Overview
| Uniprot ID | Q8N0X4 |
|---|
| Protein Name | Citramalyl-CoA lyase, mitochondrial |
|---|
| Gene Name | CLYBL |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 156 |
DKFSFHLKGRKLEQP |
| 338 |
VTLATSIKEK***** |
| 57 |
YVPGNDEKKIKKIPS |
Function
Mitochondrial enzyme required to detoxify vitamin B12-poisoning metabolites (PubMed:29056341, PubMed:40108300). Acts as a citramalyl-CoA lyase by converting citramalyl-CoA into acetyl-CoA and pyruvate in the C5-dicarboxylate catabolism pathway, a pathway required to detoxify itaconate, a vitamin B12-poisoning metabolite (PubMed:29056341). Also acts as a malyl-CoA thioesterase to detoxify malyl-CoA, a side product of citric acid cycle enzymes, which is toxic for the vitamin B12-dependent enzyme MMUT (PubMed:40108300). Also acts as a malate synthase in vitro, converting glyoxylate and acetyl-CoA to malate (PubMed:24334609, PubMed:29056341). Also acts as a beta-methylmalate synthase in vitro, by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (PubMed:24334609, PubMed:29056341). Also has very weak citramalate synthase activity in vitro (PubMed:24334609, PubMed:29056341)
Protein Sequence
10
MALRLLRRAA
20
RGAAAAALLR
30
LKASLAADIP
40
RLGYSSSSHH
50
KYIPRRAVLY
60
VPGNDEKKIK
70
KIPSLNVDCA
80
VLDCEDGVAA
90
NKKNEARLRI
100
VKTLEDIDLG
110
PTEKCVRVNS
120
VSSGLAEEDL
130
ETLLQSRVLP
140
SSLMLPKVES
150
PEEIQWFADK
160
FSFHLKGRKL
170
EQPMNLIPFV
180
ETAMGLLNFK
190
AVCEETLKVG
200
PQVGLFLDAV
210
VFGGEDFRAS
220
IGATSSKETL
230
DILYARQKIV
240
VIAKAFGLQA
250
IDLVYIDFRD
260
GAGLLRQSRE
270
GAAMGFTGKQ
280
VIHPNQIAVV
290
QEQFSPSPEK
300
IKWAEELIAA
310
FKEHQQLGKG
320
AFTFQGSMID
330
MPLLKQAQNT
340
VTLATSIKEK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Molecular Function |
GO:0047777 |
(S)-citramalyl-CoA lyase activity |
| Molecular Function |
GO:0016289 |
acyl-CoA hydrolase activity |
| Molecular Function |
GO:0000287 |
magnesium ion binding |
| Molecular Function |
GO:0004474 |
malate synthase activity |
| Biological Process |
GO:0106121 |
positive regulation of cobalamin metabolic process |
| Biological Process |
GO:0070207 |
protein homotrimerization |
| Biological Process |
GO:0106064 |
regulation of cobalamin metabolic process |
| Biological Process |
GO:0110052 |
toxic metabolite repair |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.