ID A0Q7Z5_FRATN Unreviewed; 631 AA.
AC A0Q7Z5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN Name=aceF {ECO:0000313|EMBL:ABK90360.1};
GN OrderedLocusNames=FTN_1493 {ECO:0000313|EMBL:ABK90360.1};
GN ORFNames=AW25_508 {ECO:0000313|EMBL:AJI60477.1};
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK90360.1, ECO:0000313|Proteomes:UP000000762};
RN [1] {ECO:0000313|EMBL:ABK90360.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U112 {ECO:0000313|EMBL:ABK90360.1};
RA Brittnacher M., Rohmer L., Zhou Y., Abmayr S., D'Argenio D., Bovee D.,
RA Chang J., Chen J., Drees B., Ernst R., Fong C., Forsman M., Gallagher L.,
RA Gallis B., Gillett W., Goodlett D., Guina T., Guenthner D., Haugen E.,
RA Hayden H., Jacobs M., Kang A., Larson Freeman T., Levy R., Lim R.,
RA Manoil C., Olson M.V., Radey M., Shaffer S., Svensson K., Taylor G.,
RA Wasnick M., Kaul R., Miller S.I.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112 {ECO:0000313|Proteomes:UP000000762};
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
RN [3] {ECO:0000313|EMBL:AJI60477.1, ECO:0000313|Proteomes:UP000031872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112 {ECO:0000313|EMBL:AJI60477.1,
RC ECO:0000313|Proteomes:UP000031872};
RX PubMed=25931589;
RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O.,
RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S.,
RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT "Genome sequencing of 18 francisella strains to aid in assay development
RT and testing.";
RL Genome Announc. 3:0-0(2015).
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). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
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 Evidence={ECO:0000256|ARBA:ARBA00000925,
CC ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 3 lipoyl cofactors covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484,
CC ECO:0000256|RuleBase:RU361137}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR EMBL; CP000439; ABK90360.1; -; Genomic_DNA.
DR EMBL; CP009633; AJI60477.1; -; Genomic_DNA.
DR RefSeq; WP_003040481.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q7Z5; -.
DR KEGG; ftn:FTN_1493; -.
DR KEGG; ftx:AW25_508; -.
DR OMA; HPCIMAP; -.
DR BioCyc; FTUL401614:G1G75-1541-MONOMER; -.
DR Proteomes; UP000000762; Chromosome.
DR Proteomes; UP000031872; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 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 NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW ECO:0000313|EMBL:ABK90360.1};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:ABK90360.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AJI60477.1}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 107..181
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 207..281
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 331..368
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 284..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 67155 MW; 28D7B051C983C08F CRC64;
MSIEIVKVPD IGDYDNVDVI EVNVAVGDVI AEEDSLITLE TDKASMEVPS PVAGKITKLT
VKVGDKVSQG TAIMEVEVES AADQAATTQS QPQTTSSAPV AATTNQIVDV EVPDIGDYDS
VDVIEVSVKV GDEIAEEDSL ITLETDKASM EVPSPVAGKV VEVITKVGDK VSQGSLILKV
ETGSSAQAPA QEQSQQSAPV KSAAEEIIDV KVPDIGDYDS VDVIEVSVAV GDKIEEEDSL
ITLETDKASM EVPSPVAGEV VEIITKVGDK VSQGSLILKV KTQGSAPVEQ TSSQPAPAKQ
EQAKQQAATP AAPAPASSSV NEYAVDNSNA HASPAVRKLA RILNIDLSKV KATGRKGRVT
KEDCYNYIKH AVTQVQTGKV AASGSGLDLL DDPVVDFAKF GEIETQPLSR INKISAKNLH
RNWVKIPHVT FYDDADVTDL EEFRNAKKAF AEKKGIKITP LSFLVKAAAV ALQEFPRFNS
SLSNDGENLI IKKYYNIGFA ADTPAGLMVP VIKDADKKGI IEISKDIMEL AGKARDGKLG
AKDMTGATFT ISSLGVLGTT SFTPIINMPE VAIMGVSKTA VKPIWNGKEF IPRTMLPLSL
STDHRVIDGA LAAKFLTRYC QILSDLREII M
//