ID A8GJ15_SERP5 Unreviewed; 630 AA.
AC A8GJ15;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN OrderedLocusNames=Spro_4010 {ECO:0000313|EMBL:ABV43105.1};
OS Serratia proteamaculans (strain 568).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV43105.1};
RN [1] {ECO:0000313|EMBL:ABV43105.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568 {ECO:0000313|EMBL:ABV43105.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000826; ABV43105.1; -; Genomic_DNA.
DR AlphaFoldDB; A8GJ15; -.
DR STRING; 399741.Spro_4010; -.
DR KEGG; spe:Spro_4010; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OMA; HPCIMAP; -.
DR OrthoDB; 9805770at2; -.
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:ABV43105.1};
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:ABV43105.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:ABV43105.1}.
FT DOMAIN 2..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 105..178
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 208..281
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 327..364
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 630 AA; 65709 MW; A23B04CF9BB36773 CRC64;
MSIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGVVKEIKVA
VGDKTETGKL LMIFEAEGAA QAAPAAKAEE KPAAAPAAAP AAAAAKDVAV PDIGADEVEV
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KIATGDKVTT GSMIMVFEVA
GAASAAAPAA AQAPAAPAAP AASAASAAKD VAVPDIGGDE VEVTEVMVKV GDKVAAEQSL
ITVEGDKASM EVPAPFAGTV KEIKISAGDK VKTGSLIMVF EVEGAAPAAA PAQKAEAAPA
PAASSAPAQQ AAPAAKGEFT ENDAYVHATP VIRRLAREFG VNLAKVKGTG RKGRILREDV
QTYVKDAVKR AEAAPAAAAG GGLPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW
VMIPHVTHFD KTDITDLEAF RKQQNEEAAK RKLDVKFTPV VFIMKAVAAA LEQMPRFNSS
LSEDGQKLTL KKYINVGVAV DTPNGLVVPV FKDVNKKSIT ELSRELMAIS KKARDGKLTA
GEMQGGCFTI SSLGGIGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMMPMSLS
FDHRVIDGAD GARFITIINN MLADIRRMVM
//