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Conserved domains on  [gi|2649334648|ref|WP_325052547|]
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ACT domain-containing protein, partial [Sinorhizobium meliloti]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13011 super family cl28993
formyltetrahydrofolate deformylase; Reviewed
 1-143 7.74e-88

formyltetrahydrofolate deformylase; Reviewed


The actual alignment was detected with superfamily member PRK13011:

Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 257.22  E-value: 7.74e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEERVGLAALEEGLKPIASKFEMETALH 80
Cdd:PRK13011    5 PDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGFAPIAARFGMQWELH 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2649334648  81 EQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:PRK13011   85 DPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITP 147
 
Name Accession Description Interval E-value
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 1-143 7.74e-88

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 257.22  E-value: 7.74e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEERVGLAALEEGLKPIASKFEMETALH 80
Cdd:PRK13011    5 PDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGFAPIAARFGMQWELH 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2649334648  81 EQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:PRK13011   85 DPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITP 147
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 1-143 1.84e-74

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 223.00  E-value: 1.84e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSF-ISEERVGLAALEEGLKPIASKFEMETAL 79
Cdd:COG0788     1 MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFeAPGLDFDLEALRAAFAPLAERFGMDWRL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2649334648  80 HEQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:COG0788    81 HDSDRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTK 144
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 4-143 1.65e-32

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 115.99  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   4 FVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFiseERVGLAALEEGL-----KPIASKFEMETA 78
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEF---QLEGFRLEESSLlaafkSALAEKFEMTWE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2649334648  79 LHEQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:TIGR00655  78 LILADKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATK 142
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
 5-76 4.49e-27

N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase); This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153147 [Multi-domain]  Cd Length: 74  Bit Score: 96.09  E-value: 4.49e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2649334648   5 VLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEER-VGLAALEEGLKPIASKFEME 76
Cdd:cd04875     1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGFdLSREALEAAFAPVAAEFDMD 73
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 5-64 4.45e-05

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.21  E-value: 4.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   5 VLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEERVGlAALEE 64
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE-EVLEA 60
 
Name Accession Description Interval E-value
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 1-143 7.74e-88

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 257.22  E-value: 7.74e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEERVGLAALEEGLKPIASKFEMETALH 80
Cdd:PRK13011    5 PDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGFAPIAARFGMQWELH 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2649334648  81 EQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:PRK13011   85 DPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITP 147
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-143 8.18e-77

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 229.22  E-value: 8.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEE-RVGLAALEEGLKPIASKFEMETAL 79
Cdd:PRK06027    4 MQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGDGlIFNLETLRADFAALAEEFEMDWRL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2649334648  80 HEQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:PRK06027   84 LDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTK 147
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 1-143 1.84e-74

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 223.00  E-value: 1.84e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSF-ISEERVGLAALEEGLKPIASKFEMETAL 79
Cdd:COG0788     1 MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFeAPGLDFDLEALRAAFAPLAERFGMDWRL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2649334648  80 HEQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:COG0788    81 HDSDRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTK 144
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 1-143 2.59e-72

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 218.13  E-value: 2.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFI--SEERVGLAALEEGLKPIASKFEMETA 78
Cdd:PRK13010    7 SPSYVLTLACPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHaqSAEAASVDTFRQEFQPVAEKFDMQWA 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2649334648  79 LHEQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:PRK13010   87 IHPDGQRPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAVQHDIPFHHLPVTP 151
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 4-143 1.65e-32

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 115.99  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   4 FVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFiseERVGLAALEEGL-----KPIASKFEMETA 78
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEF---QLEGFRLEESSLlaafkSALAEKFEMTWE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2649334648  79 LHEQSERMKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:TIGR00655  78 LILADKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATK 142
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
 5-76 4.49e-27

N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase); This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153147 [Multi-domain]  Cd Length: 74  Bit Score: 96.09  E-value: 4.49e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2649334648   5 VLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEER-VGLAALEEGLKPIASKFEME 76
Cdd:cd04875     1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGFdLSREALEAAFAPVAAEFDMD 73
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 86-143 5.31e-24

Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine.


Pssm-ID: 187717 [Multi-domain]  Cd Length: 196  Bit Score: 91.85  E-value: 5.31e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2649334648  86 MKVLLMVSRFGHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVVNHDIPFHHIKVTK 143
Cdd:cd08648     1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTK 58
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 20-143 2.08e-12

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 62.46  E-value: 2.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648  20 LSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEERV-GLAALEEGLKPIASKFEMETA---LHEQSERMKVLLMVSRF 95
Cdd:PLN02828    1 LSDCIASRGGNILGVDVFVPENKNVFYSRSEFIFDPVKwPRAQMDEDFQEISKHFKALKSvvrVPGLDPKYKIAVLASKQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2649334648  96 GHCLNDLLYRWKIGALPIDIVGVVSNHFDYQKVVV-----NHDIPFHHIKVTK 143
Cdd:PLN02828   81 DHCLIDLLHRWQDGRLPVDITCVISNHERGPNTHVmrfleRHGIPYHYLPTTK 133
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
1-85 1.05e-08

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 50.99  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSS------QFDdldtgkFFMRTSfISEERVglAALEEGLKPIASKFE 74
Cdd:COG2716     1 MQHLVITAIGPDRPGIVAALARAVSEHGCNILDSRmarlggEFA------GILLVS-GPWDAI--AKLEAALPALAAELG 71

                          90
                  ....*....|.
gi 2649334648  75 METALHEQSER 85
Cdd:COG2716    72 LLVTVKRTEPH 82
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 5-64 4.45e-05

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.21  E-value: 4.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   5 VLTVSCKSTRGVVAALSGYLAEQGCNIADSSQFDDLDTGKFFMRTSFISEERVGlAALEE 64
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE-EVLEA 60
PRK00194 PRK00194
ACT domain-containing protein;
1-67 8.35e-05

ACT domain-containing protein;


Pssm-ID: 178923 [Multi-domain]  Cd Length: 90  Bit Score: 39.02  E-value: 8.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQ--FDDLDTgkFFMRTSfISEERVGLAALEEGLK 67
Cdd:PRK00194    1 MMKAIITVIGKDKVGIIAGVSTVLAELNVNILDISQtiMDGYFT--MIMLVD-ISESKKDFAELKEELE 66
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 6-63 1.60e-04

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 37.66  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2649334648   6 LTVSCKSTRGVVAALSGYLAEQGCNIADSSQF--DDLDTGKFFMRTSFISEERVGLAALE 63
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRtsGDGGEADIFIVVDGDGDLEKLLEALE 60
ACT COG3830
ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];
1-36 1.35e-03

ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];


Pssm-ID: 443042 [Multi-domain]  Cd Length: 212  Bit Score: 37.37  E-value: 1.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2649334648   1 MQNFVLTVSCKSTRGVVAALSGYLAEQGCNIADSSQ 36
Cdd:COG3830     2 SMKALITVTGKDRPGITAAVSGVLAEHGVNILDISQ 37
 
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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