ODP2_HAEIN
ID ODP2_HAEIN Reviewed; 567 AA.
AC P45118;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
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;
GN Name=aceF; OrderedLocusNames=HI_1232;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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) (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 2 lipoyl cofactors covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22885.1; -; Genomic_DNA.
DR PIR; I64111; I64111.
DR RefSeq; NP_439388.1; NC_000907.1.
DR RefSeq; WP_010869159.1; NC_000907.1.
DR AlphaFoldDB; P45118; -.
DR SMR; P45118; -.
DR STRING; 71421.HI_1232; -.
DR EnsemblBacteria; AAC22885; AAC22885; HI_1232.
DR KEGG; hin:HI_1232; -.
DR PATRIC; fig|71421.8.peg.1284; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OMA; TMEFESF; -.
DR PhylomeDB; P45118; -.
DR BioCyc; HINF71421:G1GJ1-1263-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
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 PANTHER; PTHR43178:SF2; PTHR43178:SF2; 3.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 2.
DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..567
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162279"
FT DOMAIN 2..75
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 108..181
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 258..295
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 192..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /evidence="ECO:0000255"
FT ACT_SITE 540
FT /evidence="ECO:0000255"
FT ACT_SITE 544
FT /evidence="ECO:0000255"
FT MOD_RES 41
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 147
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 567 AA; 59411 MW; 891DBCDEB388C5B0 CRC64;
MSKQIQIPDI GSDEVTVTEV MVNVGDTISV DQSIINVEGD KASMEVPAPE AGVVKEILVK
VGDKVSTGTP MLVLEAAGAA PAADEPTAPV ADAPTAPVVA TAPTASAIVE VNVPDIGGDE
VNVTEIMVAV GDTITEEQSL ITVEGDKASM EVPAPFGGVV KEILVKSGDK VSTGSLIMRF
EVLGAAPAES ASAPASTSAP QTAAPATTAQ APQAAAPDTT AQAPQAAAPD TTAQAAQSNN
NVSGLSQEQV EASTGYAHAT PVIRRLAREF GVNLDKVKGT GRKGRIVKED IEAYVKTAVK
AYESGATAQA TGNGVANGAG LGLLPWPKVD FSKFGEIEEV ELSRINKISG ANLHRNWVII
PHVTHFDKAD ITDLEAFRKE QNALREKQKL GVKITPVVFI MKAVAKALEA YPRFNSSITE
DAQRLILKKY INIGVAVDTP NGLVVPVFKN VNKKGIIELS RELMEVSKKA REGKLTASDM
QGGCFTISSL GGIGTTHFAP IVNAPEVAIL GVSKSSMEPV WNGKEFAPRL ILPMSLSFDH
RVIDGADGAR FISYLGSVLA DLRRLVM
