3B6R,1M15


Conserved Protein Domain Family
phosphagen_kinases

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cd00330: phosphagen_kinases 
Click on image for an interactive view with Cn3D
Phosphagen (guanidino) kinases.
Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized.
Statistics
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PSSM-Id: 153075
View PSSM: cd00330
Aligned: 3 rows
Threshold Bit Score: 364.219
Threshold Setting Gi: 586899
Created: 6-Mar-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:ADP binding site [chemical binding site]
Evidence:
  • Structure:1M15: a transition state analogue of Limulus polyphemus arginine kinase binds ADP-Mg++, contacts at 4A
    View structure with Cn3D
  • Citation:PMID 9041648

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1       # # #                                                            #            
3B6R_B    126 VLSSRVRTGRSIrGFCLPphcSRGERRAIEKLAVEALSsldgdlaGRYYALKSMt--eAEQQQLIDDHFLFDKpvsplll 203 human
1M15_A    120 IISTRVRCGRSLqGYPFNpclTAEQYKEMEEKVSSTLSsmedelkGTYYPLTGMs--kATQQQLIDDHFLFKEgdrflqt 197 Limulus polyphemus
P37570     25 VLSSRIRLARNFeHIRFPtrySNEEASSIIQQFEDQFSeqeipgiGKFVLIRMNdaqpLEKRVLVEKHLISPNlt----- 99  Bacillus subtilis
Feature 1                             #       #                                               
3B6R_B    204 asgmardWPDARGIWHNDnkTFLVWVNEEDHLRVISMQKGgNMKEVFTRFCTGLTQIETLFkskdyeFMWNPHLGYILTC 283 human
1M15_A    198 -anacryWPTGRGIFHNDakTFLVWVNEEDHLRIISMQKGgDLKTVYKRLVTAVDNIESKLp-----FSHDDRFGFLTFC 271 Limulus polyphemus
P37570    100 ------eSPFGGCLLSENe-EVSVMLNEEDHIRIQCLFPGfQLLEAMKAANQVDDWIEEKVd-----YAFNEQRGYLTSC 167 Bacillus subtilis
Feature 1             # ###                          # #            #                         
3B6R_B    284 PSNLGTGLRAGVHIKLPNLGkh---eKFSEVLKRLRLQKRGTggvdtaavggVFDVSNADRLgfsevELVQMVVDGVKLL 360 human
1M15_A    272 PTNLGTTMRASVHIQLPKLAkd--rkVLEDIASKFNLQVRGTrgehteseggVYDISNKRRLglteyQAVREMQDGILEM 349 Limulus polyphemus
P37570    168 PTNVGTGLRASVMMHLPALVltrqinRIIPAINQLGLVVRGIygegseavgnIFQISNQITLgkseqDIVEDLNSVAAQL 247 Bacillus subtilis
Feature 1           
3B6R_B    361 IEMEQR 366 human
1M15_A    350 IKMEKA 355 Limulus polyphemus
P37570    248 IEQERS 253 Bacillus subtilis

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