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Conserved domains on  [gi|1193860936|gb|OTW65134|]
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acetolactate synthase isozyme 1 small subunit [Bacillus thuringiensis serovar coreanensis]

Protein Classification

acetolactate synthase 1 small subunit( domain architecture ID 10012801)

acetolactate synthase 1 acts as a thiamin diphosphate (ThDP)-dependent enzyme that catalyzes the first common step in the biosynthesis of the branched-chain amino acids valine, leucine and isoleucine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06737 PRK06737
ACT domain-containing protein;
4-79 2.84e-39

ACT domain-containing protein;


:

Pssm-ID: 180675  Cd Length: 76  Bit Score: 124.42  E-value: 2.84e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1193860936  4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVNKL 79
Cdd:PRK06737   1 MSHTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINVLQVNKL 76
 
Name Accession Description Interval E-value
PRK06737 PRK06737
ACT domain-containing protein;
4-79 2.84e-39

ACT domain-containing protein;


Pssm-ID: 180675  Cd Length: 76  Bit Score: 124.42  E-value: 2.84e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1193860936  4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVNKL 79
Cdd:PRK06737   1 MSHTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINVLQVNKL 76
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 6-77 4.90e-22

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: 80.63  E-value: 4.90e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1193860936  6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVN 77
Cdd:cd04878    1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKVS 72
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 6-76 3.08e-16

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: 68.13  E-value: 3.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1193860936   6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMklTAVCTENEATL--LVGQLKKLIDVLQV 76
Cdd:COG0440     2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRM--TIVVEGDERVIeqITKQLNKLIDVIKV 72
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 6-79 3.92e-15

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: 65.46  E-value: 3.92e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1193860936   6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVNKL 79
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDL 75
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 14-76 1.52e-09

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: 48.74  E-value: 1.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1193860936 14 NEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCtENEATLLVGQLKKLIDVLQV 76
Cdd:pfam13710  1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQLTVES-DRSVELLLNQLEKLYDVVKV 62
 
Name Accession Description Interval E-value
PRK06737 PRK06737
ACT domain-containing protein;
4-79 2.84e-39

ACT domain-containing protein;


Pssm-ID: 180675  Cd Length: 76  Bit Score: 124.42  E-value: 2.84e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1193860936  4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVNKL 79
Cdd:PRK06737   1 MSHTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINVLQVNKL 76
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 6-77 4.90e-22

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: 80.63  E-value: 4.90e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1193860936  6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVN 77
Cdd:cd04878    1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKVS 72
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 6-76 3.08e-16

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: 68.13  E-value: 3.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1193860936   6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMklTAVCTENEATL--LVGQLKKLIDVLQV 76
Cdd:COG0440     2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRM--TIVVEGDERVIeqITKQLNKLIDVIKV 72
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 4-79 4.28e-16

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 67.79  E-value: 4.28e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1193860936   4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVNKL 79
Cdd:PRK11895    1 MRHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDL 76
ilvH CHL00100
acetohydroxyacid synthase small subunit
 4-76 3.48e-15

acetohydroxyacid synthase small subunit


Pssm-ID: 214364 [Multi-domain]  Cd Length: 174  Bit Score: 65.89  E-value: 3.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1193860936   4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQV 76
Cdd:CHL00100    1 MKHTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNILKV 73
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 6-79 3.92e-15

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: 65.46  E-value: 3.92e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1193860936   6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCTENEATLLVGQLKKLIDVLQVNKL 79
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDL 75
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 14-76 1.52e-09

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: 48.74  E-value: 1.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1193860936 14 NEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVCtENEATLLVGQLKKLIDVLQV 76
Cdd:pfam13710  1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQLTVES-DRSVELLLNQLEKLYDVVKV 62
IlvM COG3978
Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]; ...
 4-77 8.29e-09

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


Pssm-ID: 443177  Cd Length: 75  Bit Score: 47.14  E-value: 8.29e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1193860936  4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDtSGVSEMKLTaVCTENEATLLVGQLKKLIDVLQVN 77
Cdd:COG3978    2 MQYQLTIEARRRPGALERVLRVVRHRGFEVRSMNMEAND-GDGLNIELT-VSSDRPIELLTRQLEKLYDVESVE 73
PRK13562 PRK13562
ACT domain-containing protein;
4-79 2.50e-08

ACT domain-containing protein;


Pssm-ID: 184144  Cd Length: 84  Bit Score: 46.10  E-value: 2.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1193860936  4 MSHTFSLVIHNEPSVLLRISGIFARRGYYISSLHLNERDTSGVSEMKLTAVcTENEAT--LLVGQLKKLIDVLQVNKL 79
Cdd:PRK13562   1 MTRILKLQVADQVSTLNRITSAFVRLQYNIDTLHVTHSEQPGISNMEIQVD-IQDDTSlhILIKKLKQQINVLTVECY 77
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 6-72 3.28e-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: 32.66  E-value: 3.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1193860936  6 HTFSLVIHNEPSVLLRISGIFARRGYYISSLHLnERDTSGVSEMKLTAVCTENEATLLVGQLKKLID 72
Cdd:pfam01842  1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQ-GTSEDKGGIVFVVIVVDEEDLEEVLEALKKLEG 66
 
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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