|
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: 906.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKA 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFE-NGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAKnFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1891815632 399 MARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKLEQRNK 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-445 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 817.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKA 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPV-QDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:COG4770 160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF-ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQA 398
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDPARgFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1891815632 399 MARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKLE 445
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELA 446
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-450 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 736.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKA 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNL-EDAEEAIAIARQIGYPVMLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFENGE-FYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFKFTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQAM 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1891815632 400 ARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKLEQRNKR 450
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVKKSTK 450
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-445 |
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: 735.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGaLPDDPAEITRIAKRIGYPIIIKA 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFE-NGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKtFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1891815632 399 MARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKLE 445
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLG 446
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-441 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 697.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKA 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGI-EDIEEAKEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGEK 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 321 LRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQAM 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPLNdFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1891815632 400 ARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLE 441
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIE 441
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-444 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 627.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKA 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEI-ENEEEALEIAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF-ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPKNgFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1891815632 399 MARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKL 444
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKL 445
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-433 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 612.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSP-QSYLNIPAIISAAEVTDAQAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 80 PGYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGaLPDDPAEITRIAKRIGYPIIIK 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEG-PIDDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 160 AAGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKV 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 240 IEEAPAPGITDKHRKKIgeaCADA---CRKIGYRGAGTFEFLF-ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRI 315
Cdd:PRK12999 243 VEIAPAPGLSEELRERI---CEAAvklARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 316 AAGEKLR------YTQKDVVLRGHAMECRINAEDPF-KFTPSPGRITTYHPPGGPGIRMDS-HIYQGYFVPPNYDSMIAK 387
Cdd:PRK12999 320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPAnNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1891815632 388 VISFGDTRDQAMARMRIALSEMVVEGISTNIPLHNELLNDSAFQRG 433
Cdd:PRK12999 400 LTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG 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: 603.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREA----KyvklADESVCIGPAPSP-QSYLNIPAIISAAEVTDA 75
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSlhrfK----ADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 76 QAIHPGYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGAlPDDPAEITRIAKRIGYP 155
Cdd:COG1038 79 DAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGP-VDDLEEALAFAEEIGYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 156 IIIKAAGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRR 235
Cdd:COG1038 158 VMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 236 HQKVIEEAPAPGITDKHRKKIgeaCADA---CRKIGYRGAGTFEFLF-ENGEFYFIEMNTRVQVEHPVTELITGIDIVQE 311
Cdd:COG1038 238 HQKVVEIAPAPNLDEELREAI---CEAAvklAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 312 QIRIAAGEKLR------YTQKDVVLRGHAMECRINAEDPF-KFTPSPGRITTYHPPGGPGIRMDS-HIYQGYFVPPNYDS 383
Cdd:COG1038 315 QILIAEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPAnNFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1891815632 384 MIAKVISFGDTRDQAMARMRIALSEMVVEGISTNIP-LHNeLLNDSAFQRG 433
Cdd:COG1038 395 LLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPfLEN-VLNHPDFLAG 444
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 586.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 3 EKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHPGY 82
Cdd:PRK08462 5 KRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 83 GFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKAAG 162
Cdd:PRK08462 85 GFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAL-KSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 163 GGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVIEE 242
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 243 APAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFE-NGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGEKL 321
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 322 rYTQKDVVLRGHAMECRINAEDPFKFTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQAMAR 401
Cdd:PRK08462 324 -PSQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAK 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1891815632 402 MRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHK 443
Cdd:PRK08462 403 MKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
4-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 567.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 4 KILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHPGYG 83
Cdd:PRK12833 7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 84 FLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKAAGG 163
Cdd:PRK12833 87 FLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVV-ASLDAALEVAARIGYPLMIKAAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 164 GGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYgNAIYLGERDCSMQRRHQKVIEEA 243
Cdd:PRK12833 166 GGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 244 PAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF--ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGEKL 321
Cdd:PRK12833 245 PSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 322 RYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQAMA 400
Cdd:PRK12833 325 RFAQGDIALRGAALECRINAEDPLRdFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALA 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1891815632 401 RMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKLEQR 447
Cdd:PRK12833 405 RAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAWLAEW 451
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-433 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 559.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSpQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALpDDPAEITRIAKRIGYPIIIKA 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNL-ADLDEALAEAERIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFE-NGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPKNdFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1891815632 399 MARMRIALSEMVVEGISTNIPLHNELLNDSAFQRG 433
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSG 433
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-446 |
2.30e-175 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 499.72 E-value: 2.30e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 1 MFEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSpQSYLNIPAIISAAEVTDAQAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALPDDPAEITRIAKRIGYPIIIKA 160
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF-ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQA 398
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKnFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1891815632 399 MARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLEHKLEQ 446
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQE 447
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
2-441 |
7.22e-169 |
|
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: 506.11 E-value: 7.22e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 2 FEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHPG 81
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 82 YGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSdgALPDDPAEITRIAKRIGYPIIIKAA 161
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT--GLLSSLDEALEAAKEIGYPVMLKST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 162 GGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVIE 241
Cdd:TIGR02712 159 AGGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 242 EAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF--ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:TIGR02712 239 ETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdeARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQ--KDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGgpGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRD 396
Cdd:TIGR02712 319 LPDFASlnISLTPRGAAIEARVYAENPAKnFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1891815632 397 QAMARMRIALSEMVVEGISTNIPLHNELLNDSAFQRGGTSIHYLE 441
Cdd:TIGR02712 397 DAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLN 441
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-433 |
2.83e-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: 2.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 4 KILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAP--SP-QSYLNIPAIISAAEVTDAQAIHP 80
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPdlGPiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 81 GYGFLSENADFAERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGaLPDDPAEITRIAKRIGYPIIIKA 160
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDG-PPETMEEVLDFAAAIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 161 AGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVI 240
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 241 EEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF-ENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 320 KLR------YTQKDVVLRGHAMECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDS-HIYQGYFVPPNYDSMIAKVISF 391
Cdd:TIGR01235 320 SLPtpqlgvPNQEDIRTNGYAIQCRVTTEDPANnFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1891815632 392 GDTRDQAMARMRIALSEMVVEGISTNIPLHNELLNDSAFQRG 433
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
1.18e-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: 289.20 E-value: 1.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 115 DKVSAKDAMKAAAVPCVPGSDGAlPDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFG 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGP-VETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 195 NPTVYMEKFLENPRHIEIQILADEYGNAIYLGERDCSMQRRHQKVIEEAPAPGITDKHRKKIGEACADACRKIGYRGAGT 274
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1891815632 275 FEFLFE--NGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGEKLR 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-320 |
3.65e-74 |
|
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: 233.61 E-value: 3.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 62 NIPAIISAAevtdaQAIHPGYGF---LSENAD----FAERVEQSGFvfIGPRPDSIRLMGDKVSAKDAMKAAAVPcVPGS 134
Cdd:COG0439 1 DIDAIIAAA-----AELARETGIdavLSESEFavetAAELAEELGL--PGPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 135 DGAlpDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAALINSVNMTRAEAQAAFGNPTVYMEKFLENpRHIEIQI 214
Cdd:COG0439 73 ALV--DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 215 LADEyGNAIYlgerdCSMQRRHQK---VIE---EAPAPgITDKHRKKIGEACADACRKIGY-RGAGTFEFLF-ENGEFYF 286
Cdd:COG0439 150 LVRD-GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYL 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 1891815632 287 IEMNTRVQVEH--PVTELITGIDIVQEQIRIAAGEK 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 |
9.14e-64 |
|
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: 200.79 E-value: 9.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 2 FEKILIANRGEIALRVLRACREMGIKTVVVHSEADREAKYVKLADESVCIGPAPSPQSYLNIPAIISAAEVTDAQAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1891815632 82 YGFLSENADFAERVEQSGFVFIGPRPDS 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 |
3.61e-57 |
|
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: 183.77 E-value: 3.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 336 ECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQAMARMRIALSEMVVEGI 414
Cdd:smart00878 1 ECRINAEDPANgFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 1891815632 415 STNIPLHNELLNDSAFQRGGTSIHYLE 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 |
4.23e-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: 178.46 E-value: 4.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 336 ECRINAEDPFK-FTPSPGRITTYHPPGGPGIRMDSHIYQGYFVPPNYDSMIAKVISFGDTRDQAMARMRIALSEMVVEGI 414
Cdd:pfam02785 1 EARIYAEDPDNnFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 1891815632 415 STNIPLHNELLNDSAFQRGGTSIHYLEH 442
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-321 |
1.71e-14 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 76.16 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 92 AERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGsdgALPDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRV 171
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG---LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 172 VHTEAALinsvnmTRAEAQAAFGNPTVYMEKFLENpRHIEIQILADeyGNAIYLG---ErdcsmqrrHqkvIEEA----- 243
Cdd:PRK12815 724 VYDEPAL------EAYLAENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiE--------H---IEQAgvhsg 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 244 ------PAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAA 317
Cdd:PRK12815 784 dsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLL 863
|
....
gi 1891815632 318 GEKL 321
Cdd:PRK12815 864 GKSL 867
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
13-293 |
7.86e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 72.65 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 13 IALRVLRACREMGIKTVVVHSEADREAKYVKLADESV-CIGPAPSPQSYLNipAIISAAEVTDAQAIHPGY----GFLSE 87
Cdd:COG3919 16 NALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvVPDPGDDPEAFVD--ALLELAERHGPDVLIPTGdeyvELLSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 88 NADFAERveqsGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPcVPgsDGALPDDPAEITRIAKRIGYPIIIKAAGGGGGR 167
Cdd:COG3919 94 HRDELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVP-VP--KTVVLDSADDLDALAEDLGFPVVVKPADSVGYD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 168 G--------MRVVHTEAALINSVnmtrAEAQAAFGNPTVymEKFLENPRHIE--IQILADEYGNAIYLgerdCSMQRRHQ 237
Cdd:COG3919 167 ElsfpgkkkVFYVDDREELLALL----RRIAAAGYELIV--QEYIPGDDGEMrgLTAYVDRDGEVVAT----FTGRKLRH 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1891815632 238 KVIEEAPAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLF--ENGEFYFIEMNTRV 293
Cdd:COG3919 237 YPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
92-322 |
5.40e-13 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 71.18 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 92 AERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGsdgALPDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRV 171
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW---KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEI 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 172 VHTEAALINSVNmtraEAQAAFGNPTVYMEKFLENPRHIEIQILADeyGNAIYLGErdcSMQrrHqkvIEEA-------- 243
Cdd:TIGR01369 723 VYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEEVLIPG---IME--H---IEEAgvhsgdst 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 244 ---PAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGEK 320
Cdd:TIGR01369 789 cvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKK 868
|
..
gi 1891815632 321 LR 322
Cdd:TIGR01369 869 LE 870
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
103-322 |
1.70e-11 |
|
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: 66.06 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 103 IGPRPDSIRLMGDKVSAKDAMKAAAVPcVPGSDGAlpDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAALINsv 182
Cdd:COG0458 102 LGTSPDAIDLAEDRELFKELLDKLGIP-QPKSGTA--TSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEE-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 183 NMTRAeAQAAFGNPtVYMEKFLENPRHIEIQILADEYGNAIYLgerdCSMQrrHqkvIEEA-----------PAPGITDK 251
Cdd:COG0458 177 YLERA-LKVSPDHP-VLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDK 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1891815632 252 HRKKIGEACADACRKIGYRGAGTFEFLFENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGEKLR 322
Cdd:COG0458 246 EYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
96-291 |
3.81e-10 |
|
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: 60.89 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 96 EQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPcVPGSDGALPDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTE 175
Cdd:COG1181 76 ELLGIPYTGSGVLASALAMDKALTKRVLAAAGLP-TPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 176 AALINSVnmtrAEAqAAFGNPtVYMEKFLEnPRHIEIQILADEYGNAIYLGE-------RDcsmqrRHQK-----VIEEA 243
Cdd:COG1181 155 EELAAAL----EEA-FKYDDK-VLVEEFID-GREVTVGVLGNGGPRALPPIEivpengfYD-----YEAKytdggTEYIC 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1891815632 244 PAPgITDKHRKKIGEACADACRKIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:COG1181 223 PAR-LPEELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-291 |
2.85e-07 |
|
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: 50.78 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 123 MKAAAVPCVPG---SDGALPDDPAEITR-IAKRIGYPIIIKAAGGGGGRGMRVVHTEAALINSVNmtraeaqAAFG-NPT 197
Cdd:pfam07478 2 LKAAGLPVVPFvtfTRADWKLNPKEWCAqVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIE-------EAFQyDEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 198 VYMEKFLENpRHIEIQILADEYGNAIYLGER--DCSMQRRHQKVIEEA-----PApGITDKHRKKIGEACADACRKIGYR 270
Cdd:pfam07478 75 VLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALGCR 152
|
170 180
....*....|....*....|..
gi 1891815632 271 GAGTFE-FLFENGEFYFIEMNT 291
Cdd:pfam07478 153 GLARVDfFLTEDGEIVLNEVNT 174
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-311 |
5.89e-07 |
|
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: 50.71 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 16 RVLRACREMGIktvvvhseadrEAKYVKLADESVCIGPAPSPQSYLNIPAIisaaevtDA---QAIHPGYGFlsenaDFA 92
Cdd:COG0189 18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSEF-------DAvlpRIDPPFYGL-----ALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 93 ERVEQSGFVFIgPRPDSIRLMGDKVSAKDAMKAAAVPCvpgsdgalPD-----DPAEITRIAKRIGYPIIIKAAGGGGGR 167
Cdd:COG0189 75 RQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV--------PPtlvtrDPDDLRAFLEELGGPVVLKPLDGSGGR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 168 GMRVVHTEAALiNSVnmtrAEAQAAFGNPTVYMEKFLENPRHIEIQIladeygnaIYLGERD-CSMQRRHQK-------- 238
Cdd:COG0189 146 GVFLVEDEDAL-ESI----LEALTELGSEPVLVQEFIPEEDGRDIRV--------LVVGGEPvAAIRRIPAEgefrtnla 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891815632 239 ---VIEEAPAPgitdkhrKKIGEACADACRKIGYRGAGtFEFLFENGEFYFIEMNTRVQVEHpvTELITGIDIVQE 311
Cdd:COG0189 213 rggRAEPVELT-------DEERELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
92-359 |
7.28e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 51.70 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 92 AER--VEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCVPGSDGALPDdpaEITRIAKRIG-YPIIIKAAGGGGGRG 168
Cdd:PLN02735 119 AESgiLEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLD---ECFEIAEDIGeFPLIIRPAFTLGGTG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 169 MRVVHTEAALINSVNmtraEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLgerdCS------MQRRHQKVIEE 242
Cdd:PLN02735 196 GGIAYNKEEFETICK----AGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSienidpMGVHTGDSITV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 243 APAPGITDKHRKKIGEACADACRKIGYRGAGT---FEFLFENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQIRIAAGE 319
Cdd:PLN02735 268 APAQTLTDKEYQRLRDYSVAIIREIGVECGGSnvqFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGY 347
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1891815632 320 KLRYTQKDVVLRghamecrinaeDPFKFTPSPGRITTYHP 359
Cdd:PLN02735 348 TLDQIPNDITLK-----------TPASFEPSIDYVVTKIP 376
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
110-293 |
9.52e-07 |
|
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: 51.54 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 110 IRLMGDKVSA----------KDAMKAAAVPcVPGSDGALPDDPAEitRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAALI 179
Cdd:TIGR01369 112 VEVLGTPVEAikkaedrelfREAMKEIGEP-VPESEIAHSVEEAL--AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 180 NSVnmtrAEAQAAFGNPTVYMEKFLENPRHIEIQILADEYGNAIYLgerdCSMQR-----RHQ-KVIEEAPAPGITDKHR 253
Cdd:TIGR01369 189 EIA----ERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEY 260
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1891815632 254 KKIGEACADACRKIGYRGAGTFEFLF--ENGEFYFIEMNTRV 293
Cdd:TIGR01369 261 QMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPRV 302
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-324 |
1.35e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 50.74 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 96 EQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPcVPGSDGAlpDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTE 175
Cdd:PRK12815 109 EQYGVELLGTNIEAIQKGEDRERFRALMKELGEP-VPESEIV--TSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 176 AALInsvNMTRAEAQAAFGNpTVYMEKFLENPRHIEIQILADEYGNAIYLgerdCSMQRrhqkvIEE-----------AP 244
Cdd:PRK12815 186 EELE---QLFKQGLQASPIH-QCLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDPvgihtgdsivvAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 245 APGITDKHRKKIGEACADACRKIGYRGAGTFEFLF--ENGEFYFIEMNTRVQVEHPVTELITGIDIVqeqiRIAAGEKLR 322
Cdd:PRK12815 253 SQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALdpKSKQYYLIEVNPRVSRSSALASKATGYPIA----KIAAKLAVG 328
|
..
gi 1891815632 323 YT 324
Cdd:PRK12815 329 YT 330
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
20-204 |
3.89e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 48.61 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 20 ACREMGIKTVVVHSEADREAKYVklADESVCIgpapspqSYLNIPAIISAAE----VTdaqaihpgYGFlsEN--ADFAE 93
Cdd:PRK06019 20 AAAPLGYKVIVLDPDPDSPAAQV--ADEVIVA-------DYDDVAALRELAEqcdvIT--------YEF--ENvpAEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 94 RVEQSGFVFigPRPDSIRLMGDKVSAKDAMKAAAVPCVPGsdgALPDDPAEITRIAKRIGYPIIIKAAgggggrgmR--- 170
Cdd:PRK06019 81 ALAARVPVP--PGPDALAIAQDRLTEKQFLDKLGIPVAPF---AVVDSAEDLEAALADLGLPAVLKTR--------Rggy 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1891815632 171 ------VVHTEAALinsvnmtrAEAQAAFGNPTVYMEKFL 204
Cdd:PRK06019 148 dgkgqwVIRSAEDL--------EAAWALLGSVPCILEEFV 179
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
77-292 |
6.53e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 47.96 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 77 AIHPGY----GFLSENADfaeRVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPCvPGSdgALPDDPAEITRI--AK 150
Cdd:PRK12767 72 LLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPT-PKS--YLPESLEDFKAAlaKG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 151 RIGYPIIIKAAGGGGGRGMRVVHTEAALINsvnmtraeaqaafgnptvymeKFLENPRHIeIQ--ILADEYGNAIYL--- 225
Cdd:PRK12767 146 ELQFPLFVKPRDGSASIGVFKVNDKEELEF---------------------LLEYVPNLI-IQefIEGQEYTVDVLCdln 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1891815632 226 GERDCSMQRRHQKVIEEAPAPGITDKhRKKIGEACADACRKIGYRGAGTFEFLFENGEFYFIEMNTR 292
Cdd:PRK12767 204 GEVISIVPRKRIEVRAGETSKGVTVK-DPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
115-291 |
1.48e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 46.64 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 115 DKVSAKDAMKAAAVPcVPgsDGALPDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAALINSVnmtrAEAqAAFG 194
Cdd:PRK01372 98 DKLRTKLVWQAAGLP-TP--PWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL----ELA-FKYD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 195 NpTVYMEKFLENPrhiEIQ--ILADE-------------------Y--GNAIYLgerdCsmqrrhqkvieeaPApGITDK 251
Cdd:PRK01372 170 D-EVLVEKYIKGR---ELTvaVLGGKalpvieivpagefydyeakYlaGGTQYI----C-------------PA-GLPAE 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1891815632 252 HRKKIGEACADACRKIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:PRK01372 228 IEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYLLEVNT 268
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
92-321 |
4.05e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.24 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 92 AERVEQSGFVFIGPRPDSIRLMGDKVSAKDAMKAAAVPcVPGSDGALpdDPAEITRIAKRIGYPIII--------KAagg 163
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIP-QPPNGTAT--SVEEALEVAEEIGYPVLVrpsyvlggRA--- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 164 gggrgMRVVHTEAALINSVNmtraEAQAAFGNPTVYMEKFLENPRHIEIQILADeyGNAIYLGErdcSMQrrHqkvIEEA 243
Cdd:PRK05294 720 -----MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLIGG---IME--H---IEEA 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 244 -----------PAPGITDKHRKKIGEACADACRKIGYRGAGTFEFLFENGEFYFIEMNTRVQVEHPVTELITGIDIVQEQ 312
Cdd:PRK05294 781 gvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIA 860
|
....*....
gi 1891815632 313 IRIAAGEKL 321
Cdd:PRK05294 861 ARVMLGKKL 869
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
22-161 |
9.42e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 44.29 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 22 REMGIKTVVVHSEADREAKYVklADESVCigpapspQSYLNIPAIISAAE----VTdaqaihpgygFLSEN--ADFAERV 95
Cdd:COG0026 11 KRLGYRVHVLDPDPDSPAAQV--ADEHIV-------ADYDDEEALREFAErcdvVT----------FEFENvpAEALEAL 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891815632 96 EQSGFVFigPRPDSIRLMGDKVSAKDAMKAAAVPCVPGsdgALPDDPAEITRIAKRIGYPIIIKAA 161
Cdd:COG0026 72 EAEVPVR--PGPEALEIAQDRLLEKAFLAELGIPVAPF---AAVDSLEDLEAAIAELGLPAVLKTR 132
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
70-411 |
5.77e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 42.53 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 70 AEVTDAQAIHpgyGFLSENADFAERVEQSGFvFI-------------GPRPDSIRLMGDKVSAKDAMKAAAVPcVPGSDG 136
Cdd:PRK02186 53 ADTSDPDRIH---RFVSSLDGVAGIMSSSEY-FIevasevarrlglpAANTEAIRTCRDKKRLARTLRDHGID-VPRTHA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 137 ALPDdpAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAALINSVNMTRAEaqaafGNPTVYMEKFLENPRHiEIQILA 216
Cdd:PRK02186 128 LALR--AVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRA-----GTRAALVQAYVEGDEY-SVETLT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 217 DEYGNAI------YLGERDCSMQRRHqkvieEAPAPgITDKHRKKIGEACADACRKIGYR-GAGTFEFLFENGEFYFIEM 289
Cdd:PRK02186 200 VARGHQVlgitrkHLGPPPHFVEIGH-----DFPAP-LSAPQRERIVRTVLRALDAVGYAfGPAHTELRVRGDTVVIIEI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 290 NTR-------VQVEHpvtelITGIDIVQEQIRIAAGE-------KLRYTQKDVVLRGHAMECR-INAEDPFKFTPSPGRi 354
Cdd:PRK02186 274 NPRlaggmipVLLEE-----AFGVDLLDHVIDLHLGVaafadptAKRYGAIRFVLPARSGVLRgLLFLPDDIAARPELR- 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1891815632 355 ttYHPPGGPGIRMDShiyQGYFvppnyDSMIAKVISFGDTRDQAMARMRIALSEMVV 411
Cdd:PRK02186 348 --FHPLKQPGDALRL---EGDF-----RDRIAAVVCAGDHRDSVAAAAERAVAGLSI 394
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
115-291 |
1.14e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 40.87 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 115 DKVSAKDAMKAAAVPCVPgSDGALPDDPAEIT--RIAKRIGYPIIIKAAgggggrgmR--------VVHTEAALINSVnm 184
Cdd:PRK01966 123 DKILTKRLLAAAGIPVAP-YVVLTRGDWEEASlaEIEAKLGLPVFVKPA--------NlgssvgisKVKNEEELAAAL-- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 185 traeaQAAFGN-PTVYMEKFLeNPRHIEIQILadeyGN---AIYLGERDCS----------MQRRHQKVIeeaPAPgITD 250
Cdd:PRK01966 192 -----DLAFEYdRKVLVEQGI-KGREIECAVL----GNdpkASVPGEIVKPddfydyeakyLDGSAELII---PAD-LSE 257
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1891815632 251 KHRKKIGEACADACRKIGYRGAG--TFeFLFENGEFYFIEMNT 291
Cdd:PRK01966 258 ELTEKIRELAIKAFKALGCSGLArvDF-FLTEDGEIYLNEINT 299
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
99-292 |
2.96e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.15 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 99 GFVFI-GPRPDSIRLMGDKVSAKDAMKAAAVPCVPGsdgALPDDPAEITRIAKRIGYPIIIKAAGGGGGRGMRVVHTEAA 177
Cdd:PLN02735 685 GNVKIwGTSPDSIDAAEDRERFNAILNELKIEQPKG---GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891815632 178 LINSVNmTRAEAQAafGNPtVYMEKFLENPRHIEIQILADEYGN-------------AIYLGERDCSMqrrhqkvieeaP 244
Cdd:PLN02735 762 LKTYLE-TAVEVDP--ERP-VLVDKYLSDATEIDVDALADSEGNvviggimehieqaGVHSGDSACSL-----------P 826
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1891815632 245 APGITDKHRKKIGEACADACRKIGYRGAGTFEF-LFENGEFYFIEMNTR 292
Cdd:PLN02735 827 TQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPR 875
|
|
| |
