1EQM,1EX8,1HKA,1CBK


Conserved Protein Domain Family
HPPK

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cd00483: HPPK 
Click on image for an interactive view with Cn3D
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is HPPK which catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The functional enzyme is a monomer. Mammals lack many of the enzymes in the folate pathway including, HPPK.
Statistics
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PSSM-Id: 238269
Aligned: 103 rows
Threshold Bit Score: 91.0007
Created: 6-Mar-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
catalyticATP binding
Conserved site includes 21 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic center binding site [active site]
Evidence:
  • Comment:the catalytic center is assembled upon the binding of both substrates (HP and MgATP)
  • Comment:A number of HP analog inhibitors have been developed which bind to this site
  • Structure:1EX8 A; HPPK binds bisubstrate inhibitor, 6-adenosine tetraphosphate-methyl-7,8-dihydropterin

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1            #                                 ## #            # #              #   #  #
1EQM_A        3 AYIAIGSNLasPLEQVNAALKALGDipeshILTVSSFYRTPPLGpq-----dQPDYLNAAVALETSLAPEELLNHTQRIE 77  Escherichia coli
1EX8_A        3 AYIAIGSNLasPLEQVNAALKALGDipeshILTVSSFYRTPPLGpq-----dQPDYLNAAVALETSLAPEELLNHTQRIE 77  Escherichia coli
CAG18868      4 VYISLGSNIq-REYHIHAAISELKKis--sTCQISRLFEAEPVGf------sGPNFFNCVVEIETSLSFDTLQQTLKELE 74  Photobacterium p...
NP_638779     4 VLLSLGSNVq-PTHYLRLAVEALRArf--gPIDVSPAYRTAAVGf------dGPDFVNNGVQLQTDWELQALDDWLHALE 74  Xanthomonas camp...
ZP_00288667  10 VLVAFGASLn-PLYHLELGLRRLHAll--gIVAISDVYQSRPVNga----vgDPPFLNGAVRLEQAPEPWALRALLRQIE 82  Magnetococcus sp...
Q9Z7E8        7 VCLSLGSNLgnRFKNLQIARTLLGEqa-vlGLRSSVILETEALLlpgsppewDLPYFNSVLVGETTLSLRELLVTIKQIE 85  Chlamydophila pn...
Q821E2        7 ICLSLGSNLgnRFEIFRKAFALLKEle-ieDLQSSIILETKALLlpgspkewDLPFFNSVLIGKTTLSPKQLLSGVKQIE 85  Chlamydophila ca...
ZP_00210975  10 VILALGSNCgnMLGYIKSAVSMLPLy----NMNYSYLYKTPALLpenaadhwDTPFLNMVVSGYTNLSPHSMLEQVKSIE 85  Ehrlichia canis ...
ZP_00187902   4 VFLGLGSNLgdRAGYLRAAVRALRRgprleVVAVSPVYETDPVEve----geQPAYLNCAVELRCGLGPLELLRYCQGVE 79  Rubrobacter xyla...
ZP_00039312  42 VLLSLGSNVrpRYYLRQAEAALHAFf---gEVLFSPVYRTLAVGf------dGPDFLNSAAMVHTAMSLSDLHAWLHALE 112 Xylella fastidio...
Feature 1           # #    #  #  # ##                #  ##    # #        
1EQM_A       78 LQQGRVRkaeRWGPRTLDLDIMLFGn--EVINTe-rLTVPHYDMKNRGFMLWPLFEI 131 Escherichia coli
1EX8_A       78 LQQGRVRkaeRWGPRTLDLDIMLFGn--EVINTe-rLTVPHYDMKNRGFMLWPLFEI 131 Escherichia coli
CAG18868     75 VQYGRSPnaqKNQSRTLDLDILLFG---DVCRDs-aPVLPRSDIYKFAFVLWPLTEL 127 Photobacterium profundum
NP_638779    75 DRHGRDRsgpRFSDRTLDVDVVFFGd--RIVEGp-gHLRVPRPELKHAFVLKPLADI 128 Xanthomonas campestris pv. campestris s...
ZP_00288667  83 AEQGRERgdnPNAPRTLDLDIALMGs--QIMDEp-lLRIPDPHWLARPFVALPMAQL 136 Magnetococcus sp. MC-1
Q9Z7E8       86 KVVGRAEespPWSPRTIDVDILLYGdesFCCDHt-eITIPLSNLLSRPFLIALIASL 141 Chlamydophila pneumoniae
Q821E2       86 RRLGRDVnalPWSPRVLDIDILLYGd--ENHQQe-dVKIPHERITERPFLLSLIASL 139 Chlamydophila caviae
ZP_00210975  86 KKLGRISh-eRWAPRPIDIDIILWEn--TVLDLd-nLSIPHKQMHCRDFVLVPLCDI 138 Ehrlichia canis str. Jake
ZP_00187902  80 AALGREGk-gEKAPRTLDIDVLLFGe--ERLEHp-eLAVPHPGVVRAFNLRCLADLD 132 Rubrobacter xylanophilus DSM 9941
ZP_00039312 113 ERYGRDRavpRFGNRTLDVDVVFYGd--LIVKEpggEYCIPRRELKHSFVLKPLVDV 167 Xylella fastidiosa Dixon

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