|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 893.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKErNMQIAKRIGYPVIIKA 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEE-ALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDPE-TFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAkNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKLGL 446
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLAL 447
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-444 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 773.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKErNMQIAKRIGYPVIIKA 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEE-ALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AgggggrgmrvvRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:COG4770 160 SaggggkgmrvvRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDPE-TFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDPArGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKL 444
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 755.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGpVSDDKERNMQIAKRIGYPVIIKA 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDP-ETFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKLGL 446
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-444 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 700.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERnMQIAKRIGYPVIIKA 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEA-IAIARQIGYPVMLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYENGE-FYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDPETFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVAI 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 567929072 400 ARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKL 444
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQL 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 670.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERnMQIAKRIGYPVIIKA 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEA-KEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQP 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 321 LSFTQDDVVIRGHAIECRINAEDP-ETFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVAI 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 567929072 400 ARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKLGL 446
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 598.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERnMQIAKRIGYPVIIKA 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEA-LEIAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDPET-FIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPKNgFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKLG 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: 566.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPAT-ESYLDIPRIIAAAEVTDAVAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 80 PGYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERnMQIAKRIGYPVIIK 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEA-LEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 160 AAGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKV 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 240 VEEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAG 318
Cdd:PRK12999 243 VEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 319 QPLSF------TQDDVVIRGHAIECRINAEDPET-FIPSPGKITRFHPAGGLGIRWDS-HIYADYTVPPHYDSMIGKLIT 390
Cdd:PRK12999 323 ATLHDleigipSQEDIRLRGYAIQCRITTEDPANnFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 567929072 391 YGENRDVAIARARNALNELVIDGIKTNTPLHKKILADENFQSG 433
Cdd:PRK12999 403 WGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG 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: 561.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 2 LDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 82 YGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVsDDKERNMQIAKRIGYPVIIKAA 161
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVV-ASLDAALEVAARIGYPLMIKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 162 GGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQgNAVHLGERDCSMQRRHQKVVE 241
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 242 EAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY--ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDPE-TFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPLrDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLE 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: 545.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPP-ATESYLDIPRIIAAAEVTDAVAIH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKgPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 80 PGYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERnMQIAKRIGYPVIIK 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEA-LAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 160 AAGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKV 239
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 240 VEEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAG 318
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 319 QPLS------FTQDDVVIRGHAIECRINAEDPET-FIPSPGKITRFHPAGGLGIRWDS-HIYADYTVPPHYDSMIGKLIT 390
Cdd:COG1038 322 YSLDdpeigiPSQEDIRLNGYAIQCRITTEDPANnFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVKVTA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 567929072 391 YGENRDVAIARARNALNELVIDGIKTNTPLHKKILADENFQSG 433
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAG 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: 544.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 2 LDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 82 YGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERNmQIAKRIGYPVIIKAA 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAK-KIAKEIGYPVILKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 162 GGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVVE 241
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 242 EAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQP 320
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 321 LsFTQDDVVIRGHAIECRINAEDPETFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVAIA 400
Cdd:PRK08462 323 L-PSQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 567929072 401 RARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKK 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: 533.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPaTESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERnMQIAKRIGYPVIIKA 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEA-LAEAERIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDPET-FIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPKNdFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLE 441
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-445 |
1.28e-169 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 485.09 E-value: 1.28e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 1 MLDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPaTESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP-IKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKERNMQIAKRIGYPVIIKA 160
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLSFTQDDVVIRGHAIECRINAEDP-ETFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVA 398
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVwKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 567929072 399 IARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEKKLG 445
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-442 |
1.57e-167 |
|
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: 502.64 E-value: 1.57e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 3 DKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHPGY 82
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 83 GFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSdgPVSDDKERNMQIAKRIGYPVIIKAAG 162
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT--GLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 163 GGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVVEE 242
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 243 APAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY--ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQP 320
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdeARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 321 LSFTQ--DDVVIRGHAIECRINAEDP-ETFIPSPGKITRFH-PAgglGIRWDSHIYADYTVPPHYDSMIGKLITYGENRD 396
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPaKNFQPSPGLLTDVQfPD---DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 567929072 397 VAIARARNALNELVIDGIKTNTPLHKKILADENFQSGGTNIHYLEK 442
Cdd:TIGR02712 397 DAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-433 |
2.61e-160 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 482.40 E-value: 2.61e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 4 KVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPA---TESYLDIPRIIAAAEVTDAVAIHP 80
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDlgpIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 81 GYGFLSENADFADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVsDDKERNMQIAKRIGYPVIIKA 160
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPP-ETMEEVLDFAAAIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 161 AGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVV 240
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 241 EEAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQ 319
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 320 PLS------FTQDDVVIRGHAIECRINAEDPE-TFIPSPGKITRFHPAGGLGIRWDS-HIYADYTVPPHYDSMIGKLITY 391
Cdd:TIGR01235 320 SLPtpqlgvPNQEDIRTNGYAIQCRVTTEDPAnNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 567929072 392 GENRDVAIARARNALNELVIDGIKTNTPLHKKILADENFQSG 433
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
5.21e-96 |
|
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: 287.28 E-value: 5.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 115 DKVSAINAMRKAGVPCVPGSDGPVSDDKErNMQIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFG 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEE-ALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 195 NSMVYMEKFLENPRHIEIQVLADGQGNAVHLGERDCSMQRRHQKVVEEAPAPGITAEVRKFIGERCTRACIEIGYRGAGT 274
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 567929072 275 FEFLYE--NGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQPLS 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-320 |
3.69e-67 |
|
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: 215.12 E-value: 3.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 62 DIPRIIAAAEvtdavAIHPGYGF---LSENAD----FADQVEQSGFVFIGPkgDTIRLMGDKVSAINAMRKAGVPcVPGS 134
Cdd:COG0439 1 DIDAIIAAAA-----ELARETGIdavLSESEFavetAAELAEELGLPGPSP--EAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 135 DgpVSDDKERNMQIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELIDSIALTQQEAKQFFGNSMVYMEKFLENpRHIEIQV 214
Cdd:COG0439 73 A--LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 215 LADgQGNAVHlgerdCSMQRRHQK---VVE---EAPAPgITAEVRKFIGERCTRACIEIGY-RGAGTFEFLY-ENGEFYF 286
Cdd:COG0439 150 LVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYL 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 567929072 287 IEMNTRIQVEH--PVTEMVSGVDLIKEQLKIAAGQP 320
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
8.53e-59 |
|
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: 188.08 E-value: 8.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 2 LDKVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPATESYLDIPRIIAAAEVTDAVAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 567929072 82 YGFLSENADFADQVEQSGFVFIGPKGDT 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 |
1.04e-56 |
|
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: 182.61 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 336 ECRINAEDPE-TFIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVAIARARNALNELVIDGI 414
Cdd:smart00878 1 ECRINAEDPAnGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 567929072 415 KTNTPLHKKILADENFQSGGTNIHYLE 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 |
8.40e-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: 177.69 E-value: 8.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 336 ECRINAEDPET-FIPSPGKITRFHPAGGLGIRWDSHIYADYTVPPHYDSMIGKLITYGENRDVAIARARNALNELVIDGI 414
Cdd:pfam02785 1 EARIYAEDPDNnFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 567929072 415 KTNTPLHKKILADENFQSGGTNIHYLEK 442
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
4-308 |
5.00e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 67.26 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 4 KVVIANRGEIALRVLRACKELGIKTVAVHSTADRDLKHVLLADETICIGRPPA-TESYLDipRIIAAAE---------VT 73
Cdd:COG3919 7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDdPEAFVD--ALLELAErhgpdvlipTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 74 DAVAIhpgygFLSENADfadQVEQsGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPcVPGSDgpVSDDKERNMQIAKRIG 153
Cdd:COG3919 85 DEYVE-----LLSRHRD---ELEE-HYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV--VLDSADDLDALAEDLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 154 YPVIIKAAGGGGGRGMRVVR--------SEAELIDSIAltqqEAKQFFGNSMVymEKFLENPRHIE--IQVLADGQGNAV 223
Cdd:COG3919 153 FPVVVKPADSVGYDELSFPGkkkvfyvdDREELLALLR----RIAAAGYELIV--QEYIPGDDGEMrgLTAYVDRDGEVV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 224 HLgerdCSMQRRHQK--------VVEEAPAPGITAEVRKFIGErctracieIGYRGAGTFEFLY--ENGEFYFIEMNTRI 293
Cdd:COG3919 227 AT----FTGRKLRHYppaggnsaARESVDDPELEEAARRLLEA--------LGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
330
....*....|....*..
gi 567929072 294 --QVEHPVtemVSGVDL 308
Cdd:COG3919 295 wrSLYLAT---AAGVNF 308
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
17-321 |
2.49e-11 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 65.79 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 17 VLRACKELGIKTVAVHS----------TADRdlkhvLLADeticigrPPATESYLDIPRIiaaaEVTDAVAIHPGyGFLS 86
Cdd:TIGR01369 580 AVLALRELGYETIMINYnpetvstdydTSDR-----LYFE-------PLTFEDVMNIIEL----EKPEGVIVQFG-GQTP 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 87 ENAdfADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSdgpVSDDKERNMQIAKRIGYPVIIKAAGGGGG 166
Cdd:TIGR01369 643 LNL--AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWK---TATSVEEAVEFASEIGYPVLVRPSYVLGG 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 167 RGMRVVRSEAELIDSIaltqQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQG-----------NA-VHLGERDCSMqr 234
Cdd:TIGR01369 718 RAMEIVYNEEELRRYL----EEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEvlipgimehieEAgVHSGDSTCVL-- 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 235 rhqkvveeaPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLK 314
Cdd:TIGR01369 792 ---------PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
....*..
gi 567929072 315 IAAGQPL 321
Cdd:TIGR01369 863 VMLGKKL 869
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-291 |
1.96e-08 |
|
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: 54.24 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 123 MRKAGVPCVP----GSDGPVSDDKERNMQIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELIDSIAltqqEAKQFFGNSMV 198
Cdd:pfam07478 2 LKAAGLPVVPfvtfTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIE----EAFQYDEKVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 199 ymEKFLENpRHIEIQVLADGQGNAVHLGER--DCSMQRRHQKVVEEA-----PApGITAEVRKFIGERCTRACIEIGYRG 271
Cdd:pfam07478 78 --EEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALGCRG 153
|
170 180
....*....|....*....|.
gi 567929072 272 AGTFE-FLYENGEFYFIEMNT 291
Cdd:pfam07478 154 LARVDfFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-322 |
1.30e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 54.20 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 92 ADQVEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSdgpVSDDKERNMQIAKRIGYPVIIKAAGGGGGRGMRV 171
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL---TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 172 VRSEAELIdsiALTQQEAKQFFGnsmVYMEKFLENpRHIEIQVLADG------------QGNAVHLGERDCSMqrrhqkv 239
Cdd:PRK12815 724 VYDEPALE---AYLAENASQLYP---ILIDQFIDG-KEYEVDAISDGedvtipgiiehiEQAGVHSGDSIAVL------- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 240 veeaPAPGITAEVRKFIgERCTRACI-EIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAG 318
Cdd:PRK12815 790 ----PPQSLSEEQQEKI-RDYAIKIAkKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
|
....
gi 567929072 319 QPLS 322
Cdd:PRK12815 865 KSLA 868
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
110-292 |
2.38e-07 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 52.96 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 110 IRLMGDKVSAI----------NAMRKAGVPCVPGsdGPVSDDKErNMQIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELI 179
Cdd:COG0458 99 VKILGTSPDAIdlaedrelfkELLDKLGIPQPKS--GTATSVEE-ALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 180 DSIaltqQEAKQFFGNSMVYMEKFLENPRHIEIQVLADGQGNaVHLGerdCSMQrrHqkvVEEA-----------PAPGI 248
Cdd:COG0458 176 EYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDN-VIIV---GIME--H---IEPAgvhsgdsicvaPPQTL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 567929072 249 TAEVRKFIgERCTRACI-EIGYRGAGTFEFLYENGEFYFIEMNTR 292
Cdd:COG0458 243 SDKEYQRL-RDATLKIArALGVVGLCNIQFAVDDGRVYVIEVNPR 286
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
40-412 |
4.03e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.46 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 40 KHVLLADETICIGRPPATESYLDIPRIIA-AAEVTDAVAIHpgyGFLSENADFADQVEQSGFvFIG-----------PKG 107
Cdd:PRK02186 22 KALLRGFTPYFLTANRGKYPFLDAIRVVTiSADTSDPDRIH---RFVSSLDGVAGIMSSSEY-FIEvasevarrlglPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 108 DT--IRLMGDKVSAINAMRKAGVPcVPGSDGPVSDDKERNmqIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELID-SIAL 184
Cdd:PRK02186 98 NTeaIRTCRDKKRLARTLRDHGID-VPRTHALALRAVALD--ALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAhCAAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 185 TQQEAKQFFgnsmvyMEKFLENPRHiEIQVLADGQGNAV------HLGERDCSMQRRHqkvveEAPAPgITAEVRKFIGE 258
Cdd:PRK02186 175 RRAGTRAAL------VQAYVEGDEY-SVETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAP-LSAPQRERIVR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 259 RCTRACIEIGYR-GAGTFEFLYENGEFYFIEMNTR-----IQVehpVTEMVSGVDLIKEQLKIAAGQPlsFTQDDVVIRG 332
Cdd:PRK02186 242 TVLRALDAVGYAfGPAHTELRVRGDTVVIIEINPRlaggmIPV---LLEEAFGVDLLDHVIDLHLGVA--AFADPTAKRY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 333 HAIECRINAEDPE----TFIPSP---GKITRFHPAGGLGirwdshiyADYTVPPHYDSMIGKLITYGENRDVAIARARNA 405
Cdd:PRK02186 317 GAIRFVLPARSGVlrglLFLPDDiaaRPELRFHPLKQPG--------DALRLEGDFRDRIAAVVCAGDHRDSVAAAAERA 388
|
....*..
gi 567929072 406 LNELVID 412
Cdd:PRK02186 389 VAGLSID 395
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-159 |
2.53e-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: 45.70 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 16 RVLRACKELGIktvavhstadrDLKHVLLADETICIGRPPATESYLDIPRIiaaaevtDAV---AIHPGYGFlsenaDFA 92
Cdd:COG0189 18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSEF-------DAVlprIDPPFYGL-----ALL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 93 DQVEQSGFVFIGPkGDTIRLMGDKVSAINAMRKAGVPCvpgsdgP---VSDDKERNMQIAKRIGYPVIIK 159
Cdd:COG0189 75 RQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV------PptlVTRDPDDLRAFLEELGGPVVLK 137
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
18-321 |
7.03e-05 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 45.38 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 18 LRACKELGIKTVAVHS---TADRDLKhvlLADETICIgrpPATESYLDipRIIAAaEVTDAVAIHPGyGFLSENAdfADQ 94
Cdd:TIGR01369 33 CKALKEEGYRVILVNSnpaTIMTDPE---MADKVYIE---PLTPEAVE--KIIEK-ERPDAILPTFG-GQTALNL--AVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 95 VEQSGFVfigpKGDTIRLMGDKVSAI----------NAMRKAGVPcVPGSDgpVSDDKERNMQIAKRIGYPVIIKAAGGG 164
Cdd:TIGR01369 101 LEESGVL----EKYGVEVLGTPVEAIkkaedrelfrEAMKEIGEP-VPESE--IAHSVEEALAAAKEIGYPVIVRPAFTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 165 GGRGMRVVRSEAELIDSI--ALTQQEAKQffgnsmVYMEKFLENPRHIEIQVLADGQGNA-------------VHLGErd 229
Cdd:TIGR01369 174 GGTGGGIAYNREELKEIAerALSASPINQ------VLVEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGD-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 230 cSMqrrhqkVVeeAPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEFLY--ENGEFYFIEMNTRIQVEHPVTEMVSGVD 307
Cdd:TIGR01369 246 -SI------VV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPRVSRSSALASKATGYP 316
|
330
....*....|....
gi 567929072 308 LIKEQLKIAAGQPL 321
Cdd:TIGR01369 317 IAKVAAKLAVGYTL 330
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
82-291 |
7.43e-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: 44.33 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 82 YGFLSENADFADQVEQSGF--VFI---GPKGD--TIR----LMG---------------DKVSAINAMRKAGVPCVPG-- 133
Cdd:COG1181 36 VPIGIDVEDLPAALKELKPdvVFPalhGRGGEdgTIQglleLLGipytgsgvlasalamDKALTKRVLAAAGLPTPPYvv 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 134 -SDGPVSDDKErnmqIAKRIGYPVIIKAAgggggrgmrvvrSE------------AELIDSIAltqqEAKQFFGNSMVym 200
Cdd:COG1181 116 lRRGELADLEA----IEEELGLPLFVKPA------------REgssvgvskvknaEELAAALE----EAFKYDDKVLV-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 201 EKFLEnPRHIEIQVLADGQGNAVHLGE-------RDcsmqrRHQK-----VVEEAPAPgITAEVRKFIGERCTRACIEIG 268
Cdd:COG1181 174 EEFID-GREVTVGVLGNGGPRALPPIEivpengfYD-----YEAKytdggTEYICPAR-LPEELEERIQELALKAFRALG 246
|
250 260
....*....|....*....|....
gi 567929072 269 YRGAGTFEFLY-ENGEFYFIEMNT 291
Cdd:COG1181 247 CRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
95-357 |
2.44e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 95 VEQSGFVFIGPKGDTIRLMGDKVSAINAMRKAGVPCVPGSDGPVSDDKernMQIAKRIG-YPVIIKAAGGGGGRGMRVVR 173
Cdd:PLN02735 124 LEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDEC---FEIAEDIGeFPLIIRPAFTLGGTGGGIAY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 174 SEAELiDSIALTQQEAKQffgNSMVYMEKFLENPRHIEIQVLADGQGNAVHLgerdCSMQRRHQKVVEE------APAPG 247
Cdd:PLN02735 201 NKEEF-ETICKAGLAASI---TSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHTgdsitvAPAQT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 248 ITAEVRKFIGERCTRACIEIGYRGAGT---FEFLYENGEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQPLSFT 324
Cdd:PLN02735 273 LTDKEYQRLRDYSVAIIREIGVECGGSnvqFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQI 352
|
250 260 270
....*....|....*....|....*....|....*..
gi 567929072 325 QDDvvirghaiecrINAEDPETFIPS----PGKITRF 357
Cdd:PLN02735 353 PND-----------ITLKTPASFEPSidyvVTKIPRF 378
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
54-337 |
3.37e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 39.48 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 54 PPATES-YLD-IPRIIAAAEVTdavAIHPGY----GFLSENAD-FADQveqsGFVFIGPKGDTIRLMGDKVSAINAMRKA 126
Cdd:PRK12767 50 PKVTDPnYIDrLLDICKKEKID---LLIPLIdpelPLLAQNRDrFEEI----GVKVLVSSKEVIEICNDKWLTYEFLKEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 127 GVPCvPGSDGPVSDDKERNMQIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELIDsialtqqeAKQFFGNSMVymEKFLEN 206
Cdd:PRK12767 123 GIPT-PKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEF--------LLEYVPNLII--QEFIEG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 207 PRhIEIQVLADGQGNAVHlgerdcSMQRRHQKVVEEAPAPGIT---AEVRKFigerCTRACIEIGYRGAGTFEFLYENGE 283
Cdd:PRK12767 192 QE-YTVDVLCDLNGEVIS------IVPRKRIEVRAGETSKGVTvkdPELFKL----AERLAEALGARGPLNIQCFVTDGE 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 567929072 284 FYFIEMNTRIQVEHPVTEMVsGVD----LIKEQLKIAAGQPLSFTQDDVVIRGHAIEC 337
Cdd:PRK12767 261 PYLFEINPRFGGGYPLSYMA-GANepdwIIRNLLGGENEPIIGEYKEGLYMRRYDEVV 317
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
136-333 |
6.11e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 38.99 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 136 GPVSDDKERNMQIAKRIGYPVIIKAAGGGGGRGMRVVRSEAELIDSIaltqQEAKQFFGNSMVYMEKFLENPRHIEIQVL 215
Cdd:PLN02735 720 GGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYL----ETAVEVDPERPVLVDKYLSDATEIDVDAL 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 216 ADGQGNAV-------------HLGERDCSMqrrhqkvveeaPAPGITAEVRKFIGERCTRACIEIGYRGAGTFEF-LYEN 281
Cdd:PLN02735 796 ADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPS 864
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 567929072 282 GEFYFIEMNTRIQVEHPVTEMVSGVDLIKEQLKIAAGQPLS---FTQDdvVIRGH 333
Cdd:PLN02735 865 GEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLKdlgFTEE--VIPAH 917
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
20-161 |
6.40e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 38.60 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929072 20 ACKELGIKTVAVhsTADRDLKHVLLADETICIgrppateSYLDIPRIIAAAEVTDAVAihpgYGFlsEN--ADFADQVEQ 97
Cdd:PRK06019 20 AAAPLGYKVIVL--DPDPDSPAAQVADEVIVA-------DYDDVAALRELAEQCDVIT----YEF--ENvpAEALDALAA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567929072 98 SGFVFIGPkgDTIRLMGDKVSAINAMRKAGVPCVPGSdgPVSDDKERNmQIAKRIGYPVIIKAA 161
Cdd:PRK06019 85 RVPVPPGP--DALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLE-AALADLGLPAVLKTR 143
|
|
| |
