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Conserved domains on  [gi|2501332|sp|Q57625|]
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RecName: Full=Probable acetolactate synthase small subunit; AltName: Full=Acetohydroxy-acid synthase small subunit; Short=AHAS; Short=ALS

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
 8-168 1.18e-88

acetolactate synthase 3 regulatory subunit; Reviewed


:

Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 256.16  E-value: 1.18e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332     8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:PRK11895   2 RHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    88 VQRELCLIKIYApTESAKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKI 167
Cdd:PRK11895  82 VERELALVKVRA-SGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKI 160


                 .
gi 2501332   168 L 168
Cdd:PRK11895 161 L 161
 
Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 8-168 1.18e-88

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 256.16  E-value: 1.18e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332     8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:PRK11895   2 RHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    88 VQRELCLIKIYApTESAKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKI 167
Cdd:PRK11895  82 VERELALVKVRA-SGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKI 160


                 .
gi 2501332   168 L 168
Cdd:PRK11895 161 L 161
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 8-168 8.16e-87

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: 251.48  E-value: 8.16e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:COG0440   1 RHTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332   88 VQRELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKI 167
Cdd:COG0440  81 VERELALIKVKADGET-RSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGSKS 159


                .
gi 2501332  168 L 168
Cdd:COG0440 160 L 160
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 8-165 1.12e-85

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: 248.43  E-value: 1.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332      8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2501332     88 VQRELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGP 165
Cdd:TIGR00119  81 VERELCLVKVSAPGEG-RDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 9-80 1.47e-35

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: 118.38  E-value: 1.47e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2501332    9 HVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVS 80
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 ...
 90-163 1.73e-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: 1.73e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2501332     90 RELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALAR 163
Cdd:pfam10369   1 RELALIKVKADPED-RAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
 
Name Accession Description Interval E-value
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 8-168 1.18e-88

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 256.16  E-value: 1.18e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332     8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:PRK11895   2 RHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    88 VQRELCLIKIYApTESAKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKI 167
Cdd:PRK11895  82 VERELALVKVRA-SGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGRGEKI 160


                 .
gi 2501332   168 L 168
Cdd:PRK11895 161 L 161
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 8-168 8.16e-87

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: 251.48  E-value: 8.16e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:COG0440   1 RHTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332   88 VQRELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKI 167
Cdd:COG0440  81 VERELALIKVKADGET-RSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGSKS 159


                .
gi 2501332  168 L 168
Cdd:COG0440 160 L 160
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 8-165 1.12e-85

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: 248.43  E-value: 1.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332      8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2501332     88 VQRELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGP 165
Cdd:TIGR00119  81 VERELCLVKVSAPGEG-RDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
ilvH CHL00100
acetohydroxyacid synthase small subunit
 8-167 1.79e-50

acetohydroxyacid synthase small subunit


Pssm-ID: 214364 [Multi-domain]  Cd Length: 174  Bit Score: 159.87  E-value: 1.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332     8 RHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKS 87
Cdd:CHL00100   2 KHTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNILKVQDITNIPC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    88 VQRELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKI 167
Cdd:CHL00100  82 VERELMLIKINVNSQT-RPEILEIAQIFRAKVVDLSEESLILEVTGDPGKIVAIEQLLEKFGIIEIARTGKIALIRESKV 160
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 9-80 1.47e-35

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: 118.38  E-value: 1.47e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2501332    9 HVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVS 80
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 ...
 90-163 1.73e-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: 1.73e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2501332     90 RELCLIKIYAPTESaKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALAR 163
Cdd:pfam10369   1 RELALIKVKADPED-RAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 17-79 1.38e-16

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: 69.92  E-value: 1.38e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2501332     17 NKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDkILEQVIKQLNKLIDVIKV 79
Cdd:pfam13710   1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQLTVESDR-SVELLLNQLEKLYDVVKV 62
PRK08178 PRK08178
acetolactate synthase 1 small subunit;
15-79 7.79e-14

acetolactate synthase 1 small subunit;


Pssm-ID: 236174  Cd Length: 96  Bit Score: 63.56  E-value: 7.79e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2501332    15 VLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNgDDKILEQVIKQLNKLIDVIKV 79
Cdd:PRK08178  15 VRNHPGVMSHVCGLFARRAFNVEGILCLPIQDGDKSRIWLLVN-DDQRLEQMISQIEKLEDVLKV 78
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 9-75 7.10e-12

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: 57.70  E-value: 7.10e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501332      9 HVISALVLNKPGVLQRISGLFTRRGFNISSITVGITEnPQISRVTIVVNGDDKILEQVIKQLNKLID 75
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSE-DKGGIVFVVIVVDEEDLEEVLEALKKLEG 66
PRK06737 PRK06737
ACT domain-containing protein;
9-82 1.56e-08

ACT domain-containing protein;


Pssm-ID: 180675  Cd Length: 76  Bit Score: 49.31  E-value: 1.56e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2501332     9 HVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSEL 82
Cdd:PRK06737   3 HTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINVLQVNKL 76
IlvM COG3978
Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]; ...
 4-82 1.96e-07

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


Pssm-ID: 443177  Cd Length: 75  Bit Score: 46.37  E-value: 1.96e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2501332    4 IMEHRHVISALvlNKPGVLQRISGLFTRRGFNISSITVGITENPQIsRVTIVVNGdDKILEQVIKQLNKLIDVIKVSEL 82
Cdd:COG3978   1 MMQYQLTIEAR--RRPGALERVLRVVRHRGFEVRSMNMEANDGDGL-NIELTVSS-DRPIELLTRQLEKLYDVESVEVL 75
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 11-70 2.29e-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: 2.29e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332   11 ISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDkILEQVIKQL 70
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDG-DLEKLLEAL 59
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
11-79 2.41e-05

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 43.61  E-value: 2.41e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332   11 ISALVLNKPGVLQRISGLFTRRGFNISSITVgITENPQISRVTIVVN-GDDKILEQVIKQLNKLIDVIKV 79
Cdd:COG0317 649 IRIEALDRPGLLADITSVIAEEKINILSVNT-RSRDDGTATIRFTVEvRDLDHLARVLRKLRKVPGVISV 717
PRK13562 PRK13562
ACT domain-containing protein;
15-83 4.80e-05

ACT domain-containing protein;


Pssm-ID: 184144  Cd Length: 84  Bit Score: 39.93  E-value: 4.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501332    15 VLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVN-GDDKILEQVIKQLNKLIDVIKVSELE 83
Cdd:PRK13562   9 VADQVSTLNRITSAFVRLQYNIDTLHVTHSEQPGISNMEIQVDiQDDTSLHILIKKLKQQINVLTVECYD 78
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
 17-79 9.83e-05

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151  Cd Length: 71  Bit Score: 38.99  E-value: 9.83e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2501332   17 NKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVngDDKILEQVIKQLNKLIDVIKV 79
Cdd:cd04879   8 DVPGVIGKVGTILGEHGINIAAMQVGRKEKGGIAYMVLDV--DSPVPEEVLEELKALPGIIRV 68
ACT_3PGDH-xct cd04902
C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The ...
 17-83 4.79e-03

C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with an extended C-terminal (xct) region from bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. Some 3PGDH enzymes have an additional domain formed by an extended C-terminal region. This additional domain introduces significant asymmetry to the homotetramer. Adjacent ACT (regulatory) domains interact, creating two serine-binding sites, however, this asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. How this asymmetry influences the mechanism of effector inhibition is still unknown. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153174  Cd Length: 73  Bit Score: 34.37  E-value: 4.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501332   17 NKPGVLQRISGLFTRRGFNISSITVGITENPQISrvTIVVNGDDKILEQVIKQLNKLIDVIKVSELE 83
Cdd:cd04902   8 DRPGVIGKVGTILGEAGINIAGMQVGRDEPGGEA--LMVLSVDEPVPDEVLEELRALPGILSAKVVE 72
ilvM PRK11152
acetolactate synthase 2 small subunit;
17-80 8.03e-03

acetolactate synthase 2 small subunit;


Pssm-ID: 236862  Cd Length: 76  Bit Score: 33.70  E-value: 8.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2501332    17 NKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKIlEQVIKQLNKLIDVIKVS 80
Cdd:PRK11152  12 FRPEVLERVLRVVRHRGFQVCSMNMTQNTDAQNINIELTVASERPI-DLLSSQLNKLVDVAHVE 74
 
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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