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Conserved domains on  [gi|1972900863|gb|QRF60158|]
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acetolactate synthase small subunit [Variovorax paradoxus]

Protein Classification

acetolactate synthase small subunit( domain architecture ID 11485674)

acetolactate synthase small regulatory subunit activates the large catalytic subunit of multimeric acetolactate synthase, an enzyme that catalyzes the thiamin diphosphate-dependent first common step in the biosynthesis of branched-chain amino acids

EC:  2.2.1.6
Gene Ontology:  GO:0003984|GO:1990610|GO:0009082
PubMed:  22284339|27576495
SCOP:  4000264

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 1-161 4.28e-96

acetolactate synthase 3 regulatory subunit; Reviewed


:

Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 274.65  E-value: 4.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGA 80
Cdd:PRK11895    1 MRHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863  81 YTERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGERI 160
Cdd:PRK11895   81 HVERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKI 160


                  .
gi 1972900863 161 L 161
Cdd:PRK11895  161 L 161
 
Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 1-161 4.28e-96

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 274.65  E-value: 4.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGA 80
Cdd:PRK11895    1 MRHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863  81 YTERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGERI 160
Cdd:PRK11895   81 HVERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKI 160


                  .
gi 1972900863 161 L 161
Cdd:PRK11895  161 L 161
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 2-161 1.05e-86

Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate synthase, small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440209 [Multi-domain]  Cd Length: 160  Bit Score: 250.71  E-value: 1.05e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   2 KHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGAY 81
Cdd:COG0440     1 RHTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863  82 TERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGERIL 161
Cdd:COG0440    81 VERELALIKVKADGETRSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGSKSL 160
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 2-158 4.16e-69

acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine pyrophosphate enzyme with large and small subunits. One of the three isozymes in E. coli K12 contains a frameshift in the large subunit gene and is not expressed. acetohydroxyacid synthase is a synonym. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272916 [Multi-domain]  Cd Length: 157  Bit Score: 206.06  E-value: 4.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   2 KHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGAY 81
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972900863  82 TERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGE 158
Cdd:TIGR00119  81 VERELCLVKVSAPGEGRDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 3-74 1.07e-32

N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS); ACT_AHAS: N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS). AHAS catalyses the first common step in the biosynthesis of the three branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. Bacterial AHASs generally consist of regulatory and catalytic subunits. The effector (valine) binding sites are proposed to be located in two symmetrically related positions in the interface between a pair of N-terminal ACT domains with the C-terminal domain of IlvH contacting the catalytic dimer. Plants Arabidopsis and Oryza have tandem IlvH subunits; both the first and second ACT domain sequences are present in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153150  Cd Length: 72  Bit Score: 111.07  E-value: 1.07e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972900863   3 HIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVV 74
Cdd:cd04878     1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKVS 72
ALS_ss_C pfam10369
Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of ...
 84-156 1.28e-29

Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of proteins which are the small subunits of acetolactate synthase. Acetolactate synthase is a tetrameric enzyme, containing probably two large and two small subunits, which catalyzes the first step in branched-chain amino acid biosynthesis. This reaction is sensitive to certain herbicides.


Pssm-ID: 463060  Cd Length: 73  Bit Score: 103.20  E-value: 1.28e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972900863  84 RELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGR 156
Cdd:pfam10369   1 RELALIKVKADPEDRAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
 
Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 1-161 4.28e-96

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 274.65  E-value: 4.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGA 80
Cdd:PRK11895    1 MRHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863  81 YTERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGERI 160
Cdd:PRK11895   81 HVERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKI 160


                  .
gi 1972900863 161 L 161
Cdd:PRK11895  161 L 161
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 2-161 1.05e-86

Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate synthase, small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440209 [Multi-domain]  Cd Length: 160  Bit Score: 250.71  E-value: 1.05e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   2 KHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGAY 81
Cdd:COG0440     1 RHTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863  82 TERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGERIL 161
Cdd:COG0440    81 VERELALIKVKADGETRSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGSKSL 160
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 2-158 4.16e-69

acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine pyrophosphate enzyme with large and small subunits. One of the three isozymes in E. coli K12 contains a frameshift in the large subunit gene and is not expressed. acetohydroxyacid synthase is a synonym. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272916 [Multi-domain]  Cd Length: 157  Bit Score: 206.06  E-value: 4.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   2 KHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGAY 81
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972900863  82 TERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGE 158
Cdd:TIGR00119  81 VERELCLVKVSAPGEGRDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
ilvH CHL00100
acetohydroxyacid synthase small subunit
 1-160 2.47e-50

acetohydroxyacid synthase small subunit


Pssm-ID: 214364 [Multi-domain]  Cd Length: 174  Bit Score: 159.10  E-value: 2.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDLTEGA 80
Cdd:CHL00100    1 MKHTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNILKVQDITNIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863  81 YTERELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGRGERI 160
Cdd:CHL00100   81 CVERELMLIKINVNSQTRPEILEIAQIFRAKVVDLSEESLILEVTGDPGKIVAIEQLLEKFGIIEIARTGKIALIRESKV 160
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 3-74 1.07e-32

N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS); ACT_AHAS: N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS). AHAS catalyses the first common step in the biosynthesis of the three branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. Bacterial AHASs generally consist of regulatory and catalytic subunits. The effector (valine) binding sites are proposed to be located in two symmetrically related positions in the interface between a pair of N-terminal ACT domains with the C-terminal domain of IlvH contacting the catalytic dimer. Plants Arabidopsis and Oryza have tandem IlvH subunits; both the first and second ACT domain sequences are present in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153150  Cd Length: 72  Bit Score: 111.07  E-value: 1.07e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972900863   3 HIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVV 74
Cdd:cd04878     1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKVS 72
ALS_ss_C pfam10369
Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of ...
 84-156 1.28e-29

Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of proteins which are the small subunits of acetolactate synthase. Acetolactate synthase is a tetrameric enzyme, containing probably two large and two small subunits, which catalyzes the first step in branched-chain amino acid biosynthesis. This reaction is sensitive to certain herbicides.


Pssm-ID: 463060  Cd Length: 73  Bit Score: 103.20  E-value: 1.28e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972900863  84 RELMMVKVRAVGKEREEMMRMAEIFRGRIIDVTDKSYTIELTGDHGKNDAFLEAIDRSAILETVRTGASGIGR 156
Cdd:pfam10369   1 RELALIKVKADPEDRAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 11-73 4.84e-12

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.


Pssm-ID: 463962  Cd Length: 62  Bit Score: 57.59  E-value: 4.84e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972900863  11 NEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTiVTAGSDDVIEQITKHLNRLIEVVKV 73
Cdd:pfam13710   1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQ-LTVESDRSVELLLNQLEKLYDVVKV 62
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 3-69 2.41e-09

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: 50.77  E-value: 2.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972900863   3 HIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDaSLSRMTIVTAGSDDVIEQITKHLNRLIE 69
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSED-KGGIVFVVIVVDEEDLEEVLEALKKLEG 66
PRK08178 PRK08178
acetolactate synthase 1 small subunit;
7-74 2.83e-07

acetolactate synthase 1 small subunit;


Pssm-ID: 236174  Cd Length: 96  Bit Score: 46.23  E-value: 2.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972900863   7 VLLE----NEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAgSDDVIEQITKHLNRLIEVVKVV 74
Cdd:PRK08178    9 VILEltvrNHPGVMSHVCGLFARRAFNVEGILCLPIQDGDKSRIWLLVN-DDQRLEQMISQIEKLEDVLKVR 79
PRK06737 PRK06737
ACT domain-containing protein;
1-76 9.72e-07

ACT domain-containing protein;


Pssm-ID: 180675  Cd Length: 76  Bit Score: 44.30  E-value: 9.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKHLNRLIEVVKVVDL 76
Cdd:PRK06737    1 MSHTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINVLQVNKL 76
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 5-64 3.59e-06

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: 42.28  E-value: 3.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   5 IAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDvIEQITKHL 64
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGD-LEKLLEAL 59
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
5-50 2.62e-05

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


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 41.66  E-value: 2.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1972900863   5 IAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMtIVT 50
Cdd:COG4747     3 ISVFLENKPGRLAEVTRLLGDAGINIRALSIADTSDFGILRL-IVD 47
IlvM COG3978
Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]; ...
 1-73 2.13e-04

Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism];


Pssm-ID: 443177  Cd Length: 75  Bit Score: 37.90  E-value: 2.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLS-RMTIVtagSDDVIEQITKHLNRLIEVVKV 73
Cdd:COG3978     2 MQYQLTIEARRRPGALERVLRVVRHRGFEVRSMNMEANDGDGLNiELTVS---SDRPIELLTRQLEKLYDVESV 72
PRK13562 PRK13562
ACT domain-containing protein;
1-76 2.59e-04

ACT domain-containing protein;


Pssm-ID: 184144  Cd Length: 84  Bit Score: 38.01  E-value: 2.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972900863   1 MKHIIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQIT-KHLNRLIEVVKVVDL 76
Cdd:PRK13562    1 MTRILKLQVADQVSTLNRITSAFVRLQYNIDTLHVTHSEQPGISNMEIQVDIQDDTSLHILiKKLKQQINVLTVECY 77
ACT_CM-PDT cd04905
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ...
 2-32 4.69e-04

C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153177 [Multi-domain]  Cd Length: 80  Bit Score: 37.09  E-value: 4.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1972900863   2 KHIIAVLLENEPGALSRVVGLFSARGYN---IES 32
Cdd:cd04905     1 KTSIVFTLPNKPGALYDVLGVFAERGINltkIES 34
ACT_Bt0572_1 cd04908
N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; ...
 5-46 4.83e-04

N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; Included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. These tandem ACT domain proteins belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153180  Cd Length: 66  Bit Score: 36.79  E-value: 4.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972900863   5 IAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRM 46
Cdd:cd04908     4 LSVFLENKPGRLAAVTEILSEAGINIRALSIADTSEFGILRL 45
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 5-42 1.72e-03

C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD includes the C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB. AcuB is putatively involved in the anaerobic catabolism of acetoin, and related proteins. Studies report the induction of AcuB by nitrate respiration and also by fermentation. Since acetoin can be secreted and later serve as a source of carbon, it has been proposed that, during anaerobic growth when other carbon sources are exhausted, the induction of the AcuB protein results in acetoin catabolism. AcuB-like proteins have two N-terminal tandem CBS domains and a single C-terminal ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153155  Cd Length: 72  Bit Score: 35.31  E-value: 1.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1972900863   5 IAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDAS 42
Cdd:cd04883     4 IEVRVPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEED 41
ACT_AAAH-PDT-like cd04880
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
 5-32 5.86e-03

ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes appear to be regulated, in part, by the phosphorylation of serine residues N-terminal of the ACT domain. Also included in this CD are the C-terminal ACT domains of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme found in plants, fungi, bacteria, and archaea. The P-protein of Escherichia coli (CM-PDT) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153152 [Multi-domain]  Cd Length: 75  Bit Score: 34.01  E-value: 5.86e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1972900863   5 IAVLLENEPGALSRVVGLFSARGYN---IES 32
Cdd:cd04880     2 LVFSLKNKPGALAKALKVFAERGINltkIES 32
ACT_Bt0572_2 cd04882
C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD ...
 4-63 6.07e-03

C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD is the C-terminal ACT domain of a novel protein composed of just two ACT domains, as seen in the yet uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related proteins. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153154  Cd Length: 65  Bit Score: 33.73  E-value: 6.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972900863   4 IIAVLLENEPGALSRVVGLFSARGYNIESLTVAPTEDASLSRMTIVTAGSDDVIEQITKH 63
Cdd:cd04882     1 VLAVEVPDKPGGLHEILQILSEEGINIEYMYAFVEKKGGKALLIFRTEDIEKAIEVLQER 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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