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 03-AUG-2022, entry version 145.
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 / NRRL NRS-744 / VKM B-501;
RX PubMed=7961792; DOI=10.1016/s0021-9258(18)46956-6;
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}.
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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 AlphaFoldDB; P37942; -.
DR SMR; P37942; -.
DR IntAct; P37942; 1.
DR STRING; 224308.BSU24030; -.
DR jPOST; P37942; -.
DR PaxDb; P37942; -.
DR PRIDE; P37942; -.
DR EnsemblBacteria; CAB14334; CAB14334; BSU_24030.
DR GeneID; 938677; -.
DR KEGG; bsu:BSU24030; -.
DR PATRIC; fig|224308.179.peg.2617; -.
DR eggNOG; COG0508; Bacteria.
DR InParanoid; P37942; -.
DR OMA; HPCIMAP; -.
DR PhylomeDB; P37942; -.
DR BioCyc; BSUB:BSU24030-MON; -.
DR BioCyc; MetaCyc:MON-11686; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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;
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 REGION 82..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
