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Conserved domains on  [gi|881014629|ref|WP_048735338|]
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MULTISPECIES: acetolactate synthase small subunit [Corynebacterium]

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
 5-163 1.85e-77

acetolactate synthase 3 regulatory subunit; Reviewed


:

Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 227.65  E-value: 1.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:PRK11895   3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881014629  85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGPKPM 163
Cdd:PRK11895  83 ERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKIL 161
 
Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 5-163 1.85e-77

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 227.65  E-value: 1.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:PRK11895   3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881014629  85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGPKPM 163
Cdd:PRK11895  83 ERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKIL 161
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 5-163 2.20e-74

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: 219.90  E-value: 2.20e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:COG0440    2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEESV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881014629  85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGPKPM 163
Cdd:COG0440   82 ERELALIKVKADGETRSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGSKSL 160
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 5-160 9.36e-55

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: 169.85  E-value: 9.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629    5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAIV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881014629   85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGP 160
Cdd:TIGR00119  82 ERELCLVKVSAPGEGRDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
ALS_ss_C pfam10369
Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of ...
 86-158 2.04e-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: 102.81  E-value: 2.04e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881014629   86 RGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMAR 158
Cdd:pfam10369   1 RELALIKVKADPEDRAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 5-76 6.47e-29

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: 101.44  E-value: 6.47e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVV 76
Cdd:cd04878    1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKVS 72
 
Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 5-163 1.85e-77

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 227.65  E-value: 1.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:PRK11895   3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881014629  85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGPKPM 163
Cdd:PRK11895  83 ERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKIL 161
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 5-163 2.20e-74

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: 219.90  E-value: 2.20e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:COG0440    2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEESV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881014629  85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGPKPM 163
Cdd:COG0440   82 ERELALIKVKADGETRSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGSKSL 160
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 5-160 9.36e-55

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: 169.85  E-value: 9.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629    5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAIV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881014629   85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGP 160
Cdd:TIGR00119  82 ERELCLVKVSAPGEGRDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
ilvH CHL00100
acetohydroxyacid synthase small subunit
 5-161 1.13e-50

acetohydroxyacid synthase small subunit


Pssm-ID: 214364 [Multi-domain]  Cd Length: 174  Bit Score: 160.26  E-value: 1.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVVRQPPETMV 84
Cdd:CHL00100   3 HTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNILKVQDITNIPCV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881014629  85 SRGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMARGPK 161
Cdd:CHL00100  83 ERELMLIKINVNSQTRPEILEIAQIFRAKVVDLSEESLILEVTGDPGKIVAIEQLLEKFGIIEIARTGKIALIRESK 159
ALS_ss_C pfam10369
Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of ...
 86-158 2.04e-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: 102.81  E-value: 2.04e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881014629   86 RGLLMVKVSCDNTNRPQVVDAANLFRARVVDVSQESVIIEATGERSKLVALLEVLEPFGIRELIQSGTVAMAR 158
Cdd:pfam10369   1 RELALIKVKADPEDRAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 5-76 6.47e-29

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: 101.44  E-value: 6.47e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKVV 76
Cdd:cd04878    1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKVS 72
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 13-75 2.16e-13

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: 61.45  E-value: 2.16e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881014629   13 DEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETlPIEQITKQLNKLVPVLKV 75
Cdd:pfam13710   1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQLTVESDR-SVELLLNQLEKLYDVVKV 62
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 5-69 4.82e-10

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: 52.69  E-value: 4.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881014629    5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETEtEGVNRITVVVETETLPIEQITKQLNKL 69
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSE-DKGGIVFVVIVVDEEDLEEVLEALKKL 64
IlvM COG3978
Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]; ...
 5-75 5.61e-09

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


Pssm-ID: 443177  Cd Length: 75  Bit Score: 50.22  E-value: 5.61e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNrITVVVETETlPIEQITKQLNKLVPVLKV 75
Cdd:COG3978    4 YQLTIEARRRPGALERVLRVVRHRGFEVRSMNMEANDGDGLN-IELTVSSDR-PIELLTRQLEKLYDVESV 72
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 7-66 1.79e-07

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: 45.75  E-value: 1.79e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   7 LSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETlPIEQITKQL 66
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDG-DLEKLLEAL 59
PRK06737 PRK06737
ACT domain-containing protein;
5-75 5.12e-07

ACT domain-containing protein;


Pssm-ID: 180675  Cd Length: 76  Bit Score: 45.07  E-value: 5.12e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881014629   5 HTLSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVVETETLPIEQITKQLNKLVPVLKV 75
Cdd:PRK06737   3 HTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINVLQV 73
PRK08178 PRK08178
acetolactate synthase 1 small subunit;
5-81 1.69e-05

acetolactate synthase 1 small subunit;


Pssm-ID: 236174  Cd Length: 96  Bit Score: 41.61  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   5 HTLSVLTLD---EPGILVRIAGMFTRRGFSIQSITSGETETEGVNRITVVV-ETETLpiEQITKQLNKLVPVLKVVRQPP 80
Cdd:PRK08178   6 HDNVILELTvrnHPGVMSHVCGLFARRAFNVEGILCLPIQDGDKSRIWLLVnDDQRL--EQMISQIEKLEDVLKVRRNQS 83


                 .
gi 881014629  81 E 81
Cdd:PRK08178  84 D 84
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-76 1.44e-03

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 38.13  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014629   1 MAELHT---LSVLTLDEPGILVRIAGMFTRRGFSIQSITSGETETEGVnriTVVVETETLP---IEQITKQLNKLVPVLK 74
Cdd:PRK06349 342 MEEIESkyyLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGA---EIVIVTHETSeaaLRAALAAIEALDVVLG 418


                 ..
gi 881014629  75 VV 76
Cdd:PRK06349 419 IP 420
 
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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