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Conserved domains on  [gi|1945735099|gb|KAG0236976|]
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hypothetical protein BGW42_002189 [Actinomortierella wolfii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
acolac_sm super family cl36591
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 94-286 1.06e-64

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]


The actual alignment was detected with superfamily member TIGR00119:

Pssm-ID: 272916 [Multi-domain]  Cd Length: 157  Bit Score: 200.66  E-value: 1.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSILGPehvraqmnsrspewqqqfeeedaeemspsnalrqthaHLKSLTELTKLFQGKVVDVSSESVAIELS 253
Cdd:TIGR00119  82 ERELCLVKVSAPGE-------------------------------------GRDEIIRLTNIFRGRIVDVSPDSYTVEVT 124

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:TIGR00119 125 GDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
 
Name Accession Description Interval E-value
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 94-286 1.06e-64

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: 200.66  E-value: 1.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSILGPehvraqmnsrspewqqqfeeedaeemspsnalrqthaHLKSLTELTKLFQGKVVDVSSESVAIELS 253
Cdd:TIGR00119  82 ERELCLVKVSAPGE-------------------------------------GRDEIIRLTNIFRGRIVDVSPDSYTVEVT 124

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:TIGR00119 125 GDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 94-286 1.88e-61

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: 192.55  E-value: 1.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:COG0440     2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEESV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSilGPEHVRAQMNsrspewqqqfeeedaeemspsnalrqthahlksltELTKLFQGKVVDVSSESVAIELS 253
Cdd:COG0440    82 ERELALIKVK--ADGETRSEIL-----------------------------------RIAEIFRARIVDVTPDSLTIELT 124

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:COG0440   125 GDEEKIDAFIELLKPYGILEVVRTGRVALSRGS 157
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 94-286 7.24e-60

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 188.36  E-value: 7.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:PRK11895    3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSilGPEHVRAQMnsrspewqqqfeeedaeemspsnalrqthahlkslTELTKLFQGKVVDVSSESVAIELS 253
Cdd:PRK11895   83 ERELALVKVR--ASGENRAEI-----------------------------------LRLADIFRAKIVDVTPESLTIEVT 125

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:PRK11895  126 GDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGE 158
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 94-164 2.32e-33

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: 117.23  E-value: 2.32e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAV 164
Cdd:cd04878     1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKV 71
ALS_ss_C pfam10369
Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of ...
 175-284 7.15e-20

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: 81.63  E-value: 7.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 175 RELLLIKVSIlgPEHVRAQmnsrspewqqqfeeedaeemspsnalrqthahlksLTELTKLFQGKVVDVSSESVAIELSA 254
Cdd:pfam10369   1 RELALIKVKA--DPEDRAE-----------------------------------ILRIADIFRAKIVDVSPDSLTIELTG 43

                          90       100       110
                  ....*....|....*....|....*....|
gi 1945735099 255 KPERIDAFIKLVKPFGILEAARSGMMAMPR 284
Cdd:pfam10369  44 TPEKIDAFIELLKPFGILEVVRTGRVALER 73
 
Name Accession Description Interval E-value
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 94-286 1.06e-64

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: 200.66  E-value: 1.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:TIGR00119   2 HILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSILGPehvraqmnsrspewqqqfeeedaeemspsnalrqthaHLKSLTELTKLFQGKVVDVSSESVAIELS 253
Cdd:TIGR00119  82 ERELCLVKVSAPGE-------------------------------------GRDEIIRLTNIFRGRIVDVSPDSYTVEVT 124

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:TIGR00119 125 GDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 94-286 1.88e-61

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: 192.55  E-value: 1.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:COG0440     2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEESV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSilGPEHVRAQMNsrspewqqqfeeedaeemspsnalrqthahlksltELTKLFQGKVVDVSSESVAIELS 253
Cdd:COG0440    82 ERELALIKVK--ADGETRSEIL-----------------------------------RIAEIFRARIVDVTPDSLTIELT 124

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:COG0440   125 GDEEKIDAFIELLKPYGILEVVRTGRVALSRGS 157
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 94-286 7.24e-60

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 188.36  E-value: 7.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:PRK11895    3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKVSilGPEHVRAQMnsrspewqqqfeeedaeemspsnalrqthahlkslTELTKLFQGKVVDVSSESVAIELS 253
Cdd:PRK11895   83 ERELALVKVR--ASGENRAEI-----------------------------------LRLADIFRAKIVDVTPESLTIEVT 125

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:PRK11895  126 GDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGE 158
ilvH CHL00100
acetohydroxyacid synthase small subunit
 94-286 1.85e-39

acetohydroxyacid synthase small subunit


Pssm-ID: 214364 [Multi-domain]  Cd Length: 174  Bit Score: 136.76  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAVLDYTGFNVI 173
Cdd:CHL00100    3 HTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNILKVQDITNIPCV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 174 KRELLLIKvsilgpehVRAQMNSRSpewqqqfeeedaeemspsnalrqthahlkSLTELTKLFQGKVVDVSSESVAIELS 253
Cdd:CHL00100   83 ERELMLIK--------INVNSQTRP-----------------------------EILEIAQIFRAKVVDLSEESLILEVT 125

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1945735099 254 AKPERIDAFIKLVKPFGILEAARSGMMAMPRSP 286
Cdd:CHL00100  126 GDPGKIVAIEQLLEKFGIIEIARTGKIALIRES 158
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 94-164 2.32e-33

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: 117.23  E-value: 2.32e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESATIEQARRQLEDLVPVWAV 164
Cdd:cd04878     1 HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLKV 71
ALS_ss_C pfam10369
Small subunit of acetolactate synthase; ALS_ss_C is the C-terminal half of a family of ...
 175-284 7.15e-20

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: 81.63  E-value: 7.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 175 RELLLIKVSIlgPEHVRAQmnsrspewqqqfeeedaeemspsnalrqthahlksLTELTKLFQGKVVDVSSESVAIELSA 254
Cdd:pfam10369   1 RELALIKVKA--DPEDRAE-----------------------------------ILRIADIFRAKIVDVSPDSLTIELTG 43

                          90       100       110
                  ....*....|....*....|....*....|
gi 1945735099 255 KPERIDAFIKLVKPFGILEAARSGMMAMPR 284
Cdd:pfam10369  44 TPEKIDAFIELLKPFGILEVVRTGRVALER 73
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 94-158 6.03e-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: 54.62  E-value: 6.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEvADLSRMTIVLRGESATIEQARRQLEDL 158
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSE-DKGGIVFVVIVVDEEDLEEVLEALKKL 64
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 102-161 6.73e-08

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: 6.73e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 102 NEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESAtIEQARRQLEDLVPV 161
Cdd:pfam13710   1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQLTVESDRS-VELLLNQLEKLYDV 59
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 100-156 2.96e-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: 46.90  E-value: 2.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1945735099 100 VQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRGESaTIEQARRQLE 156
Cdd:cd02116     5 GPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDG-DLEKLLEALE 60
IlvM COG3978
Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]; ...
 92-161 1.04e-05

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


Pssm-ID: 443177  Cd Length: 75  Bit Score: 42.90  E-value: 1.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  92 QHHIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEvADLSRMTIVLRGESAtIEQARRQLEDLVPV 161
Cdd:COG3978     2 MQYQLTIEARRRPGALERVLRVVRHRGFEVRSMNMEAND-GDGLNIELTVSSDRP-IELLTRQLEKLYDV 69
PRK06737 PRK06737
ACT domain-containing protein;
94-164 8.00e-05

ACT domain-containing protein;


Pssm-ID: 180675  Cd Length: 76  Bit Score: 40.45  E-value: 8.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945735099  94 HIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRM--TIVLRGESATIEQArrQLEDLVPVWAV 164
Cdd:PRK06737    3 HTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMklTAVCTENEATLLVS--QLKKLINVLQV 73
PRK08178 PRK08178
acetolactate synthase 1 small subunit;
100-171 9.15e-05

acetolactate synthase 1 small subunit;


Pssm-ID: 236174  Cd Length: 96  Bit Score: 40.84  E-value: 9.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945735099 100 VQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRMTIVLRgESATIEQARRQLEDLVPVWAVL----DYTGFN 171
Cdd:PRK08178   15 VRNHPGVMSHVCGLFARRAFNVEGILCLPIQDGDKSRIWLLVN-DDQRLEQMISQIEKLEDVLKVRrnqsDPTMFN 89
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 99-158 1.23e-03

ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153153 [Multi-domain]  Cd Length: 79  Bit Score: 37.11  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945735099  99 LVQNEPGVLSRVSGILAGRGFNIDSLVvaKTEVADLSRMTIVL---RGESATIEQARRQLEDL 158
Cdd:cd04881     6 TVKDKPGVLAKITGILAEHGISIESVI--QKEADGGETAPVVIvthETSEAALNAALAEIEAL 66
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
91-183 2.03e-03

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


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 37.43  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  91 KQHHIFnclVQNEPGVLSRVSGILAGRGFNIDSLVVAktEVADLS--RMtIVLRGesatiEQARRQLEDLvpvwavldyt 168
Cdd:COG4747     1 KQISVF---LENKPGRLAEVTRLLGDAGINIRALSIA--DTSDFGilRL-IVDDP-----EKAREVLKEA---------- 59

                          90
                  ....*....|....*
gi 1945735099 169 GFNVIKRELLLIKVS 183
Cdd:COG4747    60 GFTVSETDVLAVELP 74
ACT_PDH-BS-like cd04889
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) ...
 100-156 2.69e-03

C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate; Included in this CD is the C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Also 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. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153161  Cd Length: 56  Bit Score: 35.56  E-value: 2.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1945735099 100 VQNEPGVLSRVSGILAGRGFNIDSLvvaktEVADLSRMTIVLRGESATIEQARRQLE 156
Cdd:cd04889     5 VENKPGRLAEVTEILAEAGINIKAI-----SIAETRGEFGILRLIFSDPERAKEVLK 56
ACT_Bt0572_2 cd04882
C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD ...
 100-157 3.36e-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: 35.27  E-value: 3.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099 100 VQNEPGVLSRVSGILAGRGFNIDSL--VVAKTEvadlSRMTIVLRgeSATIEQARRQLED 157
Cdd:cd04882     6 VPDKPGGLHEILQILSEEGINIEYMyaFVEKKG----GKALLIFR--TEDIEKAIEVLQE 59
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 100-142 5.70e-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: 34.92  E-value: 5.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1945735099 100 VQNEPGVLSRVSGILAGRGFNIDSLVVAKTEVADLSRmtIVLR 142
Cdd:cd04883     8 VPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEEDNKI--LVFR 48
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
82-158 8.86e-03

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 36.35  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735099  82 TPPSGRNKAKQHHIFNCLVQNEPGVLSRVSGILAGRGFNIDSLVV----AKTEVADLSRMTIVLR-GESATIEQARRQLE 156
Cdd:COG2716    79 TEPHEAPPAGLPYVVEVVGNDRPGIVAEVTQFLAERGINIEDLSTktypAPMSGTPLFSAQITVHvPAGLDIDALRDALE 158


                  ..
gi 1945735099 157 DL 158
Cdd:COG2716   159 DL 160
 
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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