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Conserved domains on  [gi|117559169|gb|ABK36117|]
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biotin/lipoate A/B protein ligase family [Aeromonas hydrophila subsp. hydrophila ATCC 7966]

Protein Classification

lipoate--protein ligase family protein( domain architecture ID 46944)

lipoate--protein ligase family protein, similar to Staphylococcus aureus lipoate--protein ligase 1 and Saccharomyces cerevisiae octanoyltransferase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BPL_LplA_LipB super family cl14057
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 19-230 4.07e-29

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.


The actual alignment was detected with superfamily member cd16443:

Pssm-ID: 449326  Cd Length: 209  Bit Score: 108.50  E-value: 4.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  19 LAEEQRWLRECAHDRQPRAHLWQAPQCLIVTRKDARLPRYQAacEQLAAEGWPVHVRDSGGTAVPHGAGILNLSLMLPRT 98
Cdd:cd16443   15 LALDEALLRSVAAPPTLRLYLWQNPPTVVIGRFQNPLEEVNL--EYAEEDGIPVVRRPSGGGAVFHDLGNLNYSLILPKE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  99 TTDLAHYYRLLGAPLLSLLGEYGLAGsyDFVPGSFCDgqynLVIGGRKVTGTAQRWlapgqdHQGAVLAQAMLLVAGNVD 178
Cdd:cd16443   93 HPSIDESYRALSQPVIKALRKLGVEA--EFGGVGRND----LVVGGKKISGSAQRR------TKGRILHHGTLLVDVDLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 117559169 179 QGTRMASRFYE-LAGGELRFLPATSTTITQAINWQgsegELVERVRTRLTALL 230
Cdd:cd16443  161 KLARVLNVPYEkLKSKGPKSVRSRVTNLSELLGRD----ITVEEVKNALLEAF 209
 
Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 19-230 4.07e-29

lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.


Pssm-ID: 319742  Cd Length: 209  Bit Score: 108.50  E-value: 4.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  19 LAEEQRWLRECAHDRQPRAHLWQAPQCLIVTRKDARLPRYQAacEQLAAEGWPVHVRDSGGTAVPHGAGILNLSLMLPRT 98
Cdd:cd16443   15 LALDEALLRSVAAPPTLRLYLWQNPPTVVIGRFQNPLEEVNL--EYAEEDGIPVVRRPSGGGAVFHDLGNLNYSLILPKE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  99 TTDLAHYYRLLGAPLLSLLGEYGLAGsyDFVPGSFCDgqynLVIGGRKVTGTAQRWlapgqdHQGAVLAQAMLLVAGNVD 178
Cdd:cd16443   93 HPSIDESYRALSQPVIKALRKLGVEA--EFGGVGRND----LVVGGKKISGSAQRR------TKGRILHHGTLLVDVDLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 117559169 179 QGTRMASRFYE-LAGGELRFLPATSTTITQAINWQgsegELVERVRTRLTALL 230
Cdd:cd16443  161 KLARVLNVPYEkLKSKGPKSVRSRVTNLSELLGRD----ITVEEVKNALLEAF 209
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 12-189 3.24e-20

Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 439865  Cd Length: 246  Bit Score: 85.67  E-value: 3.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  12 SHTPDQILAEEQRWLRECAHDRQPRA-HLWQAPQCLIVTRKDARLPryQAACEQLAAEGWPVHVRDSGGTAVPHGAGILN 90
Cdd:COG0095    7 STDPAFNLALDEALLEEVAEGEDPPTlRLWRNPPTVVIGRFQNVLP--EVNLEYVEEHGIPVVRRISGGGAVYHDPGNLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  91 LSLMLPRT--TTDLAHYYRLLGAPLLSLLGEYGLAGSYdfvpgsfcDGQYNLVIGGRKVTGTAQRWLapgqdhQGAVLAQ 168
Cdd:COG0095   85 YSLILPEDdvPLSIEESYRKLLEPILEALRKLGVDAEF--------SGRNDIVVDGRKISGNAQRRR------KGAVLHH 150

                        170       180
                 ....*....|....*....|.
gi 117559169 169 AMLLVAGNVDQGTRMASRFYE 189
Cdd:COG0095  151 GTLLVDGDLEKLAKVLRVPYE 171
 
Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 19-230 4.07e-29

lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.


Pssm-ID: 319742  Cd Length: 209  Bit Score: 108.50  E-value: 4.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  19 LAEEQRWLRECAHDRQPRAHLWQAPQCLIVTRKDARLPRYQAacEQLAAEGWPVHVRDSGGTAVPHGAGILNLSLMLPRT 98
Cdd:cd16443   15 LALDEALLRSVAAPPTLRLYLWQNPPTVVIGRFQNPLEEVNL--EYAEEDGIPVVRRPSGGGAVFHDLGNLNYSLILPKE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  99 TTDLAHYYRLLGAPLLSLLGEYGLAGsyDFVPGSFCDgqynLVIGGRKVTGTAQRWlapgqdHQGAVLAQAMLLVAGNVD 178
Cdd:cd16443   93 HPSIDESYRALSQPVIKALRKLGVEA--EFGGVGRND----LVVGGKKISGSAQRR------TKGRILHHGTLLVDVDLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 117559169 179 QGTRMASRFYE-LAGGELRFLPATSTTITQAINWQgsegELVERVRTRLTALL 230
Cdd:cd16443  161 KLARVLNVPYEkLKSKGPKSVRSRVTNLSELLGRD----ITVEEVKNALLEAF 209
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 12-189 3.24e-20

Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 439865  Cd Length: 246  Bit Score: 85.67  E-value: 3.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  12 SHTPDQILAEEQRWLRECAHDRQPRA-HLWQAPQCLIVTRKDARLPryQAACEQLAAEGWPVHVRDSGGTAVPHGAGILN 90
Cdd:COG0095    7 STDPAFNLALDEALLEEVAEGEDPPTlRLWRNPPTVVIGRFQNVLP--EVNLEYVEEHGIPVVRRISGGGAVYHDPGNLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  91 LSLMLPRT--TTDLAHYYRLLGAPLLSLLGEYGLAGSYdfvpgsfcDGQYNLVIGGRKVTGTAQRWLapgqdhQGAVLAQ 168
Cdd:COG0095   85 YSLILPEDdvPLSIEESYRKLLEPILEALRKLGVDAEF--------SGRNDIVVDGRKISGNAQRRR------KGAVLHH 150

                        170       180
                 ....*....|....*....|.
gi 117559169 169 AMLLVAGNVDQGTRMASRFYE 189
Cdd:COG0095  151 GTLLVDGDLEKLAKVLRVPYE 171
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 19-166 3.07e-09

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.


Pssm-ID: 319740  Cd Length: 198  Bit Score: 54.85  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117559169  19 LAEEQRWLRECAHDRQPRAHLWQAPQCLIVTRKDARLPRYQAacEQLAAEGWPVHVRDSGGTAVPHGAGILNLSLMLPR- 97
Cdd:cd16435   14 WAAQEKSLRENVSNQSSTLLLWEHPTTVTLGRLDRELPHLEL--AKKIERGYELVVRNRGGRAVSHDPGQLVFSPVIGPn 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117559169  98 TTTDLAHYYRLLGAPLLSLLGEYGlagsydfVPGSFCDGQYNLVIGGRKVTGTAQRWLAPGQDHQGAVL 166
Cdd:cd16435   92 VEFMISKFNLIIEEGIRDAIADFG-------QSAEVKWGRNDLWIDNRKVCGIAVRVVKEAIFHGIALN 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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