ID F1SMB2_PIG Unreviewed; 578 AA.
AC F1SMB2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 24-JAN-2024, entry version 88.
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=DLAT {ECO:0000313|Ensembl:ENSSSCP00000015954.4,
GN ECO:0000313|VGNC:VGNC:87325};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000015954.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000015954.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000015954.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000015954.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361137}.
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|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR AlphaFoldDB; F1SMB2; -.
DR PeptideAtlas; F1SMB2; -.
DR Ensembl; ENSSSCT00000016395.5; ENSSSCP00000015954.4; ENSSSCG00000015030.5.
DR VGNC; VGNC:87325; DLAT.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000154943; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR TreeFam; TF106145; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000015030; Expressed in heart left ventricle and 43 other cell types or tissues.
DR ExpressionAtlas; F1SMB2; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1SMB2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 91..167
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 287..324
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 185..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 61810 MW; 5776A327F58B0B08 CRC64;
MWRVCARRAQ NAAPRAGFGA RWTALREEPG APCAAPRAGS VPARCSSTTR GYGRSRALCG
WSASSWATPQ NRILLQLWGS PNRRWYSLPP HQKVPLPSLS PTMQAGTIAR WEKKEGDKIN
EGELIAEVET DKATVGFESL EECYMAKILV AEGTRDVPVG AIICITVEKP EDIEAFKNYT
LDSSAAPAPQ AAPAPTPAAA APAPTPSAQA PGSSYPTHMQ VVLPALSPTM TMGTVQRWEK
KVGEKLSEGD LLAEIETDKA TIAPQPVAPT PAATRPATPA GPKGRLFVSP LAKKLASEKG
IDLTQIKGTG PDGRIIKKDI DSFVPTKAAP PPAAAVPPPS PGVAPVPTGV FTDIPISNIR
RVIAQRLMQS KQTIPHYYLS VDVNMGEVLL VRKELNKMLE GRSKISVNDF IIKASALACL
KVPEANSSWL DTVIRQNHVV DISVAVSTPA GLITPIVFNA HIKGLETIAN DVVSLATKAR
EGKLQPHEFQ GGTFTISNLG MFGIKNFSAI INPPQACILA VGASEDRLFP ADNEKGFDVA
SMMSVTLSCD HRVVDGAVGA QWLAEFRKYL EKPITMLL
//