Search Results

Overview

Uniprot IDP05165
Protein NamePropionyl-CoA carboxylase alpha chain, mitochondrial
Gene NamePCCA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
150 YGFLSENKEFARCLA
186 ESKLLAKKAEVNTIP
200 PGFDGVVKDAEEAVR
219 IGYPVMIKASAGGGG
227 ASAGGGGKGMRIAWD
328 VALARAVKYSSAGTV
342 VEFLVDSKKNFYFLE
385 KGYPLRHKQADIRIN
496 IINSRFVKGDISTKF
519 FKGHMLTKSEKNQLL

Function

This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:6765947, PubMed:8434582). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:10101253, PubMed:6765947, PubMed:8434582). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate (PubMed:6765947). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity)

Protein Sequence

10 MAGFWVGTAP 20 LVAAGRRGRW 30 PPQQLMLSAA 40 LRTLKHVLYY 50 SRQCLMVSRN 60 LGSVGYDPNE 70 KTFDKILVAN 80 RGEIACRVIR 90 TCKKMGIKTV 100 AIHSDVDASS 110 VHVKMADEAV 120 CVGPAPTSKS 130 YLNMDAIMEA 140 IKKTRAQAVH 150 PGYGFLSENK 160 EFARCLAAED 170 VVFIGPDTHA 180 IQAMGDKIES 190 KLLAKKAEVN 200 TIPGFDGVVK 210 DAEEAVRIAR 220 EIGYPVMIKA 230 SAGGGGKGMR 240 IAWDDEETRD 250 GFRLSSQEAA 260 SSFGDDRLLI 270 EKFIDNPRHI 280 EIQVLGDKHG 290 NALWLNEREC 300 SIQRRNQKVV 310 EEAPSIFLDA 320 ETRRAMGEQA 330 VALARAVKYS 340 SAGTVEFLVD 350 SKKNFYFLEM 360 NTRLQVEHPV 370 TECITGLDLV 380 QEMIRVAKGY 390 PLRHKQADIR 400 INGWAVECRV 410 YAEDPYKSFG 420 LPSIGRLSQY 430 QEPLHLPGVR 440 VDSGIQPGSD 450 ISIYYDPMIS 460 KLITYGSDRT 470 EALKRMADAL 480 DNYVIRGVTH 490 NIALLREVII 500 NSRFVKGDIS 510 TKFLSDVYPD 520 GFKGHMLTKS 530 EKNQLLAIAS 540 SLFVAFQLRA 550 QHFQENSRMP 560 VIKPDIANWE 570 LSVKLHDKVH 580 TVVASNNGSV 590 FSVEVDGSKL 600 NVTSTWNLAS 610 PLLSVSVDGT 620 QRTVQCLSRE 630 AGGNMSIQFL 640 GTVYKVNILT 650 RLAAELNKFM 660 LEKVTEDTSS 670 VLRSPMPGVV 680 VAVSVKPGDA 690 VAEGQEICVI 700 EAMKMQNSMT 710 AGKTGTVKSV 720 HCQAGDTVGE GDLLVELE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Biological Process GO:0009081 branched-chain amino acid metabolic process
Biological Process GO:0006631 fatty acid metabolic process
Biological Process GO:0019626 short-chain fatty acid catabolic process
Biological Process GO:1901290 succinyl-CoA biosynthetic process
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0009374 biotin binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0004658 propionyl-CoA carboxylase activity

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] 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.