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Conserved domains on  [gi|1870085669|pdb|6WO1|B]
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Chain B, Acetohydroxyacid synthase regulatory subunit

Protein Classification

acetolactate synthase small subunit( domain architecture ID 11488632)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 77-282 1.11e-76

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: 231.10  E-value: 1.11e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B         77 QHVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEI 156
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B        157 IKRELVMARISLLGteyfedlllhhhtstnagaadsqelvaeirekqfhpanlpasevlrlkhEHLNDITNLTNNFGGRV 236
Cdd:TIGR00119  81 VERELCLVKVSAPG-------------------------------------------------EGRDEIIRLTNIFRGRI 111

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
6WO1_B        237 VDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTP 282
Cdd:TIGR00119 112 VDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
 
Name Accession Description Interval E-value
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 77-282 1.11e-76

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: 231.10  E-value: 1.11e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B         77 QHVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEI 156
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B        157 IKRELVMARISLLGteyfedlllhhhtstnagaadsqelvaeirekqfhpanlpasevlrlkhEHLNDITNLTNNFGGRV 236
Cdd:TIGR00119  81 VERELCLVKVSAPG-------------------------------------------------EGRDEIIRLTNIFRGRI 111

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
6WO1_B        237 VDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTP 282
Cdd:TIGR00119 112 VDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 78-282 9.24e-52

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: 167.51  E-value: 9.24e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B       78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEII 157
Cdd:COG0440   2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEESV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B      158 KRELVMARIsllgteyfedlllhhhtstnagAADSQELvaeirekqfhpanlpaSEVLRlkhehlnditnLTNNFGGRVV 237
Cdd:COG0440  82 ERELALIKV----------------------KADGETR----------------SEILR-----------IAEIFRARIV 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
6WO1_B      238 DISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTP 282
Cdd:COG0440 113 DVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGS 157
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 78-280 2.58e-47

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 156.39  E-value: 2.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B        78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEII 157
Cdd:PRK11895   3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B       158 KRELVMARISllgteyfedlllhhhtstnagaadsqeLVAEIRekqfhpanlpaSEVLRlkhehlnditnLTNNFGGRVV 237
Cdd:PRK11895  83 ERELALVKVR---------------------------ASGENR-----------AEILR-----------LADIFRAKIV 113

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
6WO1_B       238 DISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPR 280
Cdd:PRK11895 114 DVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGR 156
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 78-148 4.15e-32

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


Pssm-ID: 153150  Cd Length: 72  Bit Score: 114.15  E-value: 4.15e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6WO1_B       78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAV 148
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 ...
 220-280 8.56e-16

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: 70.84  E-value: 8.56e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
6WO1_B        220 EHLNDITNLTNNFGGRVVDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPR 280
Cdd:pfam10369  13 EDRAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
 
Name Accession Description Interval E-value
acolac_sm TIGR00119
acetolactate synthase, small subunit; Acetolactate synthase is a heterodimeric thiamine ...
 77-282 1.11e-76

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: 231.10  E-value: 1.11e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B         77 QHVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEI 156
Cdd:TIGR00119   1 RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVIKVSDLTESAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B        157 IKRELVMARISLLGteyfedlllhhhtstnagaadsqelvaeirekqfhpanlpasevlrlkhEHLNDITNLTNNFGGRV 236
Cdd:TIGR00119  81 VERELCLVKVSAPG-------------------------------------------------EGRDEIIRLTNIFRGRI 111

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
6WO1_B        237 VDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTP 282
Cdd:TIGR00119 112 VDVSPDSYTVEVTGDSDKIDAFLELLRPFGIKEVARTGKTALSRGP 157
IlvH COG0440
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ...
 78-282 9.24e-52

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: 167.51  E-value: 9.24e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B       78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEII 157
Cdd:COG0440   2 HTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVIKVVDLTDEESV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B      158 KRELVMARIsllgteyfedlllhhhtstnagAADSQELvaeirekqfhpanlpaSEVLRlkhehlnditnLTNNFGGRVV 237
Cdd:COG0440  82 ERELALIKV----------------------KADGETR----------------SEILR-----------IAEIFRARIV 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
6WO1_B      238 DISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTP 282
Cdd:COG0440 113 DVTPDSLTIELTGDEEKIDAFIELLKPYGILEVVRTGRVALSRGS 157
ilvH PRK11895
acetolactate synthase 3 regulatory subunit; Reviewed
 78-280 2.58e-47

acetolactate synthase 3 regulatory subunit; Reviewed


Pssm-ID: 183365 [Multi-domain]  Cd Length: 161  Bit Score: 156.39  E-value: 2.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B        78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSEII 157
Cdd:PRK11895   3 HTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDVLKVVDLTEEAHV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B       158 KRELVMARISllgteyfedlllhhhtstnagaadsqeLVAEIRekqfhpanlpaSEVLRlkhehlnditnLTNNFGGRVV 237
Cdd:PRK11895  83 ERELALVKVR---------------------------ASGENR-----------AEILR-----------LADIFRAKIV 113

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
6WO1_B       238 DISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPR 280
Cdd:PRK11895 114 DVTPESLTIEVTGDSDKIDAFIDLLRPYGIKEIVRTGVVAIGR 156
ilvH CHL00100
acetohydroxyacid synthase small subunit
 76-288 1.34e-36

acetohydroxyacid synthase small subunit


Pssm-ID: 214364 [Multi-domain]  Cd Length: 174  Bit Score: 129.06  E-value: 1.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B        76 KQHVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAVLDYTNSE 155
Cdd:CHL00100   1 MKHTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNILKVQDITNIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WO1_B       156 IIKRELVMARISLLGteyfedlllhhhtstnagaadsqelvaeirekqfhpanlpasevlrlkhEHLNDITNLTNNFGGR 235
Cdd:CHL00100  81 CVERELMLIKINVNS-------------------------------------------------QTRPEILEIAQIFRAK 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
6WO1_B       236 VVDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTPlKTSTE 288
Cdd:CHL00100 112 VVDLSEESLILEVTGDPGKIVAIEQLLEKFGIIEIARTGKIALIRES-KVNTE 163
ACT_AHAS cd04878
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ...
 78-148 4.15e-32

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


Pssm-ID: 153150  Cd Length: 72  Bit Score: 114.15  E-value: 4.15e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6WO1_B       78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVIEQARRQIEDLVPVYAV 148
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 ...
 220-280 8.56e-16

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: 70.84  E-value: 8.56e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
6WO1_B        220 EHLNDITNLTNNFGGRVVDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPR 280
Cdd:pfam10369  13 EDRAEILRIADIFRAKIVDVSPDSLTIELTGTPEKIDAFIELLKPFGILEVVRTGRVALER 73
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 78-142 3.25e-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: 55.39  E-value: 3.25e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
6WO1_B         78 HVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKdLSRMTIVLQGQDGVIEQARRQIEDL 142
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDK-GGIVFVVIVVDEEDLEEVLEALKKL 64
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 80-140 5.64e-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: 5.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
6WO1_B       80 LNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGqDGVIEQARRQIE 140
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDG-DGDLEKLLEALE 60
ACT_5 pfam13710
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 86-148 3.43e-06

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: 43.73  E-value: 3.43e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
6WO1_B         86 NEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGViEQARRQIEDLVPVYAV 148
Cdd:pfam13710   1 DRPGVLERVLRVVRRRGFHVTSMNMSATEDGGLVRIQLTVESDRSV-ELLLNQLEKLYDVVKV 62
IlvM COG3978
Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]; ...
 76-148 7.21e-05

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


Pssm-ID: 443177  Cd Length: 75  Bit Score: 40.59  E-value: 7.21e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6WO1_B       76 KQHVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEvKDLSRMTIVLQGQDGvIEQARRQIEDLVPVYAV 148
Cdd:COG3978   2 MQYQLTIEARRRPGALERVLRVVRHRGFEVRSMNMEAND-GDGLNIELTVSSDRP-IELLTRQLEKLYDVESV 72
PRK08178 PRK08178
acetolactate synthase 1 small subunit;
79-148 1.28e-04

acetolactate synthase 1 small subunit;


Pssm-ID: 236174  Cd Length: 96  Bit Score: 40.45  E-value: 1.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6WO1_B        79 VLNCLVQNEPGVLSRVSGTLAARGFNIDSlVVCnTEVKDLSRMTIVLQ-GQDGVIEQARRQIEDLVPVYAV 148
Cdd:PRK08178  10 ILELTVRNHPGVMSHVCGLFARRAFNVEG-ILC-LPIQDGDKSRIWLLvNDDQRLEQMISQIEKLEDVLKV 78
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 80-142 4.20e-04

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: 38.27  E-value: 4.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
6WO1_B       80 LNCLVQNEPGVLSRVSGTLAARGFNIDSLVvcNTEVKDLSRMTIVL---QGQDGVIEQARRQIEDL 142
Cdd:cd04881   3 LRLTVKDKPGVLAKITGILAEHGISIESVI--QKEADGGETAPVVIvthETSEAALNAALAEIEAL 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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