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Conserved domains on  [gi|581249073|gb|EVM62677|]
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biotin-[acetyl-CoA-carboxylase] ligase [Staphylococcus aureus M0929]

Protein Classification

HTH_ARSR and BPL domain-containing protein( domain architecture ID 12089015)

HTH_ARSR and BPL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 86-321 1.15e-87

Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis


:

Pssm-ID: 440109 [Multi-domain]  Cd Length: 241  Bit Score: 262.80  E-value: 1.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  86 EVYDSIDSTQLAAKKSLV-GNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDA 164
Cdd:COG0340    3 EVFDEVDSTNDEAKELAReGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVAEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 165 IQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQlENFDESIRHRATSIQLHDKNKLDRYQF 244
Cdd:COG0340   83 LRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQP-PFDPEELDQPATSLKEETGKEVDREEL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581249073 245 LERLLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGESHRLISADI 321
Cdd:COG0340  162 LAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEV 238
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 6-58 4.77e-11

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


:

Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 57.06  E-value: 4.77e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 581249073    6 QDVLQLLYKNKPNyISGQSIAESLNISRTAVKKVIDQLKLEGCKIDSVNHKGH 58
Cdd:pfam08279   1 LQILQLLLEARGP-ISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
 
Name Accession Description Interval E-value
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 86-321 1.15e-87

Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440109 [Multi-domain]  Cd Length: 241  Bit Score: 262.80  E-value: 1.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  86 EVYDSIDSTQLAAKKSLV-GNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDA 164
Cdd:COG0340    3 EVFDEVDSTNDEAKELAReGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVAEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 165 IQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQlENFDESIRHRATSIQLHDKNKLDRYQF 244
Cdd:COG0340   83 LRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQP-PFDPEELDQPATSLKEETGKEVDREEL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581249073 245 LERLLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGESHRLISADI 321
Cdd:COG0340  162 LAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEV 238
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 86-259 6.37e-65

biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.


Pssm-ID: 319741 [Multi-domain]  Cd Length: 173  Bit Score: 202.11  E-value: 6.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  86 EVYDSIDSTQLAAKKSLV-GNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDA 164
Cdd:cd16442    3 IVLDEIDSTNDEAKELARsGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVAEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 165 IQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQLENFDESIrhraTSIQLHDKNKLDRYQF 244
Cdd:cd16442   83 LEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPLPD----TSLATSLGKEVDRNEL 158

                        170
                 ....*....|....*
gi 581249073 245 LERLLQEIEKRYNQF 259
Cdd:cd16442  159 LEELLAALENRLELF 173
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
19-312 1.37e-61

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 198.86  E-value: 1.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  19 YISGQSIAESLNISRTAVKKVIDQLKLEGCKIDSVNHKG-HLLQQLPdiwyqgIIDQYTKSSALFDFS-EVYDSIDSTQL 96
Cdd:PRK11886  18 FHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGyRLAEPLD------LLDPERISSQLPPGRvTVLPVIDSTNQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  97 AAKKSLVGNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDAIQHFSQDEVKVK 176
Cdd:PRK11886  92 YLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEALRRLGAIDVGLK 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 177 WPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQlENFDESIRHRATSIQLHDKNkLDRYQFLERLLQEIEKRY 256
Cdd:PRK11886 172 WPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMP-DFPEELIDQPWSDLQEAGPT-IDRNQLAAELIKQLRAAL 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 581249073 257 NQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGE 312
Cdd:PRK11886 250 ELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVE 305
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 87-321 7.46e-49

birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]


Pssm-ID: 272917 [Multi-domain]  Cd Length: 237  Bit Score: 163.34  E-value: 7.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073   87 VYDSIDSTQLAAK-KSLVGNQSSFFILSDEQTKGRGRFNRHWSSSKGqGLWMSVVLRPNVAFSMISKFNLFIALGIRDAI 165
Cdd:TIGR00121   4 VLDVIDSTNQYALeLAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG-GLYFSLILRPDLPKSPAPGLTLVAGIAIAEVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  166 QHFSqDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINltQQLENFDESIRHRATSIQLHDKNKLDRYQFL 245
Cdd:TIGR00121  83 KELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGIN--VQNRKPAESLREQAISLSEEAGIDLDRGELI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581249073  246 ERLLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGeSHRLISADI 321
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGG-IKKIISGEI 234
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 89-212 6.44e-14

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 organizm 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.


Pssm-ID: 427135  Cd Length: 132  Bit Score: 67.47  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073   89 DSIDSTQLAAKKSLVGN-QSSFFILSDEQTKGRGRFNRHWSSSKGqGLWMSVVL-------RPNVAFSMISKFNLFIALG 160
Cdd:pfam03099   3 ERIKSTNTYLEELNSSElESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLskehpnvDPSVLEFYVLELVLAVLEA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 581249073  161 IRDAIQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDgIEAIICGIGIN 212
Cdd:pfam03099  82 LGLYKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGT-LHHGVIGLGVN 132
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 6-58 4.77e-11

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 57.06  E-value: 4.77e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 581249073    6 QDVLQLLYKNKPNyISGQSIAESLNISRTAVKKVIDQLKLEGCKIDSVNHKGH 58
Cdd:pfam08279   1 LQILQLLLEARGP-ISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
 
Name Accession Description Interval E-value
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 86-321 1.15e-87

Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440109 [Multi-domain]  Cd Length: 241  Bit Score: 262.80  E-value: 1.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  86 EVYDSIDSTQLAAKKSLV-GNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDA 164
Cdd:COG0340    3 EVFDEVDSTNDEAKELAReGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVAEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 165 IQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQlENFDESIRHRATSIQLHDKNKLDRYQF 244
Cdd:COG0340   83 LRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQP-PFDPEELDQPATSLKEETGKEVDREEL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581249073 245 LERLLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGESHRLISADI 321
Cdd:COG0340  162 LAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEV 238
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 86-259 6.37e-65

biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.


Pssm-ID: 319741 [Multi-domain]  Cd Length: 173  Bit Score: 202.11  E-value: 6.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  86 EVYDSIDSTQLAAKKSLV-GNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDA 164
Cdd:cd16442    3 IVLDEIDSTNDEAKELARsGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVAEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 165 IQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQLENFDESIrhraTSIQLHDKNKLDRYQF 244
Cdd:cd16442   83 LEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPLPD----TSLATSLGKEVDRNEL 158

                        170
                 ....*....|....*
gi 581249073 245 LERLLQEIEKRYNQF 259
Cdd:cd16442  159 LEELLAALENRLELF 173
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
19-312 1.37e-61

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 198.86  E-value: 1.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  19 YISGQSIAESLNISRTAVKKVIDQLKLEGCKIDSVNHKG-HLLQQLPdiwyqgIIDQYTKSSALFDFS-EVYDSIDSTQL 96
Cdd:PRK11886  18 FHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGyRLAEPLD------LLDPERISSQLPPGRvTVLPVIDSTNQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  97 AAKKSLVGNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALGIRDAIQHFSQDEVKVK 176
Cdd:PRK11886  92 YLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEALRRLGAIDVGLK 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 177 WPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQlENFDESIRHRATSIQLHDKNkLDRYQFLERLLQEIEKRY 256
Cdd:PRK11886 172 WPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMP-DFPEELIDQPWSDLQEAGPT-IDRNQLAAELIKQLRAAL 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 581249073 257 NQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGE 312
Cdd:PRK11886 250 ELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVE 305
BirA COG1654
Biotin operon repressor [Transcription];
1-322 2.62e-56

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 185.19  E-value: 2.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073   1 MSKYSQDVLQLLYKNKpnYISGQSIAESLNISRTAVKKVIDQLKLEGCKIDSVNHKGHLLQQLPDIWYQGIIDQYTKSSA 80
Cdd:COG1654    2 MSSTRLKLLRLLADGE--FHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEEIRAGLSTKR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  81 LFDFSEVYDSIDSTQLAAKKSLVGNQSSFFILSDEQTKGRGRFNRHWSSSKGQGLWMSVVLRPNVAFSMISKFNLFIALG 160
Cdd:COG1654   80 LGREILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 161 IRDAIQHFSQDEVKV-KWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINLTQQLENFDESIRHRATSIQLHDKNKL 239
Cdd:COG1654  160 AVAAALAEGGGLVKWkKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 240 DRYQFLERLLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGESHRLISA 319
Cdd:COG1654  240 LRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSA 319


                 ...
gi 581249073 320 DID 322
Cdd:COG1654  320 VVV 322
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 84-252 6.68e-53

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: 172.34  E-value: 6.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  84 FSEVYDSID--STQLAAKKSL---VGNQSSFFILSDEQTKGRGRF--------------------------NRHWSSSKG 132
Cdd:cd16435    1 FVEVLDSVDyeSAWAAQEKSLrenVSNQSSTLLLWEHPTTVTLGRldrelphlelakkiergyelvvrnrgGRAVSHDPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 133 QgLWMSVVLRPNVAFsMISKFNLFIALGIRDAIQHFSQdEVKVKW-PNDIYIDNGKVCGFLTEMVANndgieAIICGIGI 211
Cdd:cd16435   81 Q-LVFSPVIGPNVEF-MISKFNLIIEEGIRDAIADFGQ-SAEVKWgRNDLWIDNRKVCGIAVRVVKE-----AIFHGIAL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 581249073 212 NLTQQLENFDESIRH-----RATSIQLHDKNKLDRYQFLERLLQEI 252
Cdd:cd16435  153 NLNQDLENFTEIIPCgykpeRVTSLSLELGRKVTVEQVLERVLAAF 198
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 87-321 7.46e-49

birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]


Pssm-ID: 272917 [Multi-domain]  Cd Length: 237  Bit Score: 163.34  E-value: 7.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073   87 VYDSIDSTQLAAK-KSLVGNQSSFFILSDEQTKGRGRFNRHWSSSKGqGLWMSVVLRPNVAFSMISKFNLFIALGIRDAI 165
Cdd:TIGR00121   4 VLDVIDSTNQYALeLAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG-GLYFSLILRPDLPKSPAPGLTLVAGIAIAEVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  166 QHFSqDEVKVKWPNDIYIDNGKVCGFLTEMVANNDGIEAIICGIGINltQQLENFDESIRHRATSIQLHDKNKLDRYQFL 245
Cdd:TIGR00121  83 KELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGIN--VQNRKPAESLREQAISLSEEAGIDLDRGELI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581249073  246 ERLLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGeSHRLISADI 321
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGG-IKKIISGEI 234
PRK08330 PRK08330
biotin--protein ligase; Provisional
 88-321 3.66e-36

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 130.25  E-value: 3.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  88 YDSIDSTQLAAKKSLVGNQSSFFILSDEQTKGRGRFNRHWSSSKGqGLWMSVVLRPNVAFSMISKFNLFIALGIRDAIQH 167
Cdd:PRK08330   8 FDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEG-GLWMSVILKPKVSPEHLPKLVFLGALAVVDTLRE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 168 FSQDeVKVKWPNDIYIDNGKVCGFLTEMVAnndgiEAIICGIGINLTQQLEnfdESIRHRATSIQLHDKNKLDRYQFLER 247
Cdd:PRK08330  87 FGIE-GKIKWPNDVLVNYKKIAGVLVEGKG-----DFVVLGIGLNVNNEIP---DELRETATSMKEVLGREVPLIEVFKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581249073 248 LLQEIEKRYNQFLTLPFSEIREEYIAASNIWNRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGESHRLISADI 321
Cdd:PRK08330 158 LVENLDRWYKLFLEGPGEILEEVKGRSMILGKRVKIIGDGEILVEGIAEDIDEFGALILRLDDGTVKKVLYGDV 231
PRK05935 PRK05935
biotin--protein ligase; Provisional
 90-269 2.52e-15

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 72.93  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  90 SIDSTQLAAKKSL-VGNQSSFFILS-DEQTKGRGRFNRHWSSSKGQglwmsvvLRPNVAFsMISKFNLFIALGIR---DA 164
Cdd:PRK05935  10 ETPSTNTTAKEGMhLWDPYALTVIStREQTAGKGKFGKSWHSSDQD-------LLASFCF-FITVLNIDVSLLFRlgtEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 165 IQHFSQD----EVKVKWPNDIYIDNGKVCGFLTEMVANNDGIeAIICGIGINLTQQLENFdESIRHRATSIQLHDKNKLD 240
Cdd:PRK05935  82 VMRLGEDlgitEAVIKWPNDVLVHGEKLCGVLCETIPVKGGL-GVILGIGVNGNTTKDEL-LGIDQPATSLQELLGHPID 159

                        170       180
                 ....*....|....*....|....*....
gi 581249073 241 RYQFLERLLQEIEKRYNQflTLPFSEIRE 269
Cdd:PRK05935 160 LEEQRERLIKHIKHVLIQ--TLPKLLARE 186
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 89-212 6.44e-14

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 organizm 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.


Pssm-ID: 427135  Cd Length: 132  Bit Score: 67.47  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073   89 DSIDSTQLAAKKSLVGN-QSSFFILSDEQTKGRGRFNRHWSSSKGqGLWMSVVL-------RPNVAFSMISKFNLFIALG 160
Cdd:pfam03099   3 ERIKSTNTYLEELNSSElESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLskehpnvDPSVLEFYVLELVLAVLEA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 581249073  161 IRDAIQHFSQDEVKVKWPNDIYIDNGKVCGFLTEMVANNDgIEAIICGIGIN 212
Cdd:pfam03099  82 LGLYKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGT-LHHGVIGLGVN 132
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
86-254 6.58e-13

biotin--[acetyl-CoA-carboxylase] ligase;


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 66.52  E-value: 6.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  86 EVYDSIDSTQLAAKKSLVGNQ--SSFFILSDEQTKGRGRFNRHWSSSKGqGLWMSVVLR----PN--------VAFSMIS 151
Cdd:PRK08477   4 RVFESLDSTQTYLIEKIKNGElkAPFAIVAKEQTAGIGSRGNSWEGKKG-NLFFSFALKesdlPKdlplqsssIYFGFLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 152 KfNLFIALGirdaiqhfsqDEVKVKWPNDIYIDNGKVCGFLTEMVANNdgieaIICGIGINLTQQLENFdesirhraTSI 231
Cdd:PRK08477  83 K-EVLKELG----------SKVWLKWPNDLYLDDKKIGGVITNKIKNF-----IVCGIGLNLKFSPKNF--------ACL 138

                        170       180
                 ....*....|....*....|...
gi 581249073 232 QLhdknKLDRYQFLERLLQEIEK 254
Cdd:PRK08477 139 DI----EISDDLLLEGFLQKIEK 157
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
115-213 1.55e-12

biotin--[acetyl-CoA-carboxylase] ligase;


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 67.11  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 115 EQTKGRGRFNRHWSSSKGQGLWMSVVL---RPNVAFSMISkfnLFIALGIRDAIQHFSQD---EVKVKWPNDIYIDNGKV 188
Cdd:PRK06955  72 EQTAGRGRQGRPWFAQPGNALLFSVACvlpRPVAALAGLS---LAVGVALAEALAALPAAlgqRIALKWPNDLLIAGRKL 148

                         90       100
                 ....*....|....*....|....*
gi 581249073 189 CGFLTEMVANNDGIEAIICGIGINL 213
Cdd:PRK06955 149 AGILIETVWATPDATAVVIGIGLNV 173
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 89-213 9.37e-12

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 64.12  E-value: 9.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  89 DSIDSTQLAAKKSLV-GNQSSFFILSDEQTKGRGRFNRHWSSSKGQgLWMSVVL-RPNVAFSMISKFNLFIALGIRDAIQ 166
Cdd:PTZ00276  13 GEVTSTMDVARTMLAaAGGKPFAVLAESQTAGRGTGGRTWTSPKGN-MYFTLCIpQKGVPPELVPVLPLITGLACRAAIM 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 581249073 167 HFSQDE-VKVKWPNDIYIDNGKVCGFLTEmvanNDGiEAIICGIGINL 213
Cdd:PTZ00276  92 EVLHGAaVHTKWPNDIIYAGKKIGGSLIE----SEG-EYLIIGIGMNI 134
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 6-58 4.77e-11

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 57.06  E-value: 4.77e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 581249073    6 QDVLQLLYKNKPNyISGQSIAESLNISRTAVKKVIDQLKLEGCKIDSVNHKGH 58
Cdd:pfam08279   1 LQILQLLLEARGP-ISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
116-323 2.13e-10

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 61.65  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 116 QTKGRGRFNRHWSSSKGQGLWMS---VVLRPNVAFSMISKFnlfIALGIRDAIQHFSQdEVKVKWPNDIYIDNGKVCGFL 192
Cdd:PRK13325 118 QSKGRGRQGRKWSHRLGECLMFSfgwVFDRPQYELGSLSPV---AAVACRRALSRLGL-KTQIKWPNDLVVGRDKLGGIL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 193 TEMVANNDGIEAIIcGIGIN--LTQQLENfdesirhrATSIQ-----LHDKNKLDRYQFLERLLQEIEKRYNQFLTLPFS 265
Cdd:PRK13325 194 IETVRTGGKTVAVV-GIGINfvLPKEVEN--------AASVQslfqtASRRGNADAAVLLETLLAELDAVLLQYARDGFA 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 581249073 266 EIREEYIAASNIWNR-TLLFTENDKQFKGQAIDLDYDGYLIVRDEAGEsHRLISADIDF 323
Cdd:PRK13325 265 PFVAEYQAANRDHGKaVLLLRDGETVFEGTVKGVDGQGVLHLETAEGK-QTVVSGEISL 322
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 88-312 2.71e-07

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 50.98  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073  88 YDSIDSTQLAAKKSL--------VGNQSSFFILSDEQTKGRG------RFNRHWSSSKGQgLWMSVVLRPNVafSMISKF 153
Cdd:PTZ00275  22 FDVLDSTQLYCKRNMkrfiqngkLQDDNMIIVSCNEQTNGIGtrdtkkNQDRIWLSEKGN-LFTTFVFLWNR--NDIEKV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 154 NLFI---ALGIRDAIQHFSQdEVKVKWPNDIYIDNGKVCGFLTEM------VANNDGIEAIICGIGINLTqqLENFDESI 224
Cdd:PTZ00275  99 KYLAqtcTVAISKTLEYFHL-VTQIKWINDVLVNYKKIAGCLVHLyylddfPNLNSRYVCVMVGIGINVT--LEDKHNLL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581249073 225 RHRATSIQLHDKNKLDRYQFLERLLQEIEKRYNQFlTLPFSEIREE-------YIAASNIW-NRTLLFTENDKQFKGQAI 296
Cdd:PTZ00275 176 NNNYTSIKKELQRDFNTPKSIPSVEQVTEKLIINL-KAVINKLRKEgfssfldYITPRLLYkDKKVLIDQDNELIVGYLQ 254

                        250
                 ....*....|....*.
gi 581249073 297 DLDYDGYLIVRDEAGE 312
Cdd:PTZ00275 255 GLLHDGSLLLLREKNK 270
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 279-323 8.49e-03

Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.


Pssm-ID: 426672 [Multi-domain]  Cd Length: 48  Bit Score: 33.97  E-value: 8.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 581249073  279 NRTLLFTENDKQFKGQAIDLDYDGYLIVRDEAGESHRLISADIDF 323
Cdd:pfam02237   3 GREVRVLLGDGIVEGIAVGIDDDGALLLETDDGTIRDINSGEVSL 47
 
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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