lat1

UniProt ID: O59816
Organism: Schizosaccharomyces pombe 972h-
Review Status: DRAFT
📝 Provide Detailed Feedback

Gene Description

lat1 (SPCC794.07; UniProt O59816) encodes the lipoylated E2 dihydrolipoyllysine-residue acetyltransferase (EC 2.3.1.12) that forms the core of the mitochondrial pyruvate dehydrogenase complex and transfers the acetyl group to CoA. Function is assigned by orthology to S. cerevisiae LAT1.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity
IBA
GO_REF:0000033 		ACCEPT
Summary: E2 dihydrolipoyllysine acetyltransferase activity (PAINT/EC/similarity).
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated catalytic activity is EC 2.3.1.12, the acetyl transfer from acetyl-dihydrolipoyl-lysine to CoA, and the protein carries the mitochondrial PDH E2 family signatures (IPR006257, TIGR01349). The PAINT node lies in the E2 acetyltransferase clade, so the IBA is sound.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000250|UniProtKB:P12695};
file:SCHPO/lat1/lat1-uniprot.txt
InterPro; IPR006257; LAT1.
file:SCHPO/lat1/lat1-uniprot.txt
NCBIfam; TIGR01349; PDHac_trf_mito; 1.
GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity
IEA
GO_REF:0000120 		ACCEPT
Summary: E2 dihydrolipoyllysine acetyltransferase activity (PAINT/EC/similarity).
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated catalytic activity is EC 2.3.1.12, the acetyl transfer from acetyl-dihydrolipoyl-lysine to CoA, and the protein carries the mitochondrial PDH E2 family signatures (IPR006257, TIGR01349).
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000250|UniProtKB:P12695};
file:SCHPO/lat1/lat1-uniprot.txt
InterPro; IPR006257; LAT1.
GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity
ISS
GO_REF:0000024 		ACCEPT
Summary: E2 dihydrolipoyllysine acetyltransferase activity (PAINT/EC/similarity).
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated catalytic activity is EC 2.3.1.12, the acetyl transfer from acetyl-dihydrolipoyl-lysine to CoA, and the protein carries the mitochondrial PDH E2 family signatures (IPR006257, TIGR01349).
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000250|UniProtKB:P12695};
file:SCHPO/lat1/lat1-uniprot.txt
The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
GO:0005739 mitochondrion
HDA
PMID:16823372
ORFeome cloning and global analysis of protein localization ... 		ACCEPT
Summary: ORFeome YFP screen: mitochondrion.
Supporting Evidence:
PMID:16823372
we determined the localization of 4,431 proteins
GO:0005739 mitochondrion
IBA
GO_REF:0000033 		ACCEPT
Summary: PAINT inference of mitochondrial location.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated location is the mitochondrial matrix, which entails the organelle; the PAINT node is in the mitochondrial PDH E2 clade (TIGR01349), so the root organelle claim holds. The matrix sub-compartment is carried by its own rows.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
Mitochondrion matrix {ECO:0000250|UniProtKB:P12695}.
file:SCHPO/lat1/lat1-uniprot.txt
NCBIfam; TIGR01349; PDHac_trf_mito; 1.
GO:0005759 mitochondrial matrix
IC
GO_REF:0000111 		ACCEPT
Summary: Matrix location of this TCA enzyme (inference or mapping); consistent.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated UniProt location is the mitochondrial matrix, where the PDH complex acts.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
Mitochondrion matrix {ECO:0000250|UniProtKB:P12695}.
file:SCHPO/lat1/lat1-uniprot.txt
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
GO:0005759 mitochondrial matrix
IEA
GO_REF:0000044 		ACCEPT
Summary: Matrix location of this TCA enzyme (inference or mapping); consistent.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated UniProt location is the mitochondrial matrix, where the PDH complex acts.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
Mitochondrion matrix {ECO:0000250|UniProtKB:P12695}.
GO:0005759 mitochondrial matrix
ISS
GO_REF:0000024 		ACCEPT
Summary: Matrix location of this TCA enzyme (inference or mapping); consistent.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated UniProt location is the mitochondrial matrix, where the PDH complex acts.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
Mitochondrion matrix {ECO:0000250|UniProtKB:P12695}.
GO:0006086 pyruvate decarboxylation to acetyl-CoA
IBA
GO_REF:0000033 		ACCEPT
Summary: Oxidative decarboxylation of pyruvate to acetyl-CoA by PDH.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated FUNCTION states that the PDH complex, of which this protein is the E2 component, converts pyruvate to acetyl-CoA and CO2. The PAINT node is in the PDH E2 clade, so the IBA is sound.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
file:SCHPO/lat1/lat1-uniprot.txt
The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
GO:0006086 pyruvate decarboxylation to acetyl-CoA
IEA
GO_REF:0000002 		ACCEPT
Summary: Oxidative decarboxylation of pyruvate to acetyl-CoA by PDH.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated FUNCTION states that the PDH complex, of which this protein is the E2 component, converts pyruvate to acetyl-CoA and CO2.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
file:SCHPO/lat1/lat1-uniprot.txt
InterPro; IPR006257; LAT1.
GO:0016746 acyltransferase activity
IEA
GO_REF:0000002 		MODIFY
Summary: Generic InterPro-derived parent of the specific activity, which is already annotated.
Reason: Correct but general: by similarity to S. cerevisiae LAT1 (P12695) the acyltransferase activity is specifically the EC 2.3.1.12 dihydrolipoyllysine-residue acetyltransferase reaction, already annotated on this gene, and the InterPro hit is the 2-oxoacid dehydrogenase acyltransferase domain (PF00198).
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000250|UniProtKB:P12695};
file:SCHPO/lat1/lat1-uniprot.txt
Pfam; PF00198; 2-oxoacid_dh; 1.
file:SCHPO/lat1/lat1-uniprot.txt
The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
GO:0045254 pyruvate dehydrogenase complex
IBA
GO_REF:0000033 		ACCEPT
Summary: Component of the mitochondrial pyruvate dehydrogenase complex.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated FUNCTION lists dihydrolipoamide acetyltransferase (E2) as one of the three enzymatic components of the PDH complex, and the protein carries the mitochondrial PDH E2 family signature (IPR006257). The PAINT node is in the PDH E2 clade, so the IBA is sound.
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
file:SCHPO/lat1/lat1-uniprot.txt
InterPro; IPR006257; LAT1.
GO:0045254 pyruvate dehydrogenase complex
IEA
GO_REF:0000002 		ACCEPT
Summary: Component of the mitochondrial pyruvate dehydrogenase complex.
Reason: By similarity to S. cerevisiae LAT1 (P12695): the curated FUNCTION lists dihydrolipoamide acetyltransferase (E2) as one of the three enzymatic components of the PDH complex, and the protein carries the mitochondrial PDH E2 family signature (IPR006257).
Supporting Evidence:
file:SCHPO/lat1/lat1-uniprot.txt
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
file:SCHPO/lat1/lat1-uniprot.txt
InterPro; IPR006257; LAT1.

Core Functions

E2 acetyltransferase core of mitochondrial PDH.

Molecular Function:
dihydrolipoyllysine-residue acetyltransferase activity
Directly Involved In:
pyruvate decarboxylation to acetyl-CoA
Cellular Locations:
mitochondrial matrix
In Complex:
pyruvate dehydrogenase complex
Supporting Evidence:
  • file:SCHPO/lat1/lat1-uniprot.txt
    ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000250|UniProtKB:P12695};
  • file:SCHPO/lat1/lat1-uniprot.txt
    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
  • file:SCHPO/lat1/lat1-uniprot.txt
    The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
  • file:SCHPO/lat1/lat1-uniprot.txt
    Mitochondrion matrix {ECO:0000250|UniProtKB:P12695}.
  • file:SCHPO/lat1/lat1-uniprot.txt
    InterPro; IPR006257; LAT1.

References

Loading supporting content…

Download this section (compressed HTML)

📄 View Raw YAML

Loading supporting content…

Download this section (compressed HTML)