(data stored in SCRATCH zone)

SWISSPROT: ODB2_BACSU

ID   ODB2_BACSU              Reviewed;         424 AA.
AC   P37942;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 136.
DE   RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;
DE            EC=2.3.1.168;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase complex component E2;
DE            Short=BCKAD-E2;
DE            Short=BCKADE2;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;
DE   AltName: Full=Dihydrolipoamide branched chain transacylase;
DE   AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;
GN   Name=bfmBB; Synonyms=bfmB, bfmB2; OrderedLocusNames=BSU24030;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8504804; DOI=10.1111/j.1432-1033.1993.tb17858.x;
RA   Wang G.-F., Kuriki T., Roy K.L., Kaneda T.;
RT   "The primary structure of branched-chain alpha-oxo acid dehydrogenase from
RT   Bacillus subtilis and its similarity to other alpha-oxo acid
RT   dehydrogenases.";
RL   Eur. J. Biochem. 213:1091-1099(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 266-424.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=7961792;
RA   Ahmed M., Borsch C.M., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A.;
RT   "A protein that activates expression of a multidrug efflux transporter upon
RT   binding the transporter substrates.";
RL   J. Biol. Chem. 269:28506-28513(1994).
CC   -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC       the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: branched-chain
CC       alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-
CC         CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC         [protein] + CoA; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC         Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; M97391; AAA22280.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12600.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14334.1; -; Genomic_DNA.
DR   EMBL; L25604; AAB81541.1; -; Genomic_DNA.
DR   PIR; S32488; S32488.
DR   RefSeq; NP_390283.1; NC_000964.3.
DR   RefSeq; WP_003230323.1; NZ_JNCM01000036.1.
DR   SMR; P37942; -.
DR   IntAct; P37942; 1.
DR   STRING; 224308.BSU24030; -.
DR   jPOST; P37942; -.
DR   PaxDb; P37942; -.
DR   PRIDE; P37942; -.
DR   EnsemblBacteria; CAB14334; CAB14334; BSU24030.
DR   GeneID; 938677; -.
DR   KEGG; bsu:BSU24030; -.
DR   PATRIC; fig|224308.179.peg.2617; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281564; -.
DR   InParanoid; P37942; -.
DR   KO; K09699; -.
DR   OMA; VPNIKNC; -.
DR   PhylomeDB; P37942; -.
DR   BioCyc; BSUB:BSU24030-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-11686; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; P37942.
DR   SWISS-2DPAGE; P37942.
KW   Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Transferase.
FT   CHAIN           1..424
FT                   /note="Lipoamide acyltransferase component of branched-
FT                   chain alpha-keto acid dehydrogenase complex"
FT                   /id="PRO_0000162302"
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          116..153
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255"
FT   MOD_RES         44
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   CONFLICT        305
FT                   /note="A -> P (in Ref. 4; AAB81541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="V -> I (in Ref. 4; AAB81541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="Q -> E (in Ref. 4; AAB81541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="V -> D (in Ref. 4; AAB81541)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   424 AA;  45837 MW;  2E0C9EAF817CE228 CRC64;
     MAIEQMTMPQ LGESVTEGTI SKWLVAPGDK VNKYDPIAEV MTDKVNAEVP SSFTGTITEL
     VGEEGQTLQV GEMICKIETE GANPAEQKQE QPAASEAAEN PVAKSAGAAD QPNKKRYSPA
     VLRLAGEHGI DLDQVTGTGA GGRITRKDIQ RLIETGGVQE QNPEELKTAA PAPKSASKPE
     PKEETSYPAS AAGDKEIPVT GVRKAIASNM KRSKTEIPHA WTMMEVDVTN MVAYRNSIKD
     SFKKTEGFNL TFFAFFVKAV AQALKEFPQM NSMWAGDKII QKKDINISIA VATEDSLFVP
     VIKNADEKTI KGIAKDITGL AKKVRDGKLT ADDMQGGTFT VNNTGSFGSV QSMGIINYPQ
     AAILQVESIV KRPVVMDNGM IAVRDMVNLC LSLDHRVLDG LVCGRFLGRV KQILESIDEK
     TSVY
//

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