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Conserved domains on  [gi|695753858|ref|WP_032680102|]
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MULTISPECIES: bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA [Enterobacter]

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: 573.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   2 KDNTIPLTLISILADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNEELIRSQVEHGNV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  82 AVLPVIDSTNQYLMDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 162 HDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNLQEAGITIDRNTLAVR 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695753858 242 MIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLRSAE 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: 573.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   2 KDNTIPLTLISILADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNEELIRSQVEHGNV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  82 AVLPVIDSTNQYLMDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 162 HDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNLQEAGITIDRNTLAVR 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695753858 242 MIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 81-317 2.59e-99

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: 292.00  E-value: 2.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   81 VAVLPVIDSTNQYLMDRLSEL-SSGDACVAEYQQAGRGRRGRKWFSPFGAnLYLSMYWRLEQGPAAAVGLSLVIGIVMAE 159
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGG-LYFSLILRPDLPKSPAPGLTLVAGIAIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  160 VLHDLGaDKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNLQEAGITIDRNTLA 239
Cdd:TIGR00121  81 VLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGELI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695753858  240 VRMIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLR 317
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 80-317 4.19e-98

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: 289.00  E-value: 4.19e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  80 NVAVLPVIDSTNQYLMDRLSE-LSSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMA 158
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 159 EVLHDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNL-QEAGITIDRNT 237
Cdd:COG0340   81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 238 LAVRMIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQ-DGVIKPWVGGEISL 316
Cdd:COG0340  161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240


                 .
gi 695753858 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 ...
 80-253 4.27e-58

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: 184.77  E-value: 4.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  80 NVAVLPVIDSTNQYLMDRLSELS-SGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMA 158
Cdd:cd16442    1 KLIVLDEIDSTNDEAKELARSGApEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 159 EVLHDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWtnLQEAGITIDRNTL 238
Cdd:cd16442   81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPLPDTSL--ATSLGKEVDRNEL 158

                        170
                 ....*....|....*
gi 695753858 239 AVRMIKELRSSLSLF 253
Cdd:cd16442  159 LEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 83-208 2.26e-29

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: 109.07  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   83 VLPVIDSTNQYL-MDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGaNLYLSMYWRLEQG---PAAAVGLSLVIGIVMA 158
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 695753858  159 EVLHD----LGADKVRVKWPNDLYLNDRKLAGILVELTgKTGDAAQIVIGAGLN 208
Cdd:pfam03099  80 EALGLykpgISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
HTH_metalloreg NF033788
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ...
 8-48 6.78e-04

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: 37.82  E-value: 6.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 695753858   8 LTLISILADGEFHSGEqLGEHLGMSRAAINKHIQTLRDWGV 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: 573.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   2 KDNTIPLTLISILADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNEELIRSQVEHGNV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  82 AVLPVIDSTNQYLMDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 162 HDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNLQEAGITIDRNTLAVR 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695753858 242 MIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 81-317 2.59e-99

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: 292.00  E-value: 2.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   81 VAVLPVIDSTNQYLMDRLSEL-SSGDACVAEYQQAGRGRRGRKWFSPFGAnLYLSMYWRLEQGPAAAVGLSLVIGIVMAE 159
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGG-LYFSLILRPDLPKSPAPGLTLVAGIAIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  160 VLHDLGaDKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNLQEAGITIDRNTLA 239
Cdd:TIGR00121  81 VLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGELI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695753858  240 VRMIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLR 317
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 80-317 4.19e-98

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: 289.00  E-value: 4.19e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  80 NVAVLPVIDSTNQYLMDRLSE-LSSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMA 158
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 159 EVLHDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNL-QEAGITIDRNT 237
Cdd:COG0340   81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 238 LAVRMIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQ-DGVIKPWVGGEISL 316
Cdd:COG0340  161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240


                 .
gi 695753858 317 R 317
Cdd:COG0340  241 R 241
BirA COG1654
Biotin operon repressor [Transcription];
3-320 4.69e-81

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 248.75  E-value: 4.69e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   3 DNTIPLTLISILADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNEELIRSQVEHGNVA 82
Cdd:COG1654    2 MSSTRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEEIRAGLSTKRLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  83 --VLPVIDSTNQYLMDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMAEV 160
Cdd:COG1654   82 reILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAVAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 161 LHDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWTNLQEAGITIDRNTLAV 240
Cdd:COG1654  162 AAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLLR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 241 RMIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLRSAE 320
Cdd:COG1654  242 LLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSAVV 321
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 80-253 4.27e-58

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: 184.77  E-value: 4.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  80 NVAVLPVIDSTNQYLMDRLSELS-SGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMA 158
Cdd:cd16442    1 KLIVLDEIDSTNDEAKELARSGApEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 159 EVLHDLGADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMVMRNVQNDVVNQAWtnLQEAGITIDRNTL 238
Cdd:cd16442   81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPLPDTSL--ATSLGKEVDRNEL 158

                        170
                 ....*....|....*
gi 695753858 239 AVRMIKELRSSLSLF 253
Cdd:cd16442  159 LEELLAALENRLELF 173
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
89-320 5.06e-43

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 149.93  E-value: 5.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  89 STNQYLMDRLSELSSGDAC-------VAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMAEVL 161
Cdd:PRK06955  43 STNADLMARLKALPRSADAlpapivrVAYEQTAGRGRQGRPWFAQPGNALLFSVACVLPRPVAALAGLSLAVGVALAEAL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 162 HDL---GADKVRVKWPNDLYLNDRKLAGILVELTGKTGDAAQIVIGAGLNMV---MRNVQNDVVNQ---------AWTNL 226
Cdd:PRK06955 123 AALpaaLGQRIALKWPNDLLIAGRKLAGILIETVWATPDATAVVIGIGLNVRradAVAAEVDALRAreaalarglPPVAL 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 227 QEAGITIDRNTLAVRMIKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLIGDKEIY-GISRGIDAQGALLLEQDGV 305
Cdd:PRK06955 203 AAACAGANLTDTLAAALNALAPALQAFGADGLAPFAARWHALHAYAGREVVLLEDGAELArGVAHGIDETGQLLLDTPAG 282

                        250
                 ....*....|....*
gi 695753858 306 IKPWVGGEISLRSAE 320
Cdd:PRK06955 283 RQAIAAGDVSLREAD 297
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 83-208 2.26e-29

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: 109.07  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858   83 VLPVIDSTNQYL-MDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGaNLYLSMYWRLEQG---PAAAVGLSLVIGIVMA 158
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 695753858  159 EVLHD----LGADKVRVKWPNDLYLNDRKLAGILVELTgKTGDAAQIVIGAGLN 208
Cdd:pfam03099  80 EALGLykpgISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
PRK08330 PRK08330
biotin--protein ligase; Provisional
 80-317 1.33e-28

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 110.22  E-value: 1.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  80 NVAVLPVIDSTNQYLMDRLSELSSGDACVAEYQQAGRGRRGRKWFSPFGAnLYLSMYWRLEQGPAAAVGLSLVIGIVMAE 159
Cdd:PRK08330   4 NIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGG-LWMSVILKPKVSPEHLPKLVFLGALAVVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 160 VLHDLGADKvRVKWPNDLYLNDRKLAGILVELTGKtgdaaQIVIGAGLNmVMRNVQNDVVNQAWTNLQEAGITIDRNTLA 239
Cdd:PRK08330  83 TLREFGIEG-KIKWPNDVLVNYKKIAGVLVEGKGD-----FVVLGIGLN-VNNEIPDELRETATSMKEVLGREVPLIEVF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 240 VRMIKELRSSLSLFeQEGLASFLSRWEKLDNFINRPVKLLIGDKEI-YGISRGIDAQGALLLE-QDGVIKPWVGGEISLR 317
Cdd:PRK08330 156 KRLVENLDRWYKLF-LEGPGEILEEVKGRSMILGKRVKIIGDGEILvEGIAEDIDEFGALILRlDDGTVKKVLYGDVSLR 234
birA_repr_reg TIGR00122
BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix ...
 7-75 1.96e-25

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: 96.76  E-value: 1.96e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695753858    7 PLTLISILADGEFHsGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVpGKGYSLPEPIQLLNEELIRSQ 75
Cdd:TIGR00122   2 PLRLLALLADNPFS-GEKLGEALGMSRTAVNKHIQTLREWGVDVLTV-GKGYRLPPPIPLLNAKQIRGQ 68
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
10-317 2.98e-23

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 100.17  E-value: 2.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  10 LISILADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNEELIRSQVEHG--NVAVLPVI 87
Cdd:PRK13325  11 VLAELADGLPQHVSQLARMADMKPQQLNGFWQQMPAHIRGLLRQHDGYWRLVRPLAVFDAEGLRELGERSgfQTALKHEC 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  88 DSTNQYLMDrLSELSSGDA----CVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAVGLSLVIGIVMAEVLHD 163
Cdd:PRK13325  91 ASSNDEILE-LARIAPDKAhktiCVTHLQSKGRGRQGRKWSHRLGECLMFSFGWVFDRPQYELGSLSPVAAVACRRALSR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 164 LGADkVRVKWPNDLYLNDRKLAGILVElTGKTGDAAQIVIGAGLNMVM-RNVQNDVVNQAWTNLQEAGITIDRNTLAVRM 242
Cdd:PRK13325 170 LGLK-TQIKWPNDLVVGRDKLGGILIE-TVRTGGKTVAVVGIGINFVLpKEVENAASVQSLFQTASRRGNADAAVLLETL 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695753858 243 IKELRSSLSLFEQEGLASFLSRWEKLDNFINRPVKLLI-GDKEIYGISRGIDAQGALLLEQDGVIKPWVGGEISLR 317
Cdd:PRK13325 248 LAELDAVLLQYARDGFAPFVAEYQAANRDHGKAVLLLRdGETVFEGTVKGVDGQGVLHLETAEGKQTVVSGEISLR 323
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
87-287 2.73e-17

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 78.84  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858  87 IDSTNQYLMDRLS--ELSSGDACVAEYQQAGRGRRGRKWFSPFGaNLYLSMYWRLEQGPA--AAVGLSLVIGIVMAEVLH 162
Cdd:PRK08477   9 LDSTQTYLIEKIKngELKAPFAIVAKEQTAGIGSRGNSWEGKKG-NLFFSFALKESDLPKdlPLQSSSIYFGFLLKEVLK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 163 DLGAdKVRVKWPNDLYLNDRKLAGIlveLTGKTGDaaQIVIGAGLNMvmrnvqnDVVNQAWTNLQeagITIDRNTLAVRM 242
Cdd:PRK08477  88 ELGS-KVWLKWPNDLYLDDKKIGGV---ITNKIKN--FIVCGIGLNL-------KFSPKNFACLD---IEISDDLLLEGF 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 243 IKELrsSLSLFEQEGLASFLSRWEKLDNFI----NRPVKL-----------LIGDKEIYG 287
Cdd:PRK08477 152 LQKI--EKKILWKQIFSKYKLEFEKSKSFSfhidGKLVSLkdaelledgsiLINGKKVYS 209
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 106-209 3.56e-13

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 67.97  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 106 ACVAEYQQAGRGRRGRKWFSPFGaNLYLSM-YWRLEQGPAAAVGLSLVIGIV-MAEVLHDLGADKVRVKWPNDLYLNDRK 183
Cdd:PTZ00276  35 AVLAESQTAGRGTGGRTWTSPKG-NMYFTLcIPQKGVPPELVPVLPLITGLAcRAAIMEVLHGAAVHTKWPNDIIYAGKK 113

                         90       100
                 ....*....|....*....|....*.
gi 695753858 184 LAGILVEltgktGDAAQIVIGAGLNM 209
Cdd:PTZ00276 114 IGGSLIE-----SEGEYLIIGIGMNI 134
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 271-317 7.39e-11

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: 56.70  E-value: 7.39e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 695753858  271 FINRPVKLLIGDKEIYGISRGIDAQGALLLEQ-DGVIKPWVGGEISLR 317
Cdd:pfam02237   1 TLGREVRVLLGDGIVEGIAVGIDDDGALLLETdDGTIRDINSGEVSLR 48
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 8-58 3.73e-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: 54.75  E-value: 3.73e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 695753858    8 LTLISIL-ADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGKGY 58
Cdd:pfam08279   1 LQILQLLlEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
PRK05935 PRK05935
biotin--protein ligase; Provisional
 112-250 2.12e-09

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 56.36  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 112 QQAGRGRRGRKWFSPFGaNLYLSMYWRLEQgpaAAVGLSLVIGIVMAEVL---HDLGADKVRVKWPNDLYLNDRKLAGIL 188
Cdd:PRK05935  38 QTAGKGKFGKSWHSSDQ-DLLASFCFFITV---LNIDVSLLFRLGTEAVMrlgEDLGITEAVIKWPNDVLVHGEKLCGVL 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695753858 189 VE---LTGKTGdaaqIVIGAGLNmvmRNVQND---VVNQAWTNLQE-AGITIDRNTLAVRMIKELRSSL 250
Cdd:PRK05935 114 CEtipVKGGLG----VILGIGVN---GNTTKDellGIDQPATSLQElLGHPIDLEEQRERLIKHIKHVL 175
YobV COG2378
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ...
 8-71 9.15e-06

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


Pssm-ID: 441945 [Multi-domain]  Cd Length: 314  Bit Score: 46.61  E-value: 9.15e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695753858   8 LTLISILADGEFHSGEQLGEHLGMSRAAINKHIQTLRDWGVDVFTVPGK--GYSLPE-----PIQLLNEEL 71
Cdd:COG2378    8 LALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELGVPIEAERGRggGYRLRDgyrlpPLMLTEEEA 78
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 170-300 6.74e-05

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 43.66  E-value: 6.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695753858 170 RVKWPNDLYLNDRKLAGILVEL------TGKTGDAAQIVIGAGLNMVMRNvQNDVVNQAWTNLQEAGITiDRNT------ 237
Cdd:PTZ00275 121 QIKWINDVLVNYKKIAGCLVHLyylddfPNLNSRYVCVMVGIGINVTLED-KHNLLNNNYTSIKKELQR-DFNTpksips 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695753858 238 ---LAVRMIKELRSSLSLFEQEGLASFLsrwekldNFINrpVKLLIGDKE---------IYGISRGIDAQGALLL 300
Cdd:PTZ00275 199 veqVTEKLIINLKAVINKLRKEGFSSFL-------DYIT--PRLLYKDKKvlidqdnelIVGYLQGLLHDGSLLL 264
HTH_metalloreg NF033788
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ...
 8-48 6.78e-04

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: 37.82  E-value: 6.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 695753858   8 LTLISILADGEFHSGEqLGEHLGMSRAAINKHIQTLRDWGV 48
Cdd:NF033788  14 LRILELLAEGELCVCE-LAEALGLSQSAVSQHLKVLRDAGL 53
ArsR COG0640
DNA-binding transcriptional regulator, ArsR family [Transcription];
8-48 2.01e-03

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


Pssm-ID: 440405 [Multi-domain]  Cd Length: 92  Bit Score: 36.79  E-value: 2.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 695753858   8 LTLISILADGEFHSGEqLGEHLGMSRAAINKHIQTLRDWGV 48
Cdd:COG0640   23 LRILRLLAEGELCVGE-LAEALGLSQSTVSHHLKVLREAGL 62
 
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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