....*....|....*....|....*
gi 446807371 302 mITGVDLIKEQLRIAAGQPLSITQD-EVVVRGHAV 335
Cdd:COG3919 303 -AAGVNFPYLLYDDAVGRPLEPVPAyREGVLWRVL 336
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
90-292 |
2.51e-06 |
|
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: 49.88 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 90 NFAEQVERSGFI----FIGPKADTIRLMGDKVSAITAMKKAGVPTVPGSdgpLGDDMNANRAHAKRIGYPVIIKASGGGG 165
Cdd:COG0458 85 NLAVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKSG---TATSVEEALAIAEEIGYPVIVRPSYVLG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 166 GRGMRVVRSDAELAQSIsmtkAEAKAAFSNDMVYMEKYLENPRHIEIQVLADGQGNAIYLaerdCSMQrrHqkvVEEA-- 243
Cdd:COG0458 162 GRGMGIVYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgv 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807371 244 ---------PAPGITPE----LRRYiGERCAKAcvdIGYRGAGTFEFLFENGEFYFIEMNTR 292
Cdd:COG0458 229 hsgdsicvaPPQTLSDKeyqrLRDA-TLKIARA---LGVVGLCNIQFAVDDGRVYVIEVNPR 286
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-291 |
6.69e-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: 43.84 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 123 MKKAGVPTVP----GSDGPLGDDMNANRAHAKRIGYPVIIKAsgggggrgmrvvrsdAELAQSISMTKAEA--------K 190
Cdd:pfam07478 2 LKAAGLPVVPfvtfTRADWKLNPKEWCAQVEEALGYPVFVKP---------------ARLGSSVGVSKVESreelqaaiE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 191 AAFSND-MVYMEKYLENpRHIEIQVLADGQGNAIYLAER--DCSMQRRHQKVVEEA-----PApGITPELRRYIGERCAK 262
Cdd:pfam07478 67 EAFQYDeKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALK 144
|
170 180 190
....*....|....*....|....*....|
gi 446807371 263 ACVDIGYRGAGTFE-FLFENGEFYFIEMNT 291
Cdd:pfam07478 145 AYKALGCRGLARVDfFLTEDGEIVLNEVNT 174
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
115-291 |
9.54e-05 |
|
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: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 115 DKVSAITAMKKAGVPTVPGSDGPLGDDMNANRAHAKrIGYPVIIKASgggggrgmrvvRSDAELAQSISMTKAEAKAAFS 194
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEE-LGLPLFVKPA-----------REGSSVGVSKVKNAEELAAALE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 195 NDMVY-----MEKYLEnPRHIEIQVLADGQGNA-----I------------YLAErdcsmqrrhqKVVEEAPAPgITPEL 252
Cdd:COG1181 163 EAFKYddkvlVEEFID-GREVTVGVLGNGGPRAlppieIvpengfydyeakYTDG----------GTEYICPAR-LPEEL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446807371 253 RRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:COG1181 231 EERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
5-321 |
1.31e-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: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 5 IVIANRGEIALRILRACK---ELGIKTVAVHSSAdrdlkhvlladETVCIGPAPSVKSYL------NIPAIISAAEITGa 75
Cdd:TIGR01369 17 IVIGQAAEFDYSGSQACKalkEEGYRVILVNSNP-----------ATIMTDPEMADKVYIepltpeAVEKIIEKERPDA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 76 vaIHPGYGflSENA-NFAEQVERSGFIfigpKADTIRLMGDKVSAI----------TAMKKAGVPtVPGSDgpLGDDMNA 144
Cdd:TIGR01369 85 --ILPTFG--GQTAlNLAVELEESGVL----EKYGVEVLGTPVEAIkkaedrelfrEAMKEIGEP-VPESE--IAHSVEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 145 NRAHAKRIGYPVIIKASGGGGGRGMRVVRSDAELaqsismtKAEAKAAFSNDM---VYMEKYLENPRHIEIQVLADGQGN 221
Cdd:TIGR01369 154 ALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL-------KEIAERALSASPinqVLVEKSLAGWKEIEYEVMRDSNDN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 222 AIYLaerdCSMQR-----RHQK---VVeeAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNT 291
Cdd:TIGR01369 227 CITV----CNMENfdpmgVHTGdsiVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNP 300
|
330 340 350
....*....|....*....|....*....|
gi 446807371 292 RIQVEHPVTEMITGVDLIKEQLRIAAGQPL 321
Cdd:TIGR01369 301 RVSRSSALASKATGYPIAKVAAKLAVGYTL 330
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-290 |
4.20e-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: 42.24 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 16 RILRACKELGIktvavhssadrDLKHVLLADETVCIGPAPSVKSYLNIP---AIISAAeitgavaIHPGYGFlsenaNFA 92
Cdd:COG0189 18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSefdAVLPRI-------DPPFYGL-----ALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 93 EQVERSGFIFIGPkADTIRLMGDKVSAITAMKKAGVPTvpgsdgP---LGDDMNANRAHAKRIGYPVIIKAsgggggrgm 169
Cdd:COG0189 75 RQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV------PptlVTRDPDDLRAFLEELGGPVVLKP--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 170 rvvrsdAELAQSISMTKAEAKAAF----------SNDMVYMEKYLENPRHIEIQVLA-DGQgnaiYLAerdcSMQRRHQK 238
Cdd:COG0189 139 ------LDGSGGRGVFLVEDEDALesilealtelGSEPVLVQEFIPEEDGRDIRVLVvGGE----PVA----AIRRIPAE 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807371 239 -----------VVEEAPapgITPELRRyIGERCAKAcVDIGYrgAGtFEFLFENGEFYFIEMN 290
Cdd:COG0189 205 gefrtnlarggRAEPVE---LTDEERE-LALRAAPA-LGLDF--AG-VDLIEDDDGPLVLEVN 259
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
152-291 |
5.07e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 41.73 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 152 IGYPVIIKASGGGGGRGMRVVRSDAELAQSIsmtKAEAKaafSNDMVYMEKYLENpRHIEIQVLADGQGNAIyLAERDCS 231
Cdd:PRK14571 124 LGYPCVVKPRREGSSIGVFICESDEEFQHAL---KEDLP---RYGSVIVQEYIPG-REMTVSILETEKGFEV-LPILELR 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807371 232 MQRRHQKVVEE---------APAPgITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNT 291
Cdd:PRK14571 196 PKRRFYDYVAKytkgetefiLPAP-LNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINT 263
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
68-412 |
5.40e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 39.45 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 68 SAAEITGAVAIHPGY-GFLSENANFAEQVERSGFIFIGPKADT--IRLMGDKVSAITAMKKAGVPtVPGSDGPLGDDMNA 144
Cdd:PRK02186 57 DPDRIHRFVSSLDGVaGIMSSSEYFIEVASEVARRLGLPAANTeaIRTCRDKKRLARTLRDHGID-VPRTHALALRAVAL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 145 NRAHakRIGYPVIIKASGGGGGRGMRVVRSDAE-LAQSISMTKAEAKAAFsndmvyMEKYLENPRHiEIQVLADGQGNAI 223
Cdd:PRK02186 136 DALD--GLTYPVVVKPRMGSGSVGVRLCASVAEaAAHCAALRRAGTRAAL------VQAYVEGDEY-SVETLTVARGHQV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 224 ------YLAERDCSMQRRHqkvveEAPAPGITPELRRYigERCAKACVD-IGYR-GAGTFEFLFENGEFYFIEMNTR--- 292
Cdd:PRK02186 207 lgitrkHLGPPPHFVEIGH-----DFPAPLSAPQRERI--VRTVLRALDaVGYAfGPAHTELRVRGDTVVIIEINPRlag 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 293 --IQVehpVTEMITGVDLIKEQLRIAAGQPLsiTQDEVVVRGHAVECRINAEDPN----TFLPSP---GKITRFH---AP 360
Cdd:PRK02186 280 gmIPV---LLEEAFGVDLLDHVIDLHLGVAA--FADPTAKRYGAIRFVLPARSGVlrglLFLPDDiaaRPELRFHplkQP 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446807371 361 GGfGVRWESHiyagytvppyYDSMIGKLICYGENRDVAIARMKNALQELIID 412
Cdd:PRK02186 355 GD-ALRLEGD----------FRDRIAAVVCAGDHRDSVAAAAERAVAGLSID 395
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
115-291 |
9.09e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 37.78 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 115 DKVSAITAMKKAGVPTVPGSDGPLGDDMNANrahAKRIGYPVIIKASgggggrgmrvvrsdAElAQSISMTK----AEAK 190
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAA---IDKLGLPLVVKPA--------------RE-GSSVGVSKvkeeDELQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807371 191 AAFSNDMVY-----MEKYLENPrhiEIQV-LADGQG---------------NAIYLAErdcsmqrrhqKVVEEAPApGIT 249
Cdd:PRK01372 160 AALELAFKYddevlVEKYIKGR---ELTVaVLGGKAlpvieivpagefydyEAKYLAG----------GTQYICPA-GLP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446807371 250 PELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:PRK01372 226 AEIEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYLLEVNT 268
|
|
| |
