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Conserved domains on  [gi|1510266648|gb|AYR17031|]
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carbomoylphosphate synthase, partial [Hybos grossipes]

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 ...
 1-270 7.44e-140

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: 419.02  E-value: 7.44e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFD---PYVKDVNE--EELIQAT 75
Cdd:TIGR01369  348 SLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDlpdREVEPDEDlwRALKKPT 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   76 DKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIK-LNRDTLLKAKKLGFSDNQIANAVKSTELV 154
Cdd:TIGR01369  428 DRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPELLRRAKKLGFSDAQIARLIGVTEAE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  155 VRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNAITSDIDFPGGFTIVV-GSGVYRIGSSVEFDWCAVGCLRELRKL 233
Cdd:TIGR01369  508 VRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPNRIGQGVEFDYCCVHAVLALREL 587

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1510266648  234 GRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:TIGR01369  588 GYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNI 624
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-270 7.44e-140

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: 419.02  E-value: 7.44e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFD---PYVKDVNE--EELIQAT 75
Cdd:TIGR01369  348 SLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDlpdREVEPDEDlwRALKKPT 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   76 DKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIK-LNRDTLLKAKKLGFSDNQIANAVKSTELV 154
Cdd:TIGR01369  428 DRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPELLRRAKKLGFSDAQIARLIGVTEAE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  155 VRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNAITSDIDFPGGFTIVV-GSGVYRIGSSVEFDWCAVGCLRELRKL 233
Cdd:TIGR01369  508 VRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPNRIGQGVEFDYCCVHAVLALREL 587

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1510266648  234 GRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:TIGR01369  588 GYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNI 624
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-270 6.22e-127

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 385.60  E-value: 6.22e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFDPY-VKDVNEEELIQ----AT 75
Cdd:PRK05294   350 SLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDlFEEESLEELREelkePT 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   76 DKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIKLNRDTLLKAKKLGFSDNQIANAVKSTELVV 155
Cdd:PRK05294   430 PERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLREAKRLGFSDARIAKLLGVTEDEV 509

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  156 RKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYN----AITSDIDfpggFTIVVGSGVYRIGSSVEFDWCAVGCLRELR 231
Cdd:PRK05294   510 RKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEeeceSNPSDRK----KVLVLGSGPNRIGQGIEFDYCCVHAVLALR 585

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1510266648  232 KLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PRK05294   586 EAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEI 624
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 68-189 4.83e-58

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: 181.11  E-value: 4.83e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   68 EEELIQATDKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGI-KLNRDTLLKAKKLGFSDNQIAN 146
Cdd:smart01096   2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLdELDADLLRKAKRLGFSDRQIAK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1510266648  147 AVKSTELVVRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTY 189
Cdd:smart01096  82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-208 1.67e-41

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: 149.26  E-value: 1.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDG--FDPYVKDVNEEE--LIQATD 76
Cdd:COG0458   327 TLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSLVADDDKEEalLLARRL 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  77 KRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDhfNTLESQGIKLNRDTLLKAKKLGFSDNQIANAVKSTELVVR 156
Cdd:COG0458   407 ARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIV--DEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVT 484

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1510266648 157 KEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNAITSDIDFPGGFTIVVGS 208
Cdd:COG0458   485 TLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 69-145 4.90e-36

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: 123.26  E-value: 4.90e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1510266648  69 EELIQATDKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIKLNRDTLLKAKKLGFSDNQIA 145
Cdd:pfam02787   1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIA 77
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-270 7.44e-140

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: 419.02  E-value: 7.44e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFD---PYVKDVNE--EELIQAT 75
Cdd:TIGR01369  348 SLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDlpdREVEPDEDlwRALKKPT 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   76 DKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIK-LNRDTLLKAKKLGFSDNQIANAVKSTELV 154
Cdd:TIGR01369  428 DRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPELLRRAKKLGFSDAQIARLIGVTEAE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  155 VRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNAITSDIDFPGGFTIVV-GSGVYRIGSSVEFDWCAVGCLRELRKL 233
Cdd:TIGR01369  508 VRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPNRIGQGVEFDYCCVHAVLALREL 587

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1510266648  234 GRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:TIGR01369  588 GYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNI 624
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-270 6.22e-127

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 385.60  E-value: 6.22e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFDPY-VKDVNEEELIQ----AT 75
Cdd:PRK05294   350 SLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDlFEEESLEELREelkePT 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   76 DKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIKLNRDTLLKAKKLGFSDNQIANAVKSTELVV 155
Cdd:PRK05294   430 PERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLREAKRLGFSDARIAKLLGVTEDEV 509

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  156 RKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYN----AITSDIDfpggFTIVVGSGVYRIGSSVEFDWCAVGCLRELR 231
Cdd:PRK05294   510 RKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEeeceSNPSDRK----KVLVLGSGPNRIGQGIEFDYCCVHAVLALR 585

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1510266648  232 KLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PRK05294   586 EAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEI 624
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 1-270 6.83e-91

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 290.33  E-value: 6.83e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFDPYVK--DVNEEELIQ----A 74
Cdd:PRK12815   349 ALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGLSLPIElsGKSDEELLQdlrhP 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   75 TDKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIKLNRDTLLKAKKLGFSDNQIANAVKSTELV 154
Cdd:PRK12815   429 DDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRKVKEKGFSDALLAELTGVTEEE 508

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  155 VRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNaITSDIDFPGG--FTIVVGSGVYRIGSSVEFDWCAVGCLRELRK 232
Cdd:PRK12815   509 VRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYF-GESEAEPSSEkkKVLILGSGPIRIGQGIEFDYSSVHAAFALKK 587

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1510266648  233 LGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PRK12815   588 EGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNV 625
PLN02735 PLN02735
carbamoyl-phosphate synthase
 1-270 5.68e-74

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 244.30  E-value: 5.68e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDGFDPyvKDVNE---------EEL 71
Cdd:PLN02735   367 SIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETGFSGWGC--AKVKEldwdweqlkYKL 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   72 IQATDKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGI-KLNRDTLLKAKKLGFSDNQIANAVKS 150
Cdd:PLN02735   445 RVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLsELSKDDFYEVKRRGFSDKQIAFATKS 524

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  151 TELVVRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNAITSDIDFPGGFTIVVGSGVYRIGSSVEFDWCAVGCLREL 230
Cdd:PLN02735   525 TEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFAL 604

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1510266648  231 RKLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PLN02735   605 QDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNV 644
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 68-189 4.83e-58

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: 181.11  E-value: 4.83e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   68 EEELIQATDKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGI-KLNRDTLLKAKKLGFSDNQIAN 146
Cdd:smart01096   2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLdELDADLLRKAKRLGFSDRQIAK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1510266648  147 AVKSTELVVRKEREELGVLPFVKQIDTVAGEWPASTNYLYLTY 189
Cdd:smart01096  82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-208 1.67e-41

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: 149.26  E-value: 1.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648   1 SLDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVDG--FDPYVKDVNEEE--LIQATD 76
Cdd:COG0458   327 TLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSLVADDDKEEalLLARRL 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648  77 KRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDhfNTLESQGIKLNRDTLLKAKKLGFSDNQIANAVKSTELVVR 156
Cdd:COG0458   407 ARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIV--DEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVT 484

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1510266648 157 KEREELGVLPFVKQIDTVAGEWPASTNYLYLTYNAITSDIDFPGGFTIVVGS 208
Cdd:COG0458   485 TLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 69-145 4.90e-36

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: 123.26  E-value: 4.90e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1510266648  69 EELIQATDKRIFVLAAAIKANYSVKRLHELTKIDPWFLNKMKNIIDHFNTLESQGIKLNRDTLLKAKKLGFSDNQIA 145
Cdd:pfam02787   1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIA 77
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 206-270 5.00e-30

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: 117.67  E-value: 5.00e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1510266648 206 VGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDI 65
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 205-270 8.69e-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: 65.02  E-value: 8.69e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510266648  205 VVGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:TIGR01369   11 VIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKI 76
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 205-270 4.86e-09

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 56.90  E-value: 4.86e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510266648  205 VVGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PRK12815    12 VIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRI 77
carB PRK05294
carbamoyl-phosphate synthase large subunit;
205-270 1.01e-08

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 55.87  E-value: 1.01e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510266648  205 VVGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PRK05294    12 IIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKI 77
PLN02735 PLN02735
carbamoyl-phosphate synthase
 204-270 3.54e-07

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 50.93  E-value: 3.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1510266648  204 IVVGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISFEVVMNI 270
Cdd:PLN02735    27 MILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQV 93
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 2-77 2.50e-06

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: 48.46  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510266648    2 LDYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKALRMVDETVdgfdPY-------VKDVNEEELIQA 74
Cdd:TIGR01369  880 PKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRI----PKkgsvllsVRDKDKEELLDL 955


                   ...
gi 1510266648   75 TDK 77
Cdd:TIGR01369  956 ARK 958
carB PRK05294
carbamoyl-phosphate synthase large subunit;
7-48 3.53e-06

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 48.17  E-value: 3.53e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1510266648    7 VKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKA 48
Cdd:PRK05294   885 VKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 3-48 1.31e-05

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 46.12  E-value: 1.31e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1510266648    3 DYCVVKIPRWDLAKFTRVSKTIGSSMKSVGEAMSIGRNFEEAFQKA 48
Cdd:PRK12815   881 PFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKG 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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