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


Conserved Protein Domain Family
ACT_AK-like

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cd04868: ACT_AK-like 
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ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase)
This CD includes each of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). Typically, AK consists of two 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. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Aspartokinase 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 aspartokinase 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 aspartokinase 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 aspartokinases 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 AK family 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
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PSSM-Id: 153140
View PSSM: cd04868
Aligned: 325 rows
Threshold Bit Score: 31.314
Threshold Setting Gi: 83859687
Created: 24-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
2J0X_A       309 TLLTLHSLnml-hsRGFLAEVFGILArhNISVDLITTSeVSVALTLDttgststgdtlltQSLLMELS 375 Escherichia coli
Q04795       340 AKVSAVGAgim-gvPGVTSKIVSALSekEIPILQSADShTTIWVLVHea---------dmVPAVNALH 397 Bacillus subtilis
ZP_01465238  361 AKVSLVGIglr-sdPGIAARLCRSLTeqGIHVSGLSVNeLRISCLVEgd---------aaDQAVCILH 418 Stigmatella aurantiaca DW4/3-1
NP_623000    336 AKVSIIGNrir-gvPGVMARVIKALSkrNIEIYQTADShNTISCLVSqd---------kvEEAIRVLH 393 Thermoanaerobacter tengcong...
YP_075377    341 AKVTVVGSgmr-grPGVMATVAEALYaaEVPIWQTADShVTISCLIPaa---------dvQRAVQALH 398 Symbiobacterium thermophilu...
BAB81384     336 STIAIVGSrmr-giPGVMAKIVGALDneNIEVLQTADShMTIWCLVEsk---------nvREAIKALH 393 Clostridium perfringens str...
AAK79775     334 SKIAIIGNric-gvPGVMAKILKAITkeGIEVLQTADShTTIWCLVKsn---------vrNKAINALH 391 Clostridium acetobutylicum ...
ZP_00801907  342 SKVTVVGNrit-giPGVMATIVGALSseDIQILQSSDShSTISCLVDes---------daKKAVNALH 399 Alkaliphilus metalliredigen...
YP_535949    335 VKVSIIGGgmv-gtPGVIAKMVTALSktGVEILQTADSdTTVWILVTed---------nfKLAVNTLH 392 Lactobacillus salivarius su...
YP_001087818 343 AKVTLICSriademSGIMSKVVRGLSkaGVSLLQTSDSnMTISCLVSee---------dmHTAVHAIH 401 Clostridium difficile 630
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