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Conserved domains on  [gi|446577284|ref|WP_000654630|]
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MULTISPECIES: bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA [Enterobacteriaceae]

Protein Classification

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA( domain architecture ID 11485649)

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor, forming a BirA-biotinyl-5'-adenylate complex that can either transfer the biotinyl moiety to the BCCP subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon

CATH:  1.10.10.10
EC:  6.3.4.15
Gene Symbol:  birA
Gene Ontology:  GO:0005524|GO:0004077|GO:0003677|GO:0006355
PubMed:  3899863
SCOP:  4000146

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
2-320 0e+00

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


:

Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 560.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   2 KDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  82 AVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 162 RKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAM 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446577284 242 LIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
 
Name Accession Description Interval E-value
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
2-320 0e+00

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 560.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   2 KDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  82 AVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 162 RKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAM 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446577284 242 LIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 80-317 2.73e-108

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: 315.11  E-value: 2.73e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   80 SVAVLPVIDSTNQYLLDRIGELK-SGDACIAEYQQAGRGRRGRKWFSPFGAnLYLSMFWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:TIGR00121   1 EVIVLDVIDSTNQYALELAKEGKlKGDLVVAEYQTAGRGRRGRKWLSPEGG-LYFSLILRPDLPKSPAPGLTLVAGIAIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  159 EVLRKLGaDKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTL 238
Cdd:TIGR00121  80 EVLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGEL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446577284  239 AAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLR 317
Cdd:TIGR00121 159 IEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 80-317 3.19e-97

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: 287.07  E-value: 3.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  80 SVAVLPVIDSTNQYLLDRIGE-LKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 159 EVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITL-QEAGINLDRNT 237
Cdd:COG0340   81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 238 LAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQ-DGIIKPWMGGEISL 316
Cdd:COG0340  161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240


                 .
gi 446577284 317 R 317
Cdd:COG0340  241 R 241
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 81-253 3.94e-61

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: 192.48  E-value: 3.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  81 VAVLPVIDSTNQYLLDRIGEL-KSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAE 159
Cdd:cd16442    2 LIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 160 VLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVvnQGWITLQEAGINLDRNTLA 239
Cdd:cd16442   82 ALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPL--PDTSLATSLGKEVDRNELL 159

                        170
                 ....*....|....
gi 446577284 240 AMLIRELRAALELF 253
Cdd:cd16442  160 EELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 83-208 1.02e-31

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: 115.23  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   83 VLPVIDSTNQYLL-DRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGaNLYLSMFWRLEQG---PAAAIGLSLVIGIVMA 158
Cdd:pfam03099   1 LGERIKSTNTYLEeLNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446577284  159 EVL----RKLGADKVRVKWPNDLYLQDRKLAGILVELTgKTGDAAQIVIGAGIN 208
Cdd:pfam03099  80 EALglykPGISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
HTH_metalloreg NF033788
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ...
 8-48 1.02e-03

metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense toxic heavy metals such as arsenic or cadmium, and are released from DNA so that resistance factors will be expressed, include ArsR, SmtB, ZiaR, CadC, CadX, KmtR, etc. However, some members of this family, including the sporulation delaying system autorepressor SdpR and its family (see NF033789), may lack metal-binding cites and instead regulate other cellular processes.


Pssm-ID: 411368 [Multi-domain]  Cd Length: 76  Bit Score: 37.05  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446577284   8 LKLIALLANGEFHSGEqLGETLGMSRAAINKHIQTLRDWGV 48
Cdd:NF033788  14 LRILELLAEGELCVCE-LAEALGLSQSAVSQHLKVLRDAGL 53
 
Name Accession Description Interval E-value
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
2-320 0e+00

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 560.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   2 KDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  82 AVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 162 RKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAM 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446577284 242 LIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 80-317 2.73e-108

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: 315.11  E-value: 2.73e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   80 SVAVLPVIDSTNQYLLDRIGELK-SGDACIAEYQQAGRGRRGRKWFSPFGAnLYLSMFWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:TIGR00121   1 EVIVLDVIDSTNQYALELAKEGKlKGDLVVAEYQTAGRGRRGRKWLSPEGG-LYFSLILRPDLPKSPAPGLTLVAGIAIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  159 EVLRKLGaDKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTL 238
Cdd:TIGR00121  80 EVLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGEL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446577284  239 AAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLR 317
Cdd:TIGR00121 159 IEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 80-317 3.19e-97

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: 287.07  E-value: 3.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  80 SVAVLPVIDSTNQYLLDRIGE-LKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 159 EVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITL-QEAGINLDRNT 237
Cdd:COG0340   81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 238 LAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQ-DGIIKPWMGGEISL 316
Cdd:COG0340  161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240


                 .
gi 446577284 317 R 317
Cdd:COG0340  241 R 241
BirA COG1654
Biotin operon repressor [Transcription];
3-320 4.52e-78

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 241.04  E-value: 4.52e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   3 DNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSVA 82
Cdd:COG1654    2 MSSTRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEEIRAGLSTKRLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  83 --VLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEV 160
Cdd:COG1654   82 reILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAVAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 161 LRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAA 240
Cdd:COG1654  162 AAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLLR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 241 MLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAE 320
Cdd:COG1654  242 LLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSAVV 321
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 81-253 3.94e-61

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: 192.48  E-value: 3.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  81 VAVLPVIDSTNQYLLDRIGEL-KSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAE 159
Cdd:cd16442    2 LIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 160 VLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVvnQGWITLQEAGINLDRNTLA 239
Cdd:cd16442   82 ALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPL--PDTSLATSLGKEVDRNELL 159

                        170
                 ....*....|....
gi 446577284 240 AMLIRELRAALELF 253
Cdd:cd16442  160 EELLAALENRLELF 173
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
108-320 2.32e-42

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 148.39  E-value: 2.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 108 IAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKL---GADKVRVKWPNDLYLQDRKL 184
Cdd:PRK06955  69 VAYEQTAGRGRQGRPWFAQPGNALLFSVACVLPRPVAALAGLSLAVGVALAEALAALpaaLGQRIALKWPNDLLIAGRKL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 185 AGILVELTGKTGDAAQIVIGAGINmaMRRVEESVVNQGWITLQEA----------------GINLDRnTLAAMLIReLRA 248
Cdd:PRK06955 149 AGILIETVWATPDATAVVIGIGLN--VRRADAVAAEVDALRAREAalarglppvalaaacaGANLTD-TLAAALNA-LAP 224

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446577284 249 ALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIF-GISRGIDKQGALLLEQDGIIKPWMGGEISLRSAE 320
Cdd:PRK06955 225 ALQAFGADGLAPFAARWHALHAYAGREVVLLEDGAELArGVAHGIDETGQLLLDTPAGRQAIAAGDVSLREAD 297
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 83-208 1.02e-31

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: 115.23  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   83 VLPVIDSTNQYLL-DRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGaNLYLSMFWRLEQG---PAAAIGLSLVIGIVMA 158
Cdd:pfam03099   1 LGERIKSTNTYLEeLNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446577284  159 EVL----RKLGADKVRVKWPNDLYLQDRKLAGILVELTgKTGDAAQIVIGAGIN 208
Cdd:pfam03099  80 EALglykPGISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
birA_repr_reg TIGR00122
BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix ...
 6-76 3.80e-27

BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix repressor region of the biotin--acetyl-CoA-carboxylase ligase/biotin operon repressor bifunctional protein BirA. In many species, the biotin--acetyl-CoA-carboxylase ligase ortholog lacks this DNA-binding repressor region and therefore is not equivalent to the well-characterized BirA of E. coli. This model may recognize some other putative repressor proteins, such as DnrO of Streptomyces peucetius with scores below the noise cutoff but with significance shown by low E-value. [Regulatory functions, DNA interactions]


Pssm-ID: 272918 [Multi-domain]  Cd Length: 69  Bit Score: 101.39  E-value: 3.80e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446577284    6 VPLKLIALLANGEFHsGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVpGKGYSLPEPIQLLNAKQILGQL 76
Cdd:TIGR00122   1 MPLRLLALLADNPFS-GEKLGEALGMSRTAVNKHIQTLREWGVDVLTV-GKGYRLPPPIPLLNAKQIRGQL 69
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
9-317 3.60e-26

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 108.64  E-value: 3.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284   9 KLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQI--LGQLDGGSVAVLPV 86
Cdd:PRK13325  10 RVLAELADGLPQHVSQLARMADMKPQQLNGFWQQMPAHIRGLLRQHDGYWRLVRPLAVFDAEGLreLGERSGFQTALKHE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  87 IDSTNQYLLD--RIGELKSGDA-CIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRK 163
Cdd:PRK13325  90 CASSNDEILElaRIAPDKAHKTiCVTHLQSKGRGRQGRKWSHRLGECLMFSFGWVFDRPQYELGSLSPVAAVACRRALSR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 164 LGADkVRVKWPNDLYLQDRKLAGILVElTGKTGDAAQIVIGAGINMAM-RRVEESVVNQGWITLQEAGINLDRNTLAAML 242
Cdd:PRK13325 170 LGLK-TQIKWPNDLVVGRDKLGGILIE-TVRTGGKTVAVVGIGINFVLpKEVENAASVQSLFQTASRRGNADAAVLLETL 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446577284 243 IRELRAALELFEQEGLAPYLSRWEKLDNFINRPVkLIIGDKEIF--GISRGIDKQGALLLEQDGIIKPWMGGEISLR 317
Cdd:PRK13325 248 LAELDAVLLQYARDGFAPFVAEYQAANRDHGKAV-LLLRDGETVfeGTVKGVDGQGVLHLETAEGKQTVVSGEISLR 323
PRK08330 PRK08330
biotin--protein ligase; Provisional
 87-317 2.37e-23

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 95.97  E-value: 2.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  87 IDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGAnLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGA 166
Cdd:PRK08330  11 VDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGG-LWMSVILKPKVSPEHLPKLVFLGALAVVDTLREFGI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 167 DKvRVKWPNDLYLQDRKLAGILVELTGKtgdaaQIVIGAGINMAmRRVEESVVNQGWITLQEAGINLDRNTLAAMLIREL 246
Cdd:PRK08330  90 EG-KIKWPNDVLVNYKKIAGVLVEGKGD-----FVVLGIGLNVN-NEIPDELRETATSMKEVLGREVPLIEVFKRLVENL 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446577284 247 RAALELFeQEGLAPYLSRWEKLDNFINRPVKlIIGDKEIF--GISRGIDKQGALLLE-QDGIIKPWMGGEISLR 317
Cdd:PRK08330 163 DRWYKLF-LEGPGEILEEVKGRSMILGKRVK-IIGDGEILveGIAEDIDEFGALILRlDDGTVKKVLYGDVSLR 234
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
87-272 2.93e-17

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 78.84  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284  87 IDSTNQYLLDRI--GELKSGDACIAEYQQAGRGRRGRKWFSPFGaNLYLSMFWRLEQGP-----AAAiglSLVIGIVMAE 159
Cdd:PRK08477   9 LDSTQTYLIEKIknGELKAPFAIVAKEQTAGIGSRGNSWEGKKG-NLFFSFALKESDLPkdlplQSS---SIYFGFLLKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 160 VLRKLGAdKVRVKWPNDLYLQDRKLAGIlveLTGKTGDaaQIVIGAGINMAMrrveesvVNQGWITLQeagINLDRNTLA 239
Cdd:PRK08477  85 VLKELGS-KVWLKWPNDLYLDDKKIGGV---ITNKIKN--FIVCGIGLNLKF-------SPKNFACLD---IEISDDLLL 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446577284 240 AMLIRELRaaLELFEQEGLAPYLSRWEKLDNFI 272
Cdd:PRK08477 149 EGFLQKIE--KKILWKQIFSKYKLEFEKSKSFS 179
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 106-211 2.72e-13

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 68.35  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 106 ACIAEYQQAGRGRRGRKWFSPFGaNLYLSM-FWRLEQGPAAAIGLSLVIGIV-MAEVLRKLGADKVRVKWPNDLYLQDRK 183
Cdd:PTZ00276  35 AVLAESQTAGRGTGGRTWTSPKG-NMYFTLcIPQKGVPPELVPVLPLITGLAcRAAIMEVLHGAAVHTKWPNDIIYAGKK 113

                         90       100
                 ....*....|....*....|....*...
gi 446577284 184 LAGILVEltgktGDAAQIVIGAGINMAM 211
Cdd:PTZ00276 114 IGGSLIE-----SEGEYLIIGIGMNIEV 136
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 10-58 1.13e-10

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: 56.29  E-value: 1.13e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446577284   10 LIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGY 58
Cdd:pfam08279   4 LQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 271-317 1.85e-10

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: 55.55  E-value: 1.85e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446577284  271 FINRPVKLIIGDKEIFGISRGIDKQGALLLEQ-DGIIKPWMGGEISLR 317
Cdd:pfam02237   1 TLGREVRVLLGDGIVEGIAVGIDDDGALLLETdDGTIRDINSGEVSLR 48
PRK05935 PRK05935
biotin--protein ligase; Provisional
 112-250 1.32e-07

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 50.97  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446577284 112 QQAGRGRRGRKWFSPFGaNLYLSMFWRLEQgpaAAIGLSLVIGIVMAEVLR---KLGADKVRVKWPNDLYLQDRKLAGIL 188
Cdd:PRK05935  38 QTAGKGKFGKSWHSSDQ-DLLASFCFFITV---LNIDVSLLFRLGTEAVMRlgeDLGITEAVIKWPNDVLVHGEKLCGVL 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446577284 189 VE---LTGKTGdaaqIVIGAGINMAMRRVEESVVNQGWITLQE-AGINLDRNTLAAMLIRELRAAL 250
Cdd:PRK05935 114 CEtipVKGGLG----VILGIGVNGNTTKDELLGIDQPATSLQElLGHPIDLEEQRERLIKHIKHVL 175
YobV COG2378
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ...
 8-73 2.89e-05

Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];


Pssm-ID: 441945 [Multi-domain]  Cd Length: 314  Bit Score: 45.07  E-value: 2.89e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446577284   8 LKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGK--GYSLPE----PIQLLNAKQIL 73
Cdd:COG2378    8 LALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELGVPIEAERGRggGYRLRDgyrlPPLMLTEEEAL 79
ArsR COG0640
DNA-binding transcriptional regulator, ArsR family [Transcription];
8-48 9.81e-04

DNA-binding transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 440405 [Multi-domain]  Cd Length: 92  Bit Score: 37.56  E-value: 9.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446577284   8 LKLIALLANGEFHSGEqLGETLGMSRAAINKHIQTLRDWGV 48
Cdd:COG0640   23 LRILRLLAEGELCVGE-LAEALGLSQSTVSHHLKVLREAGL 62
HTH_metalloreg NF033788
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ...
 8-48 1.02e-03

metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense toxic heavy metals such as arsenic or cadmium, and are released from DNA so that resistance factors will be expressed, include ArsR, SmtB, ZiaR, CadC, CadX, KmtR, etc. However, some members of this family, including the sporulation delaying system autorepressor SdpR and its family (see NF033789), may lack metal-binding cites and instead regulate other cellular processes.


Pssm-ID: 411368 [Multi-domain]  Cd Length: 76  Bit Score: 37.05  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446577284   8 LKLIALLANGEFHSGEqLGETLGMSRAAINKHIQTLRDWGV 48
Cdd:NF033788  14 LRILELLAEGELCVCE-LAEALGLSQSAVSQHLKVLRDAGL 53
GbsR COG1510
DNA-binding transcriptional regulator GbsR, MarR family [Transcription];
12-55 2.08e-03

DNA-binding transcriptional regulator GbsR, MarR family [Transcription];


Pssm-ID: 441119  Cd Length: 164  Bit Score: 38.38  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446577284  12 ALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWG-VDVFTVPG 55
Cdd:COG1510   35 LLYLSDEPLTADELAEELGVSKSSVSTALRELEDWGlVRRVRKPG 79
COG1777 COG1777
Predicted transcriptional regulator, ArsR family [Transcription];
4-47 7.16e-03

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441383  Cd Length: 113  Bit Score: 35.78  E-value: 7.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446577284   4 NTVPLKLIALLANGEfHSGEQLGETLGMSRAAINKHIQTLRDWG 47
Cdd:COG1777   16 NPTRRRILALLSEEP-AYVSELARELGVSRQAVYKHLRKLEEAG 58
 
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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