Search Results

Overview

Uniprot IDQ9P2R7
Protein NameSuccinate--CoA ligase [ADP-forming] subunit beta, mitochondrial
Gene NameSUCLA2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
108 VLAGGRGKGTFESGL
116 GTFESGLKGGVKIVF
120 SGLKGGVKIVFSPEE
129 VFSPEEAKAVSSQMI
143 IGKKLFTKQTGEKGR
215 IDIEEGIKKEQALQL
216 DIEEGIKKEQALQLA
287 NSAYRQKKIFDLQDW
302 TQEDERDKDAAKANL
368 FKLITSDKKVLAILV
401 AVKDLEIKIPVVVRL
417 GTRVDDAKALIADSG
451 SEIVTLAKQAHVDVK
78 VPKGYVAKSPDEAYA
88 DEAYAIAKKLGSKDV
89 EAYAIAKKLGSKDVV
93 IAKKLGSKDVVIKAQ

Function

ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA (PubMed:15877282, PubMed:34492704, PubMed:40108300). The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity). Also able to act as an ATP-specific itaconyl- and malyl-CoA synthetase (PubMed:40108300)

Protein Sequence

10 MAASMFYGRL 20 VAVATLRNHR 30 PRTAQRAAAQ 40 VLGSSGLFNN 50 HGLQVQQQQQ 60 RNLSLHEYMS 70 MELLQEAGVS 80 VPKGYVAKSP 90 DEAYAIAKKL 100 GSKDVVIKAQ 110 VLAGGRGKGT 120 FESGLKGGVK 130 IVFSPEEAKA 140 VSSQMIGKKL 150 FTKQTGEKGR 160 ICNQVLVCER 170 KYPRREYYFA 180 ITMERSFQGP 190 VLIGSSHGGV 200 NIEDVAAESP 210 EAIIKEPIDI 220 EEGIKKEQAL 230 QLAQKMGFPP 240 NIVESAAENM 250 VKLYSLFLKY 260 DATMIEINPM 270 VEDSDGAVLC 280 MDAKINFDSN 290 SAYRQKKIFD 300 LQDWTQEDER 310 DKDAAKANLN 320 YIGLDGNIGC 330 LVNGAGLAMA 340 TMDIIKLHGG 350 TPANFLDVGG 360 GATVHQVTEA 370 FKLITSDKKV 380 LAILVNIFGG 390 IMRCDVIAQG 400 IVMAVKDLEI 410 KIPVVVRLQG 420 TRVDDAKALI 430 ADSGLKILAC 440 DDLDEAARMV 450 VKLSEIVTLA 460 KQAHVDVKFQ LPI

Gene Ontology

Classification GO ID Description
Cellular Component GO:1902494 catalytic complex
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0042709 succinate-CoA ligase complex
Cellular Component GO:0009361 succinate-CoA ligase complex (ADP-forming)
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0050074 malate-CoA ligase activity
Molecular Function GO:0004775 succinate-CoA ligase (ADP-forming) activity
Biological Process GO:0006108 malate metabolic process
Biological Process GO:0006105 succinate metabolic process
Biological Process GO:1901289 succinyl-CoA catabolic process
Biological Process GO:0006104 succinyl-CoA metabolic process
Biological Process GO:0006781 succinyl-CoA pathway
Biological Process GO:0110052 toxic metabolite repair
Biological Process GO:0006099 tricarboxylic acid cycle

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.

[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.