3A7R,3RIR,1W66,2P0L,2QHT


Conserved Protein Domain Family
BPL_LplA_LipB

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cd16435: BPL_LplA_LipB 
Click on image for an interactive view with Cn3D
biotin-lipoate ligase family
This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.
Statistics
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PSSM-Id: 319740
Aligned: 5 rows
Threshold Bit Score: 172.722
Created: 28-Mar-2013
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitecatalytic site
Conserved site includes 25 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:3A7R: Escherichia coli lipoate-protein ligase A with bound lipoyl-AMP; contacts at 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                    ##                     #     ####                              ##
3A7R_A      4 RLLISDSydp---wfNLAVEECIFrqmp--atqRVLFLWRNadTVVIGraqnpwkecntrrm--eednvrlarrssggGA 76  Escherichia coli K-12
3RIR_A     84 FSEVYDSid-----sTQLAAKKSLvgn----qsSFFILSDEqtKGRGRf----------------------------nRH 126 Staphylococcus aur...
1W66_A     15 DVRQLGTvdy---rtAWQLQRELAdarv-aggaDTLLLLEHpaVYTAGrrtetherpid--------gtpvvdtdrggKI 82  Mycobacterium tube...
2P0L_A     14 SIFKDYVtdaqdaekPFIWTEVFLreinrsnqeIILHIWPXtkTVILGxldrelphlelakkeiisrgyepvvrnfggLA 93  Streptococcus agal...
2QHT_A      4 LVEDLGLvpy---geAWAYQKRVHrevvagnrpPTLLLLEHprVITLGrkatgenllfpeswy-rengfelywverggDV 79  Thermus thermophil...
Feature 1     ###      ###                                                 ##          #  ### 
3A7R_A     77 VFHDl-gNTCFTFMAgkp-------eydKTISTSIVLNALNALgv-sAEASG--------RNDLVVktvegDRKVSGSAY 139 Escherichia coli K-12
3RIR_A    127 WSSSkgqGLWMSVVLrpnvaf-smiskfNLFIALGIRDAIQHFsqdeVKVKW--------PNDIYId----NGKVCGFLT 193 Staphylococcus aur...
1W66_A     83 TWHGp-gQLVGYPIIglaepl--dvvnyVRRLEESLIQVCADLgl-hAGRVDg-------RSGVWLpg-rpARKVAAIGV 150 Mycobacterium tube...
2P0L_A     94 VVADe-gILNFSLVIpdvferklsisdgYLIXVDFIRSIFSDFyq-pIEHFEvetsycpgKFDLSIn----GKKFAGLAQ 167 Streptococcus agal...
2QHT_A     80 TYHGp-gQLVGYPIFpvgre----vrrfLRQIEEAIVRVAAGYgi-sAYPTPg-------YAGVWVg----EDKLCAIGV 142 Thermus thermophil...
Feature 1                   ### #                                                             
3A7R_A    140 REtk-----drGFHHGTLLLnadlsrlanylnpdkkklaa-------kgitsvrsrvtnltellpgiTHEQVCEAITEAF 207 Escherichia coli K-12
3RIR_A    194 EMvanndgieaIICGIGINLtqqlenfdesirh---------------------ratsiqlhdknklDRYQFLERLLQEI 252 Staphylococcus aur...
1W66_A    151 RVsr-----atTLHGFALNCdcdlaaftaivpcgis----------------daavtslsaelgrtvTVDEVRATVAAAV 209 Mycobacterium tube...
2P0L_A    168 RRik-----ngIAVSIYLSVcgdqkgrsqxisdfykiglgdtgspiaypnvdpeixanlsdlldcpxTVEDVIDRXLISL 242 Streptococcus agal...
2QHT_A    143 AVke-----gvSFHGFALNVntdlndftvivpcglk----------------gkgvtslekllgrkvPMEEAKARVVAAF 201 Thermus thermophil...

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