ID W0Q6P2_9PAST Unreviewed; 633 AA.
AC W0Q6P2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN ORFNames=X781_13880 {ECO:0000313|EMBL:AHG73535.1};
OS Mannheimia sp. USDA-ARS-USMARC-1261.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=1432056 {ECO:0000313|EMBL:AHG73535.1, ECO:0000313|Proteomes:UP000019094};
RN [1] {ECO:0000313|EMBL:AHG73535.1, ECO:0000313|Proteomes:UP000019094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-1261 {ECO:0000313|EMBL:AHG73535.1,
RC ECO:0000313|Proteomes:UP000019094};
RX PubMed=24526648;
RA Harhay G.P., Murray R.W., Lubbers B., Griffin D., Koren S., Phillippy A.M.,
RA Harhay D.M., Bono J., Clawson M.L., Heaton M.P., Chitko-McKown C.G.,
RA Smith T.P.;
RT "Complete Closed Genome Sequences of Four Mannheimia varigena Isolates from
RT Cattle with Shipping Fever.";
RL Genome Announc. 2:e00088-14(2014).
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:ARBA00043782,
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; CP006942; AHG73535.1; -; Genomic_DNA.
DR RefSeq; WP_025236142.1; NZ_CP006942.1.
DR AlphaFoldDB; W0Q6P2; -.
DR STRING; 1432056.X781_13880; -.
DR KEGG; mvr:X781_13880; -.
DR PATRIC; fig|1432056.3.peg.1386; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000019094; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:AHG73535.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AHG73535.1}.
FT DOMAIN 2..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 100..173
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 199..272
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 324..361
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 633 AA; 66649 MW; AFDD476BCEC521E9 CRC64;
MSKQINVPDI GSDEVSVTEV MVKVGDTISV DQSIINVEGD KASMEVPAPE AGVVKEVLVK
VGDKVSTGSP MLVLESADAA PAVEVPKAEA APVAPVTSAV VEVNVPDIGS DEVNVTEIMV
KVGDSVEVDQ SIINVEGDKA SMEVPAPVAG VVKEIFINVG DKVSTGKLIM KFETASSAPA
QAAPVAEAAA PAQASASAIK DVNVPDIGGD EVNVTEIMVK VGDSVSEEQS LITVEGDKAS
MEVPAPFAGV VKEILVKSGD KVSTGSLIMK FEVAGAAPAP AATQVASDPA PQVAAPAKAD
AVATGQNQSG LNQEQVVSAA GYAHATPVIR RLAREFGVNL DKVKGTGRKG RIVKEDIQAY
VKTAVQVFEK QGGTAAAATG AANGAGLGLL PWPKVDFSKF GEVEEVELSR INKISGANLH
RNWVMIPHVT HFDRTDITEL ENFRKEQNKE AEKRKLDVKI TPVVFIMKAV ASALEAFPRF
NSSISEDAQR LTLKKYINIG VAVDTPNGLV VPVFKNVNKK GIIELSRELM EVSKKAREGK
LTASDMQGGC FTISSLGGIG TTHFTPIVNA PEVAILGVSK SEMQPIWNGK EFEPRLMLPL
SLSFDHRVID GADGARFLSY INGVLADIRR LVM
//
