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Conserved domains on  [gi|504779187|ref|WP_014966289|]
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ACT domain-containing protein [Gottschalkia acidurici]

Protein Classification

PheB family protein( domain architecture ID 11468247)

PheB family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PheB COG4492
ACT domain-containing protein, UPF0735 family [General function prediction only];
5-148 1.25e-72

ACT domain-containing protein, UPF0735 family [General function prediction only];


:

Pssm-ID: 443581 [Multi-domain]  Cd Length: 147  Bit Score: 213.85  E-value: 1.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504779187   5 ESKYLVIDKDILPDVFEKVLLAKELLRTGEVKEITEAVKKVGISRSTFYKYKDSVFTLDERSMGKKVTLSFLLSHMQGVL 84
Cdd:COG4492    4 EKKFYLVREDILPEAILKVVEAKELLESGEVKTVNEAVKKVGISRSAFYKYKDYVFPFYEMSKGKIITLSLLLEDEPGVL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504779187  85 SNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVVTME 148
Cdd:COG4492   84 SSVLNIIAEAGGNILTINQSIPIQGIANVTISIETSDMTIDIEELLEELRELEGVRKVEILGRE 147
 
Name Accession Description Interval E-value
PheB COG4492
ACT domain-containing protein, UPF0735 family [General function prediction only];
5-148 1.25e-72

ACT domain-containing protein, UPF0735 family [General function prediction only];


Pssm-ID: 443581 [Multi-domain]  Cd Length: 147  Bit Score: 213.85  E-value: 1.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504779187   5 ESKYLVIDKDILPDVFEKVLLAKELLRTGEVKEITEAVKKVGISRSTFYKYKDSVFTLDERSMGKKVTLSFLLSHMQGVL 84
Cdd:COG4492    4 EKKFYLVREDILPEAILKVVEAKELLESGEVKTVNEAVKKVGISRSAFYKYKDYVFPFYEMSKGKIITLSLLLEDEPGVL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504779187  85 SNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVVTME 148
Cdd:COG4492   84 SSVLNIIAEAGGNILTINQSIPIQGIANVTISIETSDMTIDIEELLEELRELEGVRKVEILGRE 147
PRK04435 PRK04435
ACT domain-containing protein;
5-148 1.64e-68

ACT domain-containing protein;


Pssm-ID: 179848 [Multi-domain]  Cd Length: 147  Bit Score: 203.50  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504779187   5 ESKYLVIDKDILPDVFEKVLLAKELLRTGEVKEITEAVKKVGISRSTFYKYKDSVFTLDERSMGKKVTLSFLLSHMQGVL 84
Cdd:PRK04435   4 KKKFYLVREDVLPEAVEKTLKAKELLKSGKVKSINEAVKQVGISRSAFYKYKDYVFPFDEMVKGKIITLSLLLEDRSGTL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504779187  85 SNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVVTME 148
Cdd:PRK04435  84 SKVLNVIAEAGGNILTINQSIPLQGRANVTISIDTSSMEGDIDELLEKLRNLDGVEKVELIGME 147
ACT_PheB-BS cd04888
C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway ...
 71-145 8.16e-30

C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and related domains; This CD includes the C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and other related ACT domains. In B. subtilis, the upstream gene of pheB, pheA encodes prephenate dehydratase (PDT). The presumed product of the pheB gene is chorismate mutase (CM). The deduced product of the B. subtilis pheB gene, however, has no significant homology to the CM portion of the bifunctional CM-PDT of Escherichia coli. The presence of an ACT domain lends support to the prediction that these proteins function as a phenylalanine-binding regulatory protein. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153160  Cd Length: 76  Bit Score: 103.04  E-value: 8.16e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504779187  71 VTLSFLLSHMQGVLSNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVV 145
Cdd:cd04888    1 VTLSLLLEHRPGVLSKVLNTIAQVRGNVLTINQNIPIHGRANVTISIDTSTMNGDIDELLEELREIDGVEKVELV 75
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 71-138 5.79e-03

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: 33.43  E-value: 5.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504779187   71 VTLSFLLSHMQGVLSNVLQTISANGGNVLTINQdIPIHDVANVSITFDVSHIKiSIEEVIEEVKSIEG 138
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQ-GTSEDKGGIVFVVIVVDEE-DLEEVLEALKKLEG 66
 
Name Accession Description Interval E-value
PheB COG4492
ACT domain-containing protein, UPF0735 family [General function prediction only];
5-148 1.25e-72

ACT domain-containing protein, UPF0735 family [General function prediction only];


Pssm-ID: 443581 [Multi-domain]  Cd Length: 147  Bit Score: 213.85  E-value: 1.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504779187   5 ESKYLVIDKDILPDVFEKVLLAKELLRTGEVKEITEAVKKVGISRSTFYKYKDSVFTLDERSMGKKVTLSFLLSHMQGVL 84
Cdd:COG4492    4 EKKFYLVREDILPEAILKVVEAKELLESGEVKTVNEAVKKVGISRSAFYKYKDYVFPFYEMSKGKIITLSLLLEDEPGVL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504779187  85 SNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVVTME 148
Cdd:COG4492   84 SSVLNIIAEAGGNILTINQSIPIQGIANVTISIETSDMTIDIEELLEELRELEGVRKVEILGRE 147
PRK04435 PRK04435
ACT domain-containing protein;
5-148 1.64e-68

ACT domain-containing protein;


Pssm-ID: 179848 [Multi-domain]  Cd Length: 147  Bit Score: 203.50  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504779187   5 ESKYLVIDKDILPDVFEKVLLAKELLRTGEVKEITEAVKKVGISRSTFYKYKDSVFTLDERSMGKKVTLSFLLSHMQGVL 84
Cdd:PRK04435   4 KKKFYLVREDVLPEAVEKTLKAKELLKSGKVKSINEAVKQVGISRSAFYKYKDYVFPFDEMVKGKIITLSLLLEDRSGTL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504779187  85 SNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVVTME 148
Cdd:PRK04435  84 SKVLNVIAEAGGNILTINQSIPLQGRANVTISIDTSSMEGDIDELLEKLRNLDGVEKVELIGME 147
ACT_PheB-BS cd04888
C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway ...
 71-145 8.16e-30

C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and related domains; This CD includes the C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and other related ACT domains. In B. subtilis, the upstream gene of pheB, pheA encodes prephenate dehydratase (PDT). The presumed product of the pheB gene is chorismate mutase (CM). The deduced product of the B. subtilis pheB gene, however, has no significant homology to the CM portion of the bifunctional CM-PDT of Escherichia coli. The presence of an ACT domain lends support to the prediction that these proteins function as a phenylalanine-binding regulatory protein. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153160  Cd Length: 76  Bit Score: 103.04  E-value: 8.16e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504779187  71 VTLSFLLSHMQGVLSNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKISIEEVIEEVKSIEGVQKLVVV 145
Cdd:cd04888    1 VTLSLLLEHRPGVLSKVLNTIAQVRGNVLTINQNIPIHGRANVTISIDTSTMNGDIDELLEELREIDGVEKVELV 75
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
63-141 3.49e-05

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 42.45  E-value: 3.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504779187  63 DERSMGKKVTLSFLLSHMQGVLSNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKiSIEEVIEEVKSIEGVQK 141
Cdd:COG0317  639 EDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATIRFTVEVRDLD-HLARVLRKLRKVPGVIS 716
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 81-141 2.78e-03

ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153148 [Multi-domain]  Cd Length: 71  Bit Score: 34.35  E-value: 2.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504779187  81 QGVLSNVLQTISANGGNVLTINQDIPIHDVANVSITFDVSHIKiSIEEVIEEVKSIEGVQK 141
Cdd:cd04876    9 PGLLADITTVIAEEKINILSVNTRTDDDGLATIRLTLEVRDLE-HLARIMRKLRQIPGVID 68
HTH_Hin_like cd00569
Helix-turn-helix domain of Hin and related proteins; This domain model summarizes a family of ...
 21-55 4.94e-03

Helix-turn-helix domain of Hin and related proteins; This domain model summarizes a family of DNA-binding domains unique to bacteria and represented by the Hin protein of Salmonella. The basic HTH domain is a simple fold comprised of three core helices that form a right-handed helical bundle. The principal DNA-protein interface is formed by the third helix, the recognition helix, inserting itself into the major groove of the DNA. A diverse array of HTH domains participate in a variety of functions that depend on their DNA-binding properties. HTH_Hin represents one of the simplest versions of the HTH domains; the characterization of homologous relationships between various sequence-diverse HTH domain families remains difficult. The Hin recombinase induces the site-specific inversion of a chromosomal DNA segment containing a promoter, which controls the alternate expression of two genes by reversibly switching orientation. The Hin recombinase consists of a single polypeptide chain containing a C-terminal DNA-binding domain (HTH_Hin) and a catalytic domain.


Pssm-ID: 259851 [Multi-domain]  Cd Length: 42  Bit Score: 33.07  E-value: 4.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 504779187  21 EKVLLAKELLRTGEvkEITEAVKKVGISRSTFYKY 55
Cdd:cd00569    9 EQIAEARRLLAAGE--SVAEIARELGVSRSTLYRY 41
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 71-138 5.79e-03

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: 33.43  E-value: 5.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504779187   71 VTLSFLLSHMQGVLSNVLQTISANGGNVLTINQdIPIHDVANVSITFDVSHIKiSIEEVIEEVKSIEG 138
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQ-GTSEDKGGIVFVVIVVDEE-DLEEVLEALKKLEG 66
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 73-134 7.03e-03

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: 33.03  E-value: 7.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504779187  73 LSFLLSHMQGVLSNVLQTISANGGNVLTINQDiPIHDVANVSITFDVsHIKISIEEVIEEVK 134
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQR-TSGDGGEADIFIVV-DGDGDLEKLLEALE 60
 
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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