ODP2_BACSU
ID ODP2_BACSU Reviewed; 442 AA.
AC P21883;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE AltName: Full=E2;
DE AltName: Full=S complex, 48 kDa subunit;
GN Name=pdhC; Synonyms=aceC; OrderedLocusNames=BSU14600;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LIPOYLATION AT LYS-43.
RC STRAIN=168;
RX PubMed=1697575; DOI=10.1128/jb.172.9.5052-5063.1990;
RA Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.;
RT "Secretory S complex of Bacillus subtilis: sequence analysis and identity
RT to pyruvate dehydrogenase.";
RL J. Bacteriol. 172:5052-5063(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT 168 chromosome: sequencing of a 27 kb segment and identification of several
RT genes in the area.";
RL Microbiology 142:3033-3037(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3).
CC -!- FUNCTION: The B.subtilis PDH complex possesses also branched-chain 2-
CC oxoacid dehydrogenase (BCDH) activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
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; M57435; AAA62683.1; -; Genomic_DNA.
DR EMBL; AF012285; AAC24934.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13333.1; -; Genomic_DNA.
DR PIR; D36718; D36718.
DR RefSeq; NP_389343.1; NC_000964.3.
DR RefSeq; WP_003232311.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P21883; -.
DR SMR; P21883; -.
DR IntAct; P21883; 1.
DR STRING; 224308.BSU14600; -.
DR jPOST; P21883; -.
DR PaxDb; P21883; -.
DR PRIDE; P21883; -.
DR EnsemblBacteria; CAB13333; CAB13333; BSU_14600.
DR GeneID; 936010; -.
DR KEGG; bsu:BSU14600; -.
DR PATRIC; fig|224308.179.peg.1592; -.
DR eggNOG; COG0508; Bacteria.
DR InParanoid; P21883; -.
DR OMA; TMEFESF; -.
DR PhylomeDB; P21883; -.
DR BioCyc; BSUB:BSU14600-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase 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 1: Evidence at protein level;
KW Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..442
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162274"
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 141..178
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 84..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /evidence="ECO:0000255"
FT MOD_RES 43
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:1697575"
SQ SEQUENCE 442 AA; 47539 MW; 73AFC68220717C34 CRC64;
MAFEFKLPDI GEGIHEGEIV KWFVKPNDEV DEDDVLAEVQ NDKAVVEIPS PVKGKVLELK
VEEGTVATVG QTIITFDAPG YEDLQFKGSD ESDDAKTEAQ VQSTAEAGQD VAKEEQAQEP
AKATGAGQQD QAEVDPNKRV IAMPSVRKYA REKGVDIRKV TGSGNNGRVV KEDIDSFVNG
GAQEAAPQET AAPQETAAKP AAAPAPEGEF PETREKMSGI RKAIAKAMVN SKHTAPHVTL
MDEVDVTNLV AHRKQFKQVA ADQGIKLTYL PYVVKALTSA LKKFPVLNTS IDDKTDEVIQ
KHYFNIGIAA DTEKGLLVPV VKNADRKSVF EISDEINGLA TKAREGKLAP AEMKGASCTI
TNIGSAGGQW FTPVINHPEV AILGIGRIAE KAIVRDGEIV AAPVLALSLS FDHRMIDGAT
AQNALNHIKR LLNDPQLILM EA
