PCCB
entrez
5096
canonical
uniprot
P05166
canonical
ensembl
ENSG00000114054
resolver
ensp
ENSP00000251654
resolver
ensp
ENSP00000419027
resolver
ensp
ENSP00000548416
resolver
genesymbol
PCCB
resolver
hgnc
HGNC:8654
resolver
uniprot
B7Z2Z4
resolver
uniprot
Q16813
resolver
uniprot
Q96CX0
resolver
uniprot_entry
PCCB_HUMAN
resolver
uniprot_sec
B7Z2Z4
resolver
uniprot_sec
Q16813
resolver
uniprot_sec
Q96CX0
resolver
amino_acid_sequence
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
uniprot
proteins
disease_involvement
DISEASE: Propionic acidemia type II (PA-2) [MIM:606054]: Life-threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein. {ECO:0000269|PubMed:10447268, ECO:0000269|PubMed:11749052, ECO:0000269|PubMed:12189489, ECO:0000269|PubMed:12559849, ECO:0000269|PubMed:15059621, ECO:0000269|PubMed:15890657, ECO:0000269|PubMed:2154743, ECO:0000269|PubMed:8023851, ECO:0000269|PubMed:8411997, ECO:0000269|PubMed:9683601}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:15890657, PubMed:6765947). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:15890657, PubMed:6765947). 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). {ECO:0000250|UniProtKB:P79384, ECO:0000250|UniProtKB:Q168G2, ECO:0000269|PubMed:15890657, ECO:0000269|PubMed:6765947}.
uniprot
proteins
mass_dalton
58216
uniprot
proteins
pathway_participation
PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. {ECO:0000269|PubMed:15890657, ECO:0000269|PubMed:6765947}.
uniprot
proteins
protein_family
AccD/PCCB family
uniprot
proteins
pubmed
10447268
uniprot
proteins
pubmed
10502773
uniprot
proteins
pubmed
11749052
uniprot
proteins
pubmed
12189489
uniprot
proteins
pubmed
12559849
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15059621
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15890657
uniprot
proteins
pubmed
16023992
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
20725044
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2154743
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
3460076
uniprot
proteins
pubmed
6765947
uniprot
proteins
pubmed
8023851
uniprot
proteins
pubmed
8188292
uniprot
proteins
pubmed
8225321
uniprot
proteins
pubmed
8411997
uniprot
proteins
pubmed
9683601
uniprot
proteins
sequence_length
539
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:16023992}.
uniprot
proteins