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Conserved domains on  [gi|917548753|gb|AKZ32347|]
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carbamoylphosphate synthase large subunit, partial [uncultured Planctomycetota bacterium]

Protein Classification

CarB family protein( domain architecture ID 1000166)

carB family protein such as the carbamoyl phosphate synthase large subunit, a component of the two-subunit enzyme that catalyzes the reaction of bicarbonate, glutamine, and two molecules of MgATP, to produce carbamoyl phosphate, an intermediate in the biosynthesis of arginine and pyrimidine nucleotides

EC:  6.3.5.5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carB super family cl35300
carbamoyl-phosphate synthase large subunit;
4-225 1.45e-146

carbamoyl-phosphate synthase large subunit;


The actual alignment was detected with superfamily member PRK05294:

Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 434.91  E-value: 1.45e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTDVYVAGVMEHIEE 83
Cdd:PRK05294  700 AEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEE 779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   84 AGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKI 163
Cdd:PRK05294  780 AGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKI 859

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917548753  164 AAKAMAGVKLADLDIV-ALPPGLVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PRK05294  860 AARVMLGKKLAELGYTkGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEA 922
 
Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
4-225 1.45e-146

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 434.91  E-value: 1.45e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTDVYVAGVMEHIEE 83
Cdd:PRK05294  700 AEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEE 779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   84 AGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKI 163
Cdd:PRK05294  780 AGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKI 859

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917548753  164 AAKAMAGVKLADLDIV-ALPPGLVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PRK05294  860 AARVMLGKKLAELGYTkGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEA 922
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 4-225 4.19e-127

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: 369.59  E-value: 4.19e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTD-VYVAGVMEHIE 82
Cdd:COG0458  145 AEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVIIVGIMEHIE 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  83 EAGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAK 162
Cdd:COG0458  225 PAGVHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAK 304

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917548753 163 IAAKAMAGVKLADLDivaLPPGL------VAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:COG0458  305 IAAKLALGYTLDELG---NDTGFeptldyVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEA 370
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 4-225 1.49e-108

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: 335.05  E-value: 1.49e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753     4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTDVYVAGVMEHIEE 83
Cdd:TIGR01369  700 ASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    84 AGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKI 163
Cdd:TIGR01369  780 AGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKL 859

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917548753   164 AAKAMAGVKLADLD-IVALPPGLVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:TIGR01369  860 AVRVMLGKKLEELGvGKEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEA 922
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 4-173 1.02e-29

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: 109.70  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDL----ESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTD-VYVAGVM 78
Cdd:pfam02786  34 AKEIGYPVIIKAAFGGGGLGMGIARNEEELaelfALALAEAPAAFGNPQVLVEKSLKGPKHIEYQVLRDAHGnCITVCNR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   79 EHIEEagVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQ--DGEIFVLEVNPRASRTVPFVAKAT 156
Cdd:pfam02786 114 ECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDpfSGEYYFIEMNTRLQVEHALAEKAT 191

                         170
                  ....*....|....*..
gi 917548753  157 GVPVAKIAAKAMAGVKL 173
Cdd:pfam02786 192 GYDLAKEAAKIALGYPL 208
 
Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
4-225 1.45e-146

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 434.91  E-value: 1.45e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTDVYVAGVMEHIEE 83
Cdd:PRK05294  700 AEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEE 779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   84 AGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKI 163
Cdd:PRK05294  780 AGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKI 859

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917548753  164 AAKAMAGVKLADLDIV-ALPPGLVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PRK05294  860 AARVMLGKKLAELGYTkGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEA 922
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 4-225 4.19e-127

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: 369.59  E-value: 4.19e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTD-VYVAGVMEHIE 82
Cdd:COG0458  145 AEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVIIVGIMEHIE 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  83 EAGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAK 162
Cdd:COG0458  225 PAGVHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAK 304

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917548753 163 IAAKAMAGVKLADLDivaLPPGL------VAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:COG0458  305 IAAKLALGYTLDELG---NDTGFeptldyVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEA 370
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 4-225 1.49e-108

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: 335.05  E-value: 1.49e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753     4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTDVYVAGVMEHIEE 83
Cdd:TIGR01369  700 ASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    84 AGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKI 163
Cdd:TIGR01369  780 AGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKL 859

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917548753   164 AAKAMAGVKLADLD-IVALPPGLVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:TIGR01369  860 AVRVMLGKKLEELGvGKEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEA 922
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 4-225 2.28e-100

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 313.44  E-value: 2.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAirVSGDAPLLLDRYLrDAIEIDVDAVCDGTDVYVAGVMEHIEE 83
Cdd:PRK12815  701 AKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQ 777

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   84 AGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKI 163
Cdd:PRK12815  778 AGVHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKL 857

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917548753  164 AAKAMAGVKLADLDI-VALPPG--LVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PRK12815  858 ATKVLLGKSLAELGYpNGLWPGspFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEA 922
PLN02735 PLN02735
carbamoyl-phosphate synthase
 4-225 3.73e-91

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 289.37  E-value: 3.73e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGT-DVYVAGVMEHIE 82
Cdd:PLN02735  733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIE 812

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   83 EAGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLEVNPRASRTVPFVAKATGVPVA 161
Cdd:PLN02735  813 QAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLA 892

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917548753  162 KIAAKAMAGVKLADLDIVALP-PGLVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PLN02735  893 KYASLVMSGKSLKDLGFTEEViPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKA 957
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 4-225 4.27e-42

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 151.66  E-value: 4.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAV--CDGTDVYVaGVMEHI 81
Cdd:PRK12815  159 AEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMrdRNGNCITV-CNMENI 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   82 EEAGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI--QDGEIFVLEVNPRASRTVPFVAKATGVP 159
Cdd:PRK12815  238 DPVGIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALdpKSKQYYLIEVNPRVSRSSALASKATGYP 317

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917548753  160 VAKIAAKAMAGVKLADL-------DIVALPPGL--VAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PRK12815  318 IAKIAAKLAVGYTLNELknpvtglTYASFEPALdyVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESA 392
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 4-225 2.73e-41

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: 149.38  E-value: 2.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753     4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCD--GTDVYVAGvMEHI 81
Cdd:TIGR01369  158 AKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDsnDNCITVCN-MENF 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    82 EEAGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQ--DGEIFVLEVNPRASRTVPFVAKATGVP 159
Cdd:TIGR01369  237 DPMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpdSGRYYVIEVNPRVSRSSALASKATGYP 316

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917548753   160 VAKIAAKAMAGVKLADL--DIV-----ALPPGL--VAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:TIGR01369  317 IAKVAAKLAVGYTLDELknPVTgttpaSFEPSLdyVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEA 391
carB PRK05294
carbamoyl-phosphate synthase large subunit;
4-225 4.76e-36

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 134.45  E-value: 4.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTD--VYVAGvMEHI 81
Cdd:PRK05294  159 AEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDncIIVCS-IENI 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   82 EEAGVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDV-RGLMNVQFAI--QDGEIFVLEVNPRASRTVPFVAKATGV 158
Cdd:PRK05294  238 DPMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVeTGGCNVQFALnpKDGRYIVIEMNPRVSRSSALASKATGY 317

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917548753  159 PVAKIAAKAMAGVKLADL--DIV-----ALPPGL--VAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFETA 225
Cdd:PRK05294  318 PIAKVAAKLAVGYTLDEIknDITgktpaSFEPSLdyVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEES 393
PLN02735 PLN02735
carbamoyl-phosphate synthase
 9-223 8.81e-31

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 119.11  E-value: 8.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    9 YPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTD-VYVAGVMEHIEEAGVH 87
Cdd:PLN02735  181 FPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADnVVIICSIENIDPMGVH 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   88 SGDSACALPPYSLDAAMIERLKVQAEKLARGLDVR-GLMNVQFAI--QDGEIFVLEVNPRASRTVPFVAKATGVPVAKIA 164
Cdd:PLN02735  261 TGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVnpVDGEVMIIEMNPRVSRSSALASKATGFPIAKMA 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917548753  165 AKAMAGVKLADL--DIVALPPG-------LVAVKEAVMPFARFPGVDPVLGPEMRSTGEVMGFDVTFE 223
Cdd:PLN02735  341 AKLSVGYTLDQIpnDITLKTPAsfepsidYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQ 408
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 4-173 1.02e-29

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: 109.70  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDL----ESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTD-VYVAGVM 78
Cdd:pfam02786  34 AKEIGYPVIIKAAFGGGGLGMGIARNEEELaelfALALAEAPAAFGNPQVLVEKSLKGPKHIEYQVLRDAHGnCITVCNR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   79 EHIEEagVHSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQ--DGEIFVLEVNPRASRTVPFVAKAT 156
Cdd:pfam02786 114 ECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDpfSGEYYFIEMNTRLQVEHALAEKAT 191

                         170
                  ....*....|....*..
gi 917548753  157 GVPVAKIAAKAMAGVKL 173
Cdd:pfam02786 192 GYDLAKEAAKIALGYPL 208
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 4-170 3.76e-15

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: 72.21  E-value: 3.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYV----GEAIRVSGDAPLLLDRYLrDAIEIDVDAVCDGTDVYVAGVME 79
Cdd:COG0439   85 AEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITR 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  80 HIEEA--GVHSGDSAcalpPYSLDAAMIERLKVQAEKLARGLDV-RGLMNVQFAI-QDGEIFVLEVNPRAS--RTVPFVA 153
Cdd:COG0439  164 KHQKPpyFVELGHEA----PSPLPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTE 239

                        170
                 ....*....|....*..
gi 917548753 154 KATGVPVAKIAAKAMAG 170
Cdd:COG0439  240 LATGVDLVREQIRLALG 256
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 4-174 6.41e-11

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 61.20  E-value: 6.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDL----ESYVGEAIRVSGDAPLLLDRYLRDA--IEIDVDAVCDGTDVYVaGV 77
Cdd:PRK06111 148 ARQIGYPVMLKASAGGGGIGMQLVETEQELtkafESNKKRAANFFGNGEMYIEKYIEDPrhIEIQLLADTHGNTVYL-WE 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  78 ME------H---IEEAgvhsgdsacalPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGE-IFVLEVNPRASR 147
Cdd:PRK06111 227 REcsvqrrHqkvIEEA-----------PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQV 295

                        170       180
                 ....*....|....*....|....*..
gi 917548753 148 TVPFVAKATGVPVAKIAAKAMAGVKLA 174
Cdd:PRK06111 296 EHPVTEEITGIDLVEQQLRIAAGEKLS 322
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 6-155 9.33e-10

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 57.20  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   6 ALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAirvsgdAPLLLDRYLRDaIEIDVDAVCDGTDVYVAGV-MEHIEea 84
Cdd:PRK12767 146 ELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV------PNLIIQEFIEG-QEYTVDVLCDLNGEVISIVpRKRIE-- 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917548753  85 gVHSGDSACAlppYSLDAamiERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKA 155
Cdd:PRK12767 217 -VRAGETSKG---VTVKD---PELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPLSYMA 280
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-144 1.34e-08

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 54.37  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    1 RVEARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVS----GDAPLLLDRYLRDAIEIDVDAVCDGTdvyvaG 76
Cdd:PRK12999  149 LEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAkaafGNDEVYLEKYVENPRHIEVQILGDKH-----G 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   77 VMEH---------------IEEAgvhsgdsacalPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLE 140
Cdd:PRK12999  224 NVVHlyerdcsvqrrhqkvVEIA-----------PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIE 292


                  ....
gi 917548753  141 VNPR 144
Cdd:PRK12999  293 VNPR 296
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 4-158 4.63e-08

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 52.83  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYV----GEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGTDVyvagvme 79
Cdd:PRK12833 151 AARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELplaqREAQAAFGDGGVYLERFIARARHIEVQILGDGERV------- 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  80 hieeagVHSGDSACAL-----------PPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQD--GEIFVLEVNPRAS 146
Cdd:PRK12833 224 ------VHLFERECSLqrrrqkileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQ 297

                        170
                 ....*....|..
gi 917548753 147 RTVPFVAKATGV 158
Cdd:PRK12833 298 VEHPVTEAITGI 309
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 6-158 5.40e-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: 51.16  E-value: 5.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    6 ALGYPLVLRPSfVLGGR-AMEIVRSEEDLESYVGEAIRVsgDAPLLLDRYLrDAIEIDVdAVCDGTDVYVAGVMEHIEEA 84
Cdd:pfam07478  34 ALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQY--DEKVLVEEGI-EGREIEC-AVLGNEDPEVSPVGEIVPSG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   85 GV------HSGDSACALPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQ-DGEIFVLEVNPRASRT----VPFVA 153
Cdd:pfam07478 109 GFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFFLTeDGEIVLNEVNTIPGFTsismFPKLA 188


                  ....*
gi 917548753  154 KATGV 158
Cdd:pfam07478 189 AAAGV 193
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
4-174 1.13e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 51.52  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVS----GDAPLLLDRYLRDA--IEIDVDAVCDGTDVYVaGV 77
Cdd:PRK08654 148 AEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAqsafGDSTVFIEKYLEKPrhIEIQILADKHGNVIHL-GD 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  78 ME------H---IEEAgvhsgdsacalPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRT 148
Cdd:PRK08654 227 REcsiqrrHqklIEEA-----------PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVE 295

                        170       180
                 ....*....|....*....|....*.
gi 917548753 149 VPFVAKATGVPVAKIAAKAMAGVKLA 174
Cdd:PRK08654 296 HPITEMVTGIDIVKEQIKIAAGEELS 321
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
 97-171 5.26e-07

Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];


Pssm-ID: 441833 [Multi-domain]  Cd Length: 370  Bit Score: 49.53  E-value: 5.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917548753  97 PYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPFVAKATGVPVAKIAAKAMAGV 171
Cdd:COG2232  215 PLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE 289
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 4-176 1.05e-06

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: 48.18  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFvlGG--RAMEIVRSEEDLESYVGEAIRVsgDAPLLLDRYLrDAIEIDVdAVCDGTDVYVAGVMEHI 81
Cdd:COG1181  128 EEELGLPLFVKPAR--EGssVGVSKVKNAEELAAALEEAFKY--DDKVLVEEFI-DGREVTV-GVLGNGGPRALPPIEIV 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  82 EEAGV-------HSGDSACALPPySLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLEVNprasrTVPFVA 153
Cdd:COG1181  202 PENGFydyeakyTDGGTEYICPA-RLPEELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVN-----TLPGMT 275

                        170       180
                 ....*....|....*....|...
gi 917548753 154 KATGVPvakIAAKAmAGVKLADL 176
Cdd:COG1181  276 PTSLLP---KAAAA-AGISYEEL 294
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
4-144 1.58e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 48.20  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLE----SYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDgtdvyvagvmE 79
Cdd:PRK08462 150 AKEIGYPVILKAAAGGGGRGMRVVEDESDLEnlylAAESEALSAFGDGTMYMEKFINNPRHIEVQILGD----------K 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917548753  80 HieEAGVHSGDSACAL-----------PPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLEVNPR 144
Cdd:PRK08462 220 H--GNVIHVGERDCSLqrrhqklieesPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTR 294
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 1-144 1.64e-06

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 46.48  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    1 RVEARALGYPLVLRPSfVLG--GRAMEIVRSEEDLEsyvgEAIRVSGDAPLLLDRYLRDAIEIDVDAV--CDGtDVYVAG 76
Cdd:pfam02222  20 IEAGQELGYPCVVKAR-RGGydGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVrsVDG-ETAFYP 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917548753   77 VMEHIEEAGVhsgdsaCAL--PPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQ-FAIQDGEIFVLEVNPR 144
Cdd:pfam02222  94 VVETIQEDGI------CRLsvAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDLLINELAPR 158
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
4-170 1.82e-06

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 47.62  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPS--------FVLGGRAMEIVRSEEDLESYVgEAIRVSGdAPLLLDRYL--RDAIEIDVDAVCDGT-DV 72
Cdd:COG3919  148 AEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALL-RRIAAAG-YELIVQEYIpgDDGEMRGLTAYVDRDgEV 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  73 YVAGVMEHIEEAGVHSGDSACALPPYslDAAMIErlkvQAEKLARGLDVRGLMNVQFAI--QDGEIFVLEVNPRASRTVP 150
Cdd:COG3919  226 VATFTGRKLRHYPPAGGNSAARESVD--DPELEE----AARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRFWRSLY 299

                        170       180
                 ....*....|....*....|
gi 917548753 151 FVAKAtGVPVAKIAAKAMAG 170
Cdd:COG3919  300 LATAA-GVNFPYLLYDDAVG 318
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 3-144 2.89e-06

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: 47.38  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    3 EARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGEAIRVS----GDAPLLLDRYLRDAIEIDVDAVCDGTdvyvaGVM 78
Cdd:COG1038   150 FAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAkaafGDDEVFLEKYIERPKHIEVQILGDKH-----GNI 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   79 EH---------------IEEAgvhsgdsacalPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLEVN 142
Cdd:COG1038   225 VHlferdcsvqrrhqkvVEIA-----------PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVN 293


                  ..
gi 917548753  143 PR 144
Cdd:COG1038   294 PR 295
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
3-174 3.29e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 47.01  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   3 EARALGYPLVLRPSFVLGGRAMEIVRSEEDL----ESYVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCDGtdvyvagvM 78
Cdd:PRK05586 147 IAKEIGYPVMVKASAGGGGRGIRIVRSEEELikafNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDN--------Y 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  79 EHIeeagVHSGDSACAL-----------PPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLEVNPRAS 146
Cdd:PRK05586 219 GNV----VHLGERDCSLqrrnqkvleeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQ 294

                        170       180
                 ....*....|....*....|....*...
gi 917548753 147 RTVPFVAKATGVPVAKIAAKAMAGVKLA 174
Cdd:PRK05586 295 VEHPITEMITGVDLVKEQIKIAYGEKLS 322
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 4-144 5.70e-06

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 46.33  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYV----GEAIRVSGDAPLLLDRYLRDA--IEIDVDAvcDGtdvyvagv 77
Cdd:PRK08591 148 AKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFsmarAEAKAAFGNPGVYMEKYLENPrhIEIQVLA--DG-------- 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917548753  78 mehiEEAGVHSGDSACAL-----------PPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAIQ-DGEIFVLEVNPR 144
Cdd:PRK08591 218 ----HGNAIHLGERDCSLqrrhqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTR 292
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 3-144 2.46e-05

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 43.14  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753    3 EARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVGeairvsgdaPLLLDRYLrDAIEIDVDAVCDGTDVYVAGV-MEHI 81
Cdd:pfam02655  26 ELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE---------NVLVQEFI-EGEPLSVSLLSDGEKALPLSVnRQYI 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917548753   82 EEAGVHSGDSACALP-PYSLDAAMIErlkvQAEKLARGL-DVRGLMNVQFAIQDGEIFVLEVNPR 144
Cdd:pfam02655  96 DNGGSGFVYAGNVTPsRTELKEEIIE----LAEEVVECLpGLRGYVGVDLVLKDNEPYVIEVNPR 156
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 4-169 4.11e-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: 43.39  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYVgEAIRVSGDAPLLLDRYLRDAIEIDVDA-VCDGTdvyVAGVMEHIE 82
Cdd:COG0189  127 LEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL-EALTELGSEPVLVQEFIPEEDGRDIRVlVVGGE---PVAAIRRIP 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  83 EAG-----VHSGDSACalpPYSLDAAMIERlkvqAEKLAR--GLDVRGlmnVQFAIQDGEIFVLEVNPRASrtVPFVAKA 155
Cdd:COG0189  203 AEGefrtnLARGGRAE---PVELTDEEREL----ALRAAPalGLDFAG---VDLIEDDDGPLVLEVNVTPG--FRGLERA 270

                        170
                 ....*....|....
gi 917548753 156 TGVPVAKIAAKAMA 169
Cdd:COG0189  271 TGVDIAEAIADYLE 284
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
 112-175 1.18e-04

ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434824 [Multi-domain]  Cd Length: 131  Bit Score: 40.67  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917548753  112 AEKLARGLDVRGLMNVQFAIQDGEIFVLEVNPRASRTVPfVAKATGVPVAKIAAKAMAGVKLAD 175
Cdd:pfam15632  53 ARRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD 115
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 3-150 4.08e-04

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 40.48  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   3 EARALGYPLVLRPsfVLGGR--AMEIVRSEEDLESYVGEAIR----------VSGD---APLLLDRYLrDAIEI------ 61
Cdd:PRK01372 128 AIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKyddevlvekyIKGReltVAVLGGKAL-PVIEIvpagef 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  62 -DVDAVcdgtdvYVAGVMEHIEEAGvhsgdsacalppysLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVL 139
Cdd:PRK01372 205 yDYEAK------YLAGGTQYICPAG--------------LPAEIEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYLL 264

                        170
                 ....*....|.
gi 917548753 140 EVNprasrTVP 150
Cdd:PRK01372 265 EVN-----TQP 270
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 4-171 1.97e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 39.06  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFVLGGRAMEIVRSEEDLESYvGEAIRVSGDAPLLLDRYLrDAIEIDVDAVCDGTDVYVAGVMehiee 83
Cdd:PRK02186 138 LDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAH-CAALRRAGTRAALVQAYV-EGDEYSVETLTVARGHQVLGIT----- 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  84 aGVHSGDSACALP-----PYSLDAAMIERLkvqAEKLARGLDVRGL----MNVQFAIQDGEIFVLEVNPR-ASRTVP-FV 152
Cdd:PRK02186 211 -RKHLGPPPHFVEighdfPAPLSAPQRERI---VRTVLRALDAVGYafgpAHTELRVRGDTVVIIEINPRlAGGMIPvLL 286

                        170
                 ....*....|....*....
gi 917548753 153 AKATGVPVAKIAAKAMAGV 171
Cdd:PRK02186 287 EEAFGVDLLDHVIDLHLGV 305
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 4-144 4.87e-03

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: 37.36  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   4 ARALGYPLVLRPSFvLG--GRAMEIVRSEEDLEsyvgEAIRVSGDAPLLLDRYLRDAIEIDVDAV--CDG-TDVYVAGVM 78
Cdd:COG0026  120 IAELGLPAVLKTRR-GGydGKGQVVIKSAADLE----AAWAALGGGPCILEEFVPFERELSVIVArsPDGeVATYPVVEN 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917548753  79 EHieEAGVhsgdsaCA--LPPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQ-FAIQDGEIFVLEVNPR 144
Cdd:COG0026  195 VH--RNGI------LDesIAPARISEALAAEAEEIAKRIAEALDYVGVLAVEfFVTKDGELLVNEIAPR 255
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
3-174 8.62e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 36.62  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753   3 EARALGYPLVLRPSFVLGGRAMEIVRSEEDLES----YVGEAIRVSGDAPLLLDRYLRDAIEIDVDAVCD--GTdvyvag 76
Cdd:PRK07178 146 EAERIGYPVMLKATSGGGGRGIRRCNSREELEQnfprVISEATKAFGSAEVFLEKCIVNPKHIEVQILADshGN------ 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917548753  77 vmehieeaGVHSGDSACAL-----------PPYSLDAAMIERLKVQAEKLARGLDVRGLMNVQFAI-QDGEIFVLEVNPR 144
Cdd:PRK07178 220 --------VVHLFERDCSIqrrnqklieiaPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTR 291

                        170       180       190
                 ....*....|....*....|....*....|
gi 917548753 145 ASRTVPFVAKATGVPVAKIAAKAMAGVKLA 174
Cdd:PRK07178 292 VQVEHTITEEITGIDIVREQIRIASGLPLS 321
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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