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Conserved domains on  [gi|15822562|gb|AAK13023|]
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CTP synthase, partial [Fibrobacter succinogenes subsp. succinogenes S85]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrG super family cl33917
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-133 4.15e-84

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


The actual alignment was detected with superfamily member COG0504:

Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 255.32  E-value: 4.15e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562   1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:COG0504 378 GICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISER 457

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15822562  81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:COG0504 458 HRHRYEF--NNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPE 508
 
Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-133 4.15e-84

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: 255.32  E-value: 4.15e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562   1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:COG0504 378 GICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISER 457

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15822562  81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:COG0504 458 HRHRYEF--NNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPE 508
pyrG PRK05380
CTP synthetase; Validated
 1-133 1.31e-83

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 253.79  E-value: 1.31e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562    1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:PRK05380 377 GICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYER 456

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15822562   81 HRHRYEFNYnsEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:PRK05380 457 HRHRYEVNN--KYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPE 507
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 1-133 2.34e-72

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: 215.88  E-value: 2.34e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562   1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:cd01746  89 GICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKGVKDLGGTMRLGAYPVILKPGTLAHKYYGKDEVEER 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15822562  81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:cd01746 169 HRHRYEV--NPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPE 219
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-133 5.19e-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: 218.74  E-value: 5.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562     1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:TIGR00337 377 GICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYER 456

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15822562    81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:TIGR00337 457 HRHRYEV--NNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPE 507
GATase pfam00117
Glutamine amidotransferase class-I;
1-133 1.11e-23

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 90.37  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562     1 GICLGMQMLAIEFARNVlglkvanstefdenttprfirdlEEQKDGHDKGGTMRLGLYPCKLAKDSNaanvykrEKITER 80
Cdd:pfam00117  75 GICLGHQLLALAFGGKV-----------------------VKAKKFGHHGKNSPVGDDGCGLFYGLP-------NVFIVR 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15822562    81 HRHRYEFNynsefrKELEKAGLKIAGTSPDGKLVEMVELKNHPYFeACQFHPE 133
Cdd:pfam00117 125 RYHSYAVD------PDTLPDGLEVTATSENDGTIMGIRHKKLPIF-GVQFHPE 170
 
Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-133 4.15e-84

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: 255.32  E-value: 4.15e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562   1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:COG0504 378 GICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISER 457

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15822562  81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:COG0504 458 HRHRYEF--NNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPE 508
pyrG PRK05380
CTP synthetase; Validated
 1-133 1.31e-83

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 253.79  E-value: 1.31e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562    1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:PRK05380 377 GICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYER 456

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15822562   81 HRHRYEFNYnsEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:PRK05380 457 HRHRYEVNN--KYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPE 507
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 1-133 2.34e-72

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: 215.88  E-value: 2.34e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562   1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:cd01746  89 GICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKGVKDLGGTMRLGAYPVILKPGTLAHKYYGKDEVEER 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15822562  81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:cd01746 169 HRHRYEV--NPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPE 219
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-133 5.19e-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: 218.74  E-value: 5.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562     1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHDKGGTMRLGLYPCKLAKDSNAANVYKREKITER 80
Cdd:TIGR00337 377 GICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYER 456

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15822562    81 HRHRYEFnyNSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:TIGR00337 457 HRHRYEV--NNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPE 507
PLN02327 PLN02327
CTP synthase
 1-133 5.50e-46

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 156.34  E-value: 5.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562    1 GICLGMQMLAIEFARNVLGLKVANSTEFDENTTPRFIRDLEEQKDGHdKGGTMRLGLYPCKL-AKDSNAANVY-KREKIT 78
Cdd:PLN02327 396 GICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTH-MGGTMRLGSRRTYFqTPDCKSAKLYgNVSFVD 474

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15822562   79 ERHRHRYEFNynSEFRKELEKAGLKIAGTSPDGKLVEMVELKNHPYFEACQFHPE 133
Cdd:PLN02327 475 ERHRHRYEVN--PEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPE 527
GATase pfam00117
Glutamine amidotransferase class-I;
1-133 1.11e-23

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 90.37  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562     1 GICLGMQMLAIEFARNVlglkvanstefdenttprfirdlEEQKDGHDKGGTMRLGLYPCKLAKDSNaanvykrEKITER 80
Cdd:pfam00117  75 GICLGHQLLALAFGGKV-----------------------VKAKKFGHHGKNSPVGDDGCGLFYGLP-------NVFIVR 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15822562    81 HRHRYEFNynsefrKELEKAGLKIAGTSPDGKLVEMVELKNHPYFeACQFHPE 133
Cdd:pfam00117 125 RYHSYAVD------PDTLPDGLEVTATSENDGTIMGIRHKKLPIF-GVQFHPE 170
PRK06186 PRK06186
hypothetical protein; Validated
 1-133 1.39e-19

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 80.78  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822562    1 GICLGMQMLAIEFARNVLGLKVANSTEfdenTTPRFIR--------DLEEQKDghdkggtmrlglyPCKLAKDSNAANVY 72
Cdd:PRK06186  87 GTCGGFQHALLEYARNVLGWADAAHAE----TDPEGDRpviaplscSLVEKTG-------------DIRLRPGSLIARAY 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15822562   73 KREKITERHRHRYefNYNSEFRKELEKAGLKIAGTSPDGKlVEMVELKNHPYFEACQFHPE 133
Cdd:PRK06186 150 GTLEIEEGYHCRY--GVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPE 207
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 101-133 9.83e-06

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 42.95  E-value: 9.83e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 15822562 101 GLKIAGTSPDGkLVEMVELKNHPYFEACQFHPE 133
Cdd:cd01745 141 GLRVEARAPDG-VIEAIESPDRPFVLGVQWHPE 172
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 100-133 1.25e-03

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 37.19  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15822562  100 AGLKIAGTSPDGkLVEMVELKNHPYFEACQFHPE 133
Cdd:PRK11366 192 PRLRVEARSPDG-LVEAVSVINHPFALGVQWHPE 224
 
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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