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Bacillus subtilis subsp. subtilis str. 168 (bsub0)
Gene : bkdB
DDBJ      :bkdB         branched-chain alpha-keto acid dehydrogenase E2 subunit (lipoamide acyltransferase)
Swiss-Prot:ODB2_BACSU   RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;         EC=2.3.1.168;AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;         Short=E2;AltName: Full=Dihydrolipoamide branched chain transacylase;

Homologs  Archaea  22/68 : Bacteria  782/915 : Eukaryota  192/199 : Viruses  0/175   --->[See Alignment]
a.9.1b.84.1c.43.1
:424 amino acids
:SECSTR
:PSIPRED
:DISOPRED
:BLT:PDB   5->81 1labA PDBj 1e-13 37.7 %
:BLT:PDB   110->151 1balA PDBj 8e-08 42.9 %
:BLT:PDB   188->414 1b5sA PDBj 1e-38 41.7 %
:RPS:PDB   1->121 3b7mA PDBj 4e-18 13.3 %
:RPS:PDB   108->156 1balA PDBj 2e-12 36.7 %
:RPS:PDB   197->415 1c4tA PDBj 2e-72 34.9 %
:RPS:SCOP  2->82 1gjxA  b.84.1.1 * 7e-16 26.2 %
:RPS:SCOP  108->156 1balA  a.9.1.1 * 7e-13 36.7 %
:RPS:SCOP  194->415 1c4tA  c.43.1.1 * 1e-71 35.8 %
:HMM:SCOP  1->99 1y8oB1 b.84.1.1 * 2e-26 40.4 %
:HMM:SCOP  106->156 1balA_ a.9.1.1 * 2.5e-12 43.1 %
:HMM:SCOP  180->416 1eafA_ c.43.1.1 * 1.8e-85 49.6 %
:RPS:PFM   9->72 PF00364 * Biotin_lipoyl 3e-09 43.8 %
:RPS:PFM   118->151 PF02817 * E3_binding 2e-06 61.8 %
:RPS:PFM   194->415 PF00198 * 2-oxoacid_dh 1e-51 49.1 %
:HMM:PFM   193->418 PF00198 * 2-oxoacid_dh 2.2e-87 48.2 224/231  
:HMM:PFM   5->77 PF00364 * Biotin_lipoyl 2.2e-26 38.4 73/74  
:HMM:PFM   118->150 PF02817 * E3_binding 1.2e-19 63.6 33/39  
:BLT:SWISS 1->424 ODB2_BACSU 0.0 100.0 %
:PROS 28->57|PS00189|LIPOYL
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID CAB14334.1 GT:GENE bkdB GT:PRODUCT branched-chain alpha-keto acid dehydrogenase E2 subunit (lipoamide acyltransferase) GT:DATABASE GIB00011CH01 GT:ORG bsub0 GB:ACCESSION GIB00011CH01 GB:LOCATION complement(2496796..2498070) GB:FROM 2496796 GB:TO 2498070 GB:DIRECTION - GB:GENE bkdB GB:PRODUCT branched-chain alpha-keto acid dehydrogenase E2 subunit (lipoamide acyltransferase) GB:FUNCTION 16.8: Protect 16.11: Scavenge (Catabolism) 16.2: Construct biomass (Anabolism) GB:NOTE Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 10094682, 12427936, 15241682; Product type e: enzyme GB:PROTEIN_ID CAB14334.1 GB:DB_XREF GOA:P37942 HSSP:1E2O InterPro:IPR004167 SubtiList:BG10305 UniProtKB/Swiss-Prot:P37942 GB:GENE:GENE bkdB LENGTH 424 SQ:AASEQ MAIEQMTMPQLGESVTEGTISKWLVAPGDKVNKYDPIAEVMTDKVNAEVPSSFTGTITELVGEEGQTLQVGEMICKIETEGANPAEQKQEQPAASEAAENPVAKSAGAADQPNKKRYSPAVLRLAGEHGIDLDQVTGTGAGGRITRKDIQRLIETGGVQEQNPEELKTAAPAPKSASKPEPKEETSYPASAAGDKEIPVTGVRKAIASNMKRSKTEIPHAWTMMEVDVTNMVAYRNSIKDSFKKTEGFNLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDSLFVPVIKNADEKTIKGIAKDITGLAKKVRDGKLTADDMQGGTFTVNNTGSFGSVQSMGIINYPQAAILQVESIVKRPVVMDNGMIAVRDMVNLCLSLDHRVLDGLVCGRFLGRVKQILESIDEKTSVY GT:EXON 1|1-424:0| SW:ID ODB2_BACSU SW:DE RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; EC=2.3.1.168;AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; Short=E2;AltName: Full=Dihydrolipoamide branched chain transacylase; SW:GN Name=bfmBB; Synonyms=bfmB, bfmB2; OrderedLocusNames=BSU24030; SW:KW Acyltransferase; Complete proteome; Glycolysis; Lipoyl; Transferase. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1->424|ODB2_BACSU|0.0|100.0|424/424| GO:SWS:NREP 4 GO:SWS GO:0008415|"GO:acyltransferase activity"|Acyltransferase| GO:SWS GO:0006096|"GO:glycolysis"|Glycolysis| GO:SWS GO:0031405|"GO:lipoic acid binding"|Lipoyl| GO:SWS GO:0016740|"GO:transferase activity"|Transferase| PROS 28->57|PS00189|LIPOYL|PDOC00168| SEG 167->186|ktaapapksaskpepkeets| SEG 252->263|ffaffvkavaqa| BL:PDB:NREP 3 BL:PDB:REP 5->81|1labA|1e-13|37.7|77/80| BL:PDB:REP 110->151|1balA|8e-08|42.9|42/51| BL:PDB:REP 188->414|1b5sA|1e-38|41.7|223/242| RP:PDB:NREP 3 RP:PDB:REP 1->121|3b7mA|4e-18|13.3|120/216| RP:PDB:REP 108->156|1balA|2e-12|36.7|49/51| RP:PDB:REP 197->415|1c4tA|2e-72|34.9|218/226| RP:PFM:NREP 3 RP:PFM:REP 9->72|PF00364|3e-09|43.8|64/74|Biotin_lipoyl| RP:PFM:REP 118->151|PF02817|2e-06|61.8|34/39|E3_binding| RP:PFM:REP 194->415|PF00198|1e-51|49.1|220/232|2-oxoacid_dh| HM:PFM:NREP 3 HM:PFM:REP 193->418|PF00198|2.2e-87|48.2|224/231|2-oxoacid_dh| HM:PFM:REP 5->77|PF00364|2.2e-26|38.4|73/74|Biotin_lipoyl| HM:PFM:REP 118->150|PF02817|1.2e-19|63.6|33/39|E3_binding| GO:PFM:NREP 5 GO:PFM GO:0005515|"GO:protein binding"|PF02817|IPR004167| GO:PFM GO:0008152|"GO:metabolic process"|PF02817|IPR004167| GO:PFM GO:0008415|"GO:acyltransferase activity"|PF02817|IPR004167| GO:PFM GO:0008152|"GO:metabolic process"|PF00198|IPR001078| GO:PFM GO:0008415|"GO:acyltransferase activity"|PF00198|IPR001078| RP:SCP:NREP 3 RP:SCP:REP 2->82|1gjxA|7e-16|26.2|80/81|b.84.1.1| RP:SCP:REP 108->156|1balA|7e-13|36.7|49/51|a.9.1.1| RP:SCP:REP 194->415|1c4tA|1e-71|35.8|218/226|c.43.1.1| HM:SCP:REP 1->99|1y8oB1|2e-26|40.4|99/0|b.84.1.1|1/1|Single hybrid motif| HM:SCP:REP 106->156|1balA_|2.5e-12|43.1|51/51|a.9.1.1|1/1|Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex| HM:SCP:REP 180->416|1eafA_|1.8e-85|49.6|232/243|c.43.1.1|1/1|CoA-dependent acyltransferases| OP:NHOMO 2831 OP:NHOMOORG 996 OP:PATTERN 11------1111112---111---2111--11----------------------------1111---- 1223522222223242333-322243333333444435763444344433335574462244434374544-----------4---1-111--1--22233334333333333333333333332---1----12-35533---231111111111111111111111121111111111111333331--424444444443444444464454444455344322222242233333333333333344432-1-22-1---111111111111111222211112211111-111112222222222222211111111111---1111111-1--211---------3-----------1--11311-13-2422322232224223222222255555533444-225225232432233232733354223234243333232444444442222223222222222222222222222222222222246841232234554553333333353333244442324233322222222444222221112222222222223322-1-2----------323133421333333-21---------------------112223223323343434333343333333333441-2432222222232222222222233322-222223322223222222323322232222222222222222222222222222222222222222223333333333223232222222222222223333323222324444343333433222222222222211223222223323333333332222222111-222221----------111111-1-11111111221111-------------223 33--444-733-3333333343344433333333333423333333333455554434333332222222222222222222222222-45433343333433545-3447466656434334446473Af4-74D3432514644444444463954449F37343434B54554534w444458AFD4B65684562 ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 396 STR:RPRED 93.4 SQ:SECSTR EEEEEEccTTcccTTcEEEEEEEEEEEcccccccEEEEEEEETTEEEEEEEEEcccEEEEEEEEcccccEEEEEEHHHHHHHHHHHTcccTTcEEEEEEEEEEEEEccTcTcEEEEEEEEETTHHHHTTccTTccccccTTccccHHHHTTTccccHTcccccc#######################GGGccccccccccccccHHHHHHHHHHHcccEEEEEEEEEcHHHHHHHHHHHHHHHHHHccccccHHHHHHHHHHHHHHcHHHHcEEETTEEEccccccEEEcEEETTEEEccEEccTTTccHHHHHHHHHHHHHHHHTTcccTTTTccccEEEEEcGGGTcccccccccTTccEEEEEcccEEEEEEcETTEEEEEEEEEEEEEEETTTccHHHHHHHHHHHHHHHTcGGG##### DISOP:02AL 83-124, 141-142, 149-193| PSIPRED ccEEEEEccccccccccEEEEEEEEccccEEccccEEEEEEEccEEEEEEcccccEEEEEEEccccEEEcccEEEEEEcccccccccccccccccccccccccccccccccccccccHHHHHHHHHHHcccHHHccccccccEEcHHHHHHHHHccccccccccccccccccccccccccccccccccccccccEEEEcHHHHHHHHHHHHHHHHcccEEEEEEEEcHHHHHHHHHHHHHHHHHccccEEcHHHHHHHHHHHHHHHccEEEEEEEccEEEEcccccEEEEEEccccEEEEEEcccccccHHHHHHHHHHHHHHHHHccccHHHHccccEEEEEccccccEEEEEEEccccEEEEEccccEEEEEEEccccEEEEEEEEEEEEEcccEEEHHHHHHHHHHHHHHHccccHHHccc //