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Conserved domains on  [gi|2027315838|gb|QTY39190|]
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CAD, partial [Bembidion corgenoma]

Protein Classification

carbamoyl-phosphate synthase large subunit family protein( domain architecture ID 1002141)

carbamoyl-phosphate synthase (CPSase) large subunit family protein; CPSase catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis

CATH:  3.30.470.20|1.10.1030.10|3.30.1490.20|3.40.50.1380
Gene Ontology:  GO:0005951
PubMed:  9914247|11212301
SCOP:  4001126|4002053|4003761|4003858

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-259 6.59e-131

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]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 395.52  E-value: 6.59e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    1 LSKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYIRKVDD-----EELKEPTDKRMFVVAAALKE 75
Cdd:TIGR01369  361 FDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPdedlwRALKKPTDRRIFAIAEALRR 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   76 GYTVDKLYELTKIDRWFLQKMKHIIDyqtLLERKDQHSLTYID---LLKAKQIGFSDKQIAASVKSTELAIRKQREECGV 152
Cdd:TIGR01369  441 GVSVDEIHELTKIDRWFLHKIKNIVD---LEEELEEVKLTDLDpelLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGI 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  153 LPFVKQIDTVAAEWPATTNYLYITYNASSHDLEFKE-EHTMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYN 231
Cdd:TIGR01369  518 MPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYN 597

                          250       260
                   ....*....|....*....|....*...
gi 2027315838  232 PETVSTDYDMSDRLYFEEISFEVVMDIY 259
Cdd:TIGR01369  598 PETVSTDYDTSDRLYFEPLTFEDVMNII 625
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-259 6.59e-131

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: 395.52  E-value: 6.59e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    1 LSKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYIRKVDD-----EELKEPTDKRMFVVAAALKE 75
Cdd:TIGR01369  361 FDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPdedlwRALKKPTDRRIFAIAEALRR 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   76 GYTVDKLYELTKIDRWFLQKMKHIIDyqtLLERKDQHSLTYID---LLKAKQIGFSDKQIAASVKSTELAIRKQREECGV 152
Cdd:TIGR01369  441 GVSVDEIHELTKIDRWFLHKIKNIVD---LEEELEEVKLTDLDpelLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGI 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  153 LPFVKQIDTVAAEWPATTNYLYITYNASSHDLEFKE-EHTMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYN 231
Cdd:TIGR01369  518 MPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYN 597

                          250       260
                   ....*....|....*....|....*...
gi 2027315838  232 PETVSTDYDMSDRLYFEEISFEVVMDIY 259
Cdd:TIGR01369  598 PETVSTDYDTSDRLYFEPLTFEDVMNII 625
carB PRK05294
carbamoyl-phosphate synthase large subunit;
3-260 1.71e-116

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 357.87  E-value: 1.71e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    3 KFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYIRKVDD-----EELKEPTDKRMFVVAAALKEGY 77
Cdd:PRK05294   365 KFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDLFEEESleelrEELKEPTPERLFYIAEAFRRGA 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   78 TVDKLYELTKIDRWFLQKMKHIIDYQTLLERKDQhSLTYIDLLKAKQIGFSDKQIAASVKSTELAIRKQREECGVLPFVK 157
Cdd:PRK05294   445 SVEEIHELTKIDPWFLEQIEEIVELEEELKENGL-PLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYK 523

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  158 QIDTVAAEWPATTNYLYITYNASSHDLEFKEEHTMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVST 237
Cdd:PRK05294   524 RVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVST 603

                          250       260
                   ....*....|....*....|...
gi 2027315838  238 DYDMSDRLYFEEISFEVVMDIYN 260
Cdd:PRK05294   604 DYDTSDRLYFEPLTLEDVLEIIE 626
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 55-177 2.80e-56

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 176.10  E-value: 2.80e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   55 DEELKEPTDKRMFVVAAALKEGYTVDKLYELTKIDRWFLQKMKHIIDYQTLLERKDQHSLTYIDLLKAKQIGFSDKQIAA 134
Cdd:smart01096   2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2027315838  135 SVKSTELAIRKQREECGVLPFVKQIDTVAAEWPATTNYLYITY 177
Cdd:smart01096  82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 56-134 9.32e-34

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 117.09  E-value: 9.32e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027315838  56 EELKEPTDKRMFVVAAALKEGYTVDKLYELTKIDRWFLQKMKHIIDYQTLLeRKDQHSLTYIDLLKAKQIGFSDKQIAA 134
Cdd:pfam02787   1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKEL-KEAGLDLDAELLREAKRLGFSDRQIAK 78
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 2-196 2.21e-33

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: 126.92  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   2 SKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTG--FDPYIRKVDDEELKE--PTDKRMFVVAAALKEGY 77
Cdd:COG0458   341 EKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSLVADDDKEEALLlaRRLARLGFLIEATRGTA 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  78 TVDKLYELTKIDRWFLQKMKHIIdyqTLLERKDQHSLTYIDLLKAKQIGFSDKQIAASVKSTELAIRKQREECGVLPFVK 157
Cdd:COG0458   421 EVLEEAGITVIDVFKLSEGRPII---VDEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIK 497

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2027315838 158 QIDTVAAEWPATTNYLYITYNASSHDLEFKEEHTMVLGS 196
Cdd:COG0458   498 AVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-259 6.59e-131

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: 395.52  E-value: 6.59e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    1 LSKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYIRKVDD-----EELKEPTDKRMFVVAAALKE 75
Cdd:TIGR01369  361 FDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPdedlwRALKKPTDRRIFAIAEALRR 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   76 GYTVDKLYELTKIDRWFLQKMKHIIDyqtLLERKDQHSLTYID---LLKAKQIGFSDKQIAASVKSTELAIRKQREECGV 152
Cdd:TIGR01369  441 GVSVDEIHELTKIDRWFLHKIKNIVD---LEEELEEVKLTDLDpelLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGI 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  153 LPFVKQIDTVAAEWPATTNYLYITYNASSHDLEFKE-EHTMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYN 231
Cdd:TIGR01369  518 MPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYN 597

                          250       260
                   ....*....|....*....|....*...
gi 2027315838  232 PETVSTDYDMSDRLYFEEISFEVVMDIY 259
Cdd:TIGR01369  598 PETVSTDYDTSDRLYFEPLTFEDVMNII 625
carB PRK05294
carbamoyl-phosphate synthase large subunit;
3-260 1.71e-116

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 357.87  E-value: 1.71e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    3 KFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYIRKVDD-----EELKEPTDKRMFVVAAALKEGY 77
Cdd:PRK05294   365 KFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDLFEEESleelrEELKEPTPERLFYIAEAFRRGA 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   78 TVDKLYELTKIDRWFLQKMKHIIDYQTLLERKDQhSLTYIDLLKAKQIGFSDKQIAASVKSTELAIRKQREECGVLPFVK 157
Cdd:PRK05294   445 SVEEIHELTKIDPWFLEQIEEIVELEEELKENGL-PLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYK 523

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  158 QIDTVAAEWPATTNYLYITYNASSHDLEFKEEHTMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVST 237
Cdd:PRK05294   524 RVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVST 603

                          250       260
                   ....*....|....*....|...
gi 2027315838  238 DYDMSDRLYFEEISFEVVMDIYN 260
Cdd:PRK05294   604 DYDTSDRLYFEPLTLEDVLEIIE 626
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 3-258 2.28e-78

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 255.66  E-value: 2.28e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    3 KFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYI--RKVDDEELKE----PTDKRMFVVAAALKEG 76
Cdd:PRK12815   364 KFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGLSLPIelSGKSDEELLQdlrhPDDRRLFALLEALRRG 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   77 YTVDKLYELTKIDRWFLQKMKHIIDY-QTLLERKDQhsLTYIDLLKAKQIGFSDKQIAASVKSTELAIRKQREECGVLPF 155
Cdd:PRK12815   444 ITYEEIHELTKIDPFFLQKFEHIVALeKKLAEDGLD--LSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPS 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  156 VKQIDTVAAEWPATTNYLYITYNASShDLEFKEEH--TMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPE 233
Cdd:PRK12815   522 YKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEKkkVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPE 600

                          250       260
                   ....*....|....*....|....*
gi 2027315838  234 TVSTDYDMSDRLYFEEISFEVVMDI 258
Cdd:PRK12815   601 TVSTDYDTADRLYFEPLTLEDVLNV 625
PLN02735 PLN02735
carbamoyl-phosphate synthase
 3-258 4.25e-72

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 238.52  E-value: 4.25e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838    3 KFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTGFDPYIRKV---DDEELKE----PTDKRMFVVAAALKE 75
Cdd:PLN02735   382 KFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETGFSGWGCAKVKEldwDWEQLKYklrvPNPDRIHAIYAAMKK 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   76 GYTVDKLYELTKIDRWFLQKMKHIIDYQTLLERKDQHSLTYIDLLKAKQIGFSDKQIAASVKSTELAIRKQREECGVLPF 155
Cdd:PLN02735   462 GMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPS 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  156 VKQIDTVAAEWPATTNYLYITYNASSHDLEFKEEHTMVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETV 235
Cdd:PLN02735   542 YKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETV 621

                          250       260
                   ....*....|....*....|...
gi 2027315838  236 STDYDMSDRLYFEEISFEVVMDI 258
Cdd:PLN02735   622 STDYDTSDRLYFEPLTVEDVLNV 644
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 55-177 2.80e-56

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 176.10  E-value: 2.80e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   55 DEELKEPTDKRMFVVAAALKEGYTVDKLYELTKIDRWFLQKMKHIIDYQTLLERKDQHSLTYIDLLKAKQIGFSDKQIAA 134
Cdd:smart01096   2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2027315838  135 SVKSTELAIRKQREECGVLPFVKQIDTVAAEWPATTNYLYITY 177
Cdd:smart01096  82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 56-134 9.32e-34

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 117.09  E-value: 9.32e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027315838  56 EELKEPTDKRMFVVAAALKEGYTVDKLYELTKIDRWFLQKMKHIIDYQTLLeRKDQHSLTYIDLLKAKQIGFSDKQIAA 134
Cdd:pfam02787   1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKEL-KEAGLDLDAELLREAKRLGFSDRQIAK 78
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 2-196 2.21e-33

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: 126.92  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838   2 SKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALRMVDENVTG--FDPYIRKVDDEELKE--PTDKRMFVVAAALKEGY 77
Cdd:COG0458   341 EKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSLVADDDKEEALLlaRRLARLGFLIEATRGTA 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027315838  78 TVDKLYELTKIDRWFLQKMKHIIdyqTLLERKDQHSLTYIDLLKAKQIGFSDKQIAASVKSTELAIRKQREECGVLPFVK 157
Cdd:COG0458   421 EVLEEAGITVIDVFKLSEGRPII---VDEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIK 497

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2027315838 158 QIDTVAAEWPATTNYLYITYNASSHDLEFKEEHTMVLGS 196
Cdd:COG0458   498 AVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 194-259 1.10e-31

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: 121.91  E-value: 1.10e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027315838 194 LGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIY 259
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDII 66
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 192-258 3.10e-12

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 66.18  E-value: 3.10e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027315838  192 MVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDI 258
Cdd:TIGR01369   10 LVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKI 76
carB PRK05294
carbamoyl-phosphate synthase large subunit;
192-255 4.33e-10

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 59.73  E-value: 4.33e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027315838  192 MVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVSTDYDMSDRLYFEEISFEVV 255
Cdd:PRK05294    11 LIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFV 74
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 192-258 1.70e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 54.98  E-value: 1.70e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027315838  192 MVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDI 258
Cdd:PRK12815    11 LVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRI 77
PLN02735 PLN02735
carbamoyl-phosphate synthase
 192-258 3.10e-08

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 54.01  E-value: 3.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027315838  192 MVLGSGVYRIGSSVEFDWCAVGCLRELRKLGRKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDI 258
Cdd:PLN02735    27 MILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQV 93
carB PRK05294
carbamoyl-phosphate synthase large subunit;
2-35 3.40e-06

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 47.78  E-value: 3.40e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2027315838    2 SKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKA 35
Cdd:PRK05294   893 NKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 2-37 2.14e-05

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 45.38  E-value: 2.14e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2027315838    2 SKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKALR 37
Cdd:TIGR01369  893 SKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQL 928
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 2-35 1.02e-04

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 43.42  E-value: 1.02e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2027315838    2 SKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKA 35
Cdd:PRK12815   893 LKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKG 926
 
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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