2CDQ,2HMF,2J0W,2J0X,2HMF,2CDQ,2J0X


Conserved Protein Domain Family
ACT_AK-like_2

?
cd04892: ACT_AK-like_2 
Click on image for an interactive view with Cn3D
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase)
This CD includes the second of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). The exception in this group, is the inclusion of the first ACT domain of the bifunctional aspartokinase - homoserine dehydrogenase-like enzyme group (ACT_AKi-HSDH-ThrA-like_1) which includes the monofunctional, threonine-sensitive, aspartokinase found in Methanococcus jannaschii and other related archaeal species. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. AK is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of AK with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different AK isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are AKs with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
?
PSSM-Id: 153164
View PSSM: cd04892
Aligned: 177 rows
Threshold Bit Score: 40.5581
Threshold Setting Gi: 1790376
Created: 26-Mar-2007
Updated: 2-Oct-2020
Structure
?
Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
2CDQ_A       421 AIISLIGNvq--hsSLILERAFHVLYtkGVNVQMISQGaskVNISFIVNEAEAEGCVQALHKSFFE 484 thale cress
NP_623000    336 AKVSIIGNrir-gvPGVMARVIKALSkrNIEIYQTADSh--NTISCLVSQDKVEEAIRVLHDEFSL 398 Thermoanaerobacter tengcongen...
ZP_00953207  342 AKVSVVGTglr-grADVARTLYGVLAreGIAVRMTATSe--IKISALVDADYLEHAVRALHAAYRL 404 Oceanicaulis alexandrii HTCC2633
NP_695686    103 GKVAVVGVgmk-thAGLAAKFFQALSdeGINVLMISTSe--IRIAALVPLDQLNDAVKALHTAYGL 165 Bifidobacterium longum NCC2705
YP_535949    335 VKVSIIGGgmv-gtPGVIAKMVTALSktGVEILQTADSd--TTVWILVTEDNFKLAVNTLHEAFLE 397 Lactobacillus salivarius subs...
Q04795       340 AKVSAVGAgim-gvPGVTSKIVSALSekEIPILQSADSh--TTIWVLVHEADMVPAVNALHEEFEL 402 Bacillus subtilis
ZP_01465238  361 AKVSLVGIglr-sdPGIAARLCRSLTeqGIHVSGLSVNe--LRISCLVEGDAADQAVCILHETFEL 423 Stigmatella aurantiaca DW4/3-1
BAB81384     336 STIAIVGSrmr-giPGVMAKIVGALDneNIEVLQTADSh--MTIWCLVESKNVREAIKALHRVFMK 398 Clostridium perfringens str. 13
AAK79775     334 SKIAIIGNric-gvPGVMAKILKAITkeGIEVLQTADSh--TTIWCLVKSNVRNKAINALHREFNL 396 Clostridium acetobutylicum AT...
YP_001087818 343 AKVTLICSriademSGIMSKVVRGLSkaGVSLLQTSDSn--MTISCLVSEEDMHTAVHAIHQQFYL 406 Clostridium difficile 630
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap