4WF2


Conserved Protein Domain Family
BPL_LplA_LipB

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pfam03099: BPL_LplA_LipB 
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Biotin/lipoate A/B protein ligase family
This family includes biotin protein ligase, lipoate-protein ligase A and B. 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. Each organism probably has only one BPL. 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) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.
Statistics
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PSSM-Id: 397288
Aligned: 18 rows
Threshold Bit Score: 83.2528
Threshold Setting Gi: 123074220
Created: 11-May-2020
Updated: 7-Aug-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:
4WF2_A  86 VI-DSTnq-----ylL--DRIGELKSGDACIAEYQQAGRgrrgRKWFSPFGaNLYLSMFWRLEQa---PAAAIGL--SLV 152 Escherichia coli K-12
Q1D4N3  51 AA-KRE---------NivASDAQLAKEGAEVFETNRGGD----VTYHGPGQ-LVGYPIFLLPED----RRDVRRY--VRD 109 Myxococcus xanthus DK...
O13476 135 RV-KKQitdeqiaryEgfIPSKQKYNKKPKFVQAERGGQ----VTFHGPGQ-IVAYIILDLkt---fqNLPAKCL--VST 203 Kluyveromyces lactis ...
Q06005 128 RI-KKTmtpdqiaayEsfIPETQKDNPRPKFVQVERGGQ----VTFHGPGQ-IVIYIILDLkt---fqSFPAKCL--VSC 196 Saccharomyces cerevis...
P39648  65 QDtRLP---------FlqDGISLLESEGYRVIVRNSGGL----AVVLD-DG-VLNISLIFEDEKkg--idIDKGYeaMVE 127 Bacillus subtilis sub...
O84287  50 FI-KPe-----------rFLKANWESLGVSAASRPTGGG----VTFHN--S-DYAFSLLVSSEHplyqDSILANYhtVNR 110 Chlamydia trachomatis
P54511  54 FQ-NIKk----------eINFEAVHKYNLGFVRRPTGGR----GVLHD--Q-ELTYSVIVSEEHpempATVTEAYrvISE 115 Bacillus subtilis sub...
Q9WZG7  46 FQ-KEd-----------gINVP----DWIDVVRRPSGGR----ALLHH--R-EITYCLAVPKKInfgkLSVLEFHrlVHS 102 Thermotoga maritima
Q9Y9E5  47 RQ-SVe-----------dVNLAEAEKRGYVLVRRPTGGA----ALLHPWER-EITYSLVLDSRHpyysLDVAESAatIAG 109 Aeropyrum pernix
O84730  10 RT-ESTnt-----taKegLSLWDPYALTVITTREQTAGRgkfgRVWHSTDQ-DLLASFCFFLSVnnvdSALLFRI--GTE 80  Chlamydia trachomatis
4WF2_A 153 IGIVMAEVL-------------------RKLGADKVRvk-wpNDLYLQDRKLAGILVELTGkTGDAAQIVIGAGIN 208 Escherichia coli K-12
Q1D4N3 110 VERSVMQVLaqwgi---------tagpiPKWPGVWIG-----AEGAPDARKIAAIGVHLSR-WLTTHGFALNVNTN 170 Myxococcus xanthus DK 1622
O13476 204 IDNAAMNALkvvpkfqgsdeplnlitqkTNDTGVWVS----------NQEKIASIGIHVRR-SVTSHGICINVDPD 268 Kluyveromyces lactis NRRL...
Q06005 197 IEQATIRTLkntkmcddtdkplnldamtTKDTGVWVEn---------GKKKVASVGIHVRR-SITSHGVAINVNTD 262 Saccharomyces cerevisiae ...
P39648 128 LMRRMLRPYnaki-------------eayEIEGSYCPg---sYDLSINGKKFAGISQRRVR-GGVAVQIYLCADKS 186 Bacillus subtilis subsp. ...
O84287 111 FVLKTINKLfglegsls----pievstdRAESSNFCVaktskYDVLIGNRKVGGAAQRSVK-QGFLHQGSIFLSGN 181 Chlamydia trachomatis
P54511 116 GILQGFRNLgldayfaip-rtekekeslKNPRSSVCFdapswYELVVEGRKVAGSAQTRQK-GVILQHGSILLDLD 189 Bacillus subtilis subsp. ...
Q9WZG7 103 LIRDALVEAglhae----------lsskRRGNTALCFdapsrYEIVINGVKVVGSAQFRTA-ESIVEHGSIVLKQD 167 Thermotoga maritima
Q9Y9E5 110 GVALALEELgiatrv-------ggytppPGVIGGLCYvrpgsSDVVVAGRKVSGSAQRRIG-GRLLQHGTLLLRFD 177 Aeropyrum pernix
O84730  81 AVMRLGESL--------------------GIQEAVMKw---pNDVLVQGKKLSGVLCETIP-VKTGTCVIIGIGVN 132 Chlamydia trachomatis
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