Q6ZMR3 · LDH6A_HUMAN
- ProteinL-lactate dehydrogenase A-like 6A
- GeneLDHAL6A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids332 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the interconversion of L-lactate and pyruvate with nicotinamide adenine dinucleotide NAD+ as a coenzyme (PubMed:18351441).
Significantly increases the transcriptional activity of JUN, when overexpressed
Significantly increases the transcriptional activity of JUN, when overexpressed
Catalytic activity
- (S)-lactate + NAD+ = H+ + NADH + pyruvateThis reaction proceeds in the forward and the backward directions.
Pathway
Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 29-57 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSVGVACAISILLKGLSDELVLVDVDEGK | ||||||
Binding site | 99 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 106 | substrate | ||||
Sequence: R | ||||||
Binding site | 138 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 138 | substrate | ||||
Sequence: N | ||||||
Binding site | 169 | substrate | ||||
Sequence: R | ||||||
Active site | 193 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 248 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrion | |
Molecular Function | L-lactate dehydrogenase activity | |
Biological Process | lactate metabolic process | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-lactate dehydrogenase A-like 6A
- EC number
- Short namesLDHA-like protein 6A
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6ZMR3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 413 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000168457 | 2-332 | UniProt | L-lactate dehydrogenase A-like 6A | |||
Sequence: ATIKSELIKNFAEEEAIHHNKISIVGTGSVGVACAISILLKGLSDELVLVDVDEGKLKGETMDLQHGSPFMKMPNIVSSKDYLVTANSNLVIITAGARQKKGETRLDLVQRNVSIFKLMIPNITQYSPHCKLLIVTNPVDILTYVAWKLSGFPKNRVIGSGCNLDSARFRYFIGQRLGIHSESCHGLILGEHGDSSVPVWSGVNIAGVPLKDLNPDIGTDKDPEQWENVHKKVISSGYEMVKMKGYTSWGISLSVADLTESILKNLRRVHPVSTLSKGLYGINEDIFLSVPCILGENGITDLIKVKLTLEEEACLQKSAETLWEIQKELKL | |||||||
Modified residue | 5 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 5 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 57 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 57 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 81 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 118 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 118 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 239 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 243 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 309 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 318 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 318 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 322 | UniProt | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Testis-specific.
Gene expression databases
Organism-specific databases
Structure
Sequence
- Sequence statusComplete
- Length332
- Mass (Da)36,507
- Last updated2004-07-05 v1
- Checksum7C1B9FCAE9050A9B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY581313 EMBL· GenBank· DDBJ | AAS93432.1 EMBL· GenBank· DDBJ | mRNA | ||
AK131523 EMBL· GenBank· DDBJ | BAD18662.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68387.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68388.1 EMBL· GenBank· DDBJ | Genomic DNA |