Pcca
entrez
110821
canonical
uniprot
Q91ZA3
canonical
ensembl
ENSMUSG00000041650
resolver
ensp
ENSMUSP00000038763
resolver
ensp
ENSMUSP00000237634
resolver
ensp
ENSMUSP00000237635
resolver
ensp
ENSMUSP00000237638
resolver
ensp
ENSMUSP00000237639
resolver
enst
ENSMUST00000038374
resolver
genesymbol
Pcca
resolver
uniprot
Q3UGC8
resolver
uniprot
Q80VU5
resolver
uniprot
Q922N3
resolver
uniprot_entry
PCCA_MOUSE
resolver
uniprot_entry
Q3UGC8_MOUSE
resolver
uniprot_sec
Q80VU5
resolver
uniprot_sec
Q922N3
resolver
amino_acid_sequence
MAGQWVRTVALLAARRHWRRSSQQQLLGTLKHAPVYSYQCLVVSRSLSSVEYEPKEKTFDKILIANRGEIACRVIKTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFAKRLAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDPETRQAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLRHKQEDIPISGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPIHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEALKRMEDALDNYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSDVYPDGFKGHTLTLSERNQLLAIASSVFVASQLRAQRFQEHSRVPVIRPDVAKWELSVKLHDEDHTVVASNNGPAFTVEVDGSKLNVTSTWNLASPLLSVNVDGTQRTVQCLSREAGGNMSIQFLGTVYKVHILTKLAAELNKFMLEKVPKDTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE
uniprot
proteins
disease_involvement
DISEASE: Note=Propionic acidemia due to recessively inherited deficiency of PCCase activity often causes life-threatening ketosis and acidosis.
uniprot
proteins
ec_number
6.4.1.3
uniprot
proteins
function
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. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). 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 (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity). {ECO:0000250|UniProtKB:P05165, ECO:0000250|UniProtKB:P0DTA4, ECO:0000250|UniProtKB:Q5LUF3}.
uniprot
proteins
mass_dalton
79922
uniprot
proteins
pathway_participation
PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. {ECO:0000250|UniProtKB:P05165}.
uniprot
proteins
post_translational_modification
PTM: Acetylated. {ECO:0000269|PubMed:23438705}.; PTM: The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity. Biotinylation is catalyzed by HLCS. {ECO:0000250|UniProtKB:P05165}.
uniprot
proteins
pubmed
11461925
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23438705
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
724
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P05165}.
uniprot
proteins