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Conserved domains on  [gi|763714127|gb|AJQ31448|]
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CTP synthase, partial [Leuconostoc mesenteroides]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pyrG super family cl35313
CTP synthetase; Validated
 1-162 3.43e-97

CTP synthetase; Validated


The actual alignment was detected with superfamily member PRK05380:

Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 290.00  E-value: 3.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:PRK05380 181 AAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127  81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:PRK05380 261 ERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLEEENVAEL 340


                 ..
gi 763714127 161 LA 162
Cdd:PRK05380 341 LK 342
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-162 3.43e-97

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 290.00  E-value: 3.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:PRK05380 181 AAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127  81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:PRK05380 261 ERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLEEENVAEL 340


                 ..
gi 763714127 161 LA 162
Cdd:PRK05380 341 LK 342
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-162 3.58e-96

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 287.68  E-value: 3.58e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:COG0504  182 AAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIVL 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127  81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:COG0504  262 KKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDSEDLEEENAEEL 341


                 ..
gi 763714127 161 LA 162
Cdd:COG0504  342 LK 343
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-160 8.05e-70

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 219.51  E-value: 8.05e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127    1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:TIGR00337 182 AAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKDVSSIYEVPLLLLKQGLDDYLC 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:TIGR00337 262 RRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLDTKVNIKWIDSEDLEEEGVEFL 341
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-85 7.42e-48

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 155.58  E-value: 7.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127    1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:pfam06418 181 AAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVSSIYEVPLLLEEQGLDDIIL 260


                  ....*
gi 763714127   81 NKLKL 85
Cdd:pfam06418 261 KRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 1-80 1.25e-37

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 129.14  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:cd03113  181 ATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYIL 260
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-162 3.43e-97

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 290.00  E-value: 3.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:PRK05380 181 AAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127  81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:PRK05380 261 ERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLEEENVAEL 340


                 ..
gi 763714127 161 LA 162
Cdd:PRK05380 341 LK 342
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-162 3.58e-96

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 287.68  E-value: 3.58e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:COG0504  182 AAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIVL 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127  81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:COG0504  262 KKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDSEDLEEENAEEL 341


                 ..
gi 763714127 161 LA 162
Cdd:COG0504  342 LK 343
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-160 8.05e-70

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 219.51  E-value: 8.05e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127    1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:TIGR00337 182 AAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKDVSSIYEVPLLLLKQGLDDYLC 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   81 NKLKLDAPKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAEL 160
Cdd:TIGR00337 262 RRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLDTKVNIKWIDSEDLEEEGVEFL 341
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-85 7.42e-48

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 155.58  E-value: 7.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127    1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:pfam06418 181 AAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVSSIYEVPLLLEEQGLDDIIL 260


                  ....*
gi 763714127   81 NKLKL 85
Cdd:pfam06418 261 KRLNL 265
PLN02327 PLN02327
CTP synthase
 3-159 5.35e-43

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 149.41  E-value: 5.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   3 GEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVLNK 82
Cdd:PLN02327 190 GEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAENILNLHDVSNIWHVPLLLRDQKAHEAILKV 269

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763714127  83 LKLD--APKAEMSDWSKMVELIKHPKKTVNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAE 159
Cdd:PLN02327 270 LNLLsvAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKALLHASVACSRKLVIDWVAASDLEDETAKE 348
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 1-80 1.25e-37

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 129.14  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763714127   1 AAGEAKTKPTQHSVAQLRSLGIQPDMIVLRTQRPLEENLKQKISTFTDVNENAVIESRDVETLYEIPLNLQAQGMDDVVL 80
Cdd:cd03113  181 ATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYIL 260
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 109-161 6.23e-18

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 77.21  E-value: 6.23e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 763714127 109 VNVTLVGKYTDLPDAYISVNEALKHAGYAQDADVKINHVKSENVTPENVAELL 161
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAEEAL 53
 
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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