PCCB_RAT
ID PCCB_RAT Reviewed; 541 AA.
AC P07633;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Propionyl-CoA carboxylase beta chain, mitochondrial {ECO:0000305|PubMed:3464942};
DE Short=PCCase subunit beta;
DE EC=6.4.1.3 {ECO:0000250|UniProtKB:P05166};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN Name=Pccb {ECO:0000312|RGD:3265};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3464942; DOI=10.1073/pnas.83.21.8049;
RA Kraus J.P., Firgaira F., Novotny J., Kalousek F., Williams K.R.,
RA Williamson C., Ohura T., Rosenberg L.E.;
RT "Coding sequence of the precursor of the beta subunit of rat propionyl-CoA
RT carboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8049-8053(1986).
CC -!- FUNCTION: This is one of the 2 subunits of the biotin-dependent
CC propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the
CC catabolism of odd chain fatty acids, branched-chain amino acids
CC isoleucine, threonine, methionine, and valine and other metabolites.
CC Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-
CC CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By
CC similarity). Within the holoenzyme, the alpha subunit catalyzes the
CC ATP-dependent carboxylation of the biotin carried by the biotin
CC carboxyl carrier (BCC) domain, while the beta subunit then transfers
CC the carboxyl group from carboxylated biotin to propionyl-CoA (By
CC similarity). Propionyl-CoA carboxylase also significantly acts on
CC butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-
CC ethylmalonyl-CoA (By similarity). Other alternative minor substrates
CC include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
CC {ECO:0000250|UniProtKB:P05166, ECO:0000250|UniProtKB:P79384,
CC ECO:0000250|UniProtKB:Q168G2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-
CC CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456216; EC=6.4.1.3;
CC Evidence={ECO:0000250|UniProtKB:P05166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000250|UniProtKB:P05166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoyl-CoA + hydrogencarbonate = (2S)-ethylmalonyl-CoA
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:59520, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P79384};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000250|UniProtKB:P79384};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000250|UniProtKB:P05166}.
CC -!- SUBUNIT: The holoenzyme is a dodecamer composed of 6 PCCA/alpha
CC subunits and 6 PCCB/beta subunits. {ECO:0000250|UniProtKB:P05166}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P05166}.
CC -!- DOMAIN: The beta subunit contains the carboxyl transferase (CT) domain.
CC {ECO:0000250|UniProtKB:Q168G2}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; M14634; AAA41818.1; -; mRNA.
DR PIR; A25516; A25516.
DR AlphaFoldDB; P07633; -.
DR SMR; P07633; -.
DR IntAct; P07633; 1.
DR STRING; 10116.ENSRNOP00000021657; -.
DR iPTMnet; P07633; -.
DR PhosphoSitePlus; P07633; -.
DR jPOST; P07633; -.
DR PaxDb; P07633; -.
DR PRIDE; P07633; -.
DR UCSC; RGD:3265; rat.
DR RGD; 3265; Pccb.
DR eggNOG; KOG0540; Eukaryota.
DR InParanoid; P07633; -.
DR PhylomeDB; P07633; -.
DR BioCyc; MetaCyc:MON-8607; -.
DR Reactome; R-RNO-196780; Biotin transport and metabolism.
DR Reactome; R-RNO-71032; Propionyl-CoA catabolism.
DR UniPathway; UPA00945; UER00908.
DR PRO; PR:P07633; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; ISS:UniProtKB.
DR GO; GO:0009063; P:cellular amino acid catabolic process; TAS:RGD.
DR GO; GO:0009062; P:fatty acid catabolic process; TAS:RGD.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..541
FT /note="Propionyl-CoA carboxylase beta chain, mitochondrial"
FT /id="PRO_0000000296"
FT DOMAIN 34..292
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 296..535
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 34..535
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 327..360
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05166"
FT MOD_RES 101
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 101
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 250
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 476
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 476
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 491
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 491
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
SQ SEQUENCE 541 AA; 58626 MW; 052E668E9EE23524 CRC64;
MAAVIRIRAM AAGTRLRVLN CGLGTTIRSL CSQPVSVNER IENKRHAALL GGGQRRIDAQ
HKRGKLTARE RISLLLDPGS FLESDMFVEH RCADFGMAAE KNKFPGDSVV TGRGRINGRL
VYVFSQDFTV FGGSLSGAHA QKICKIMDQA ITVGAPVIGL NDSGGARIQE GVESLAGYAD
IFLRNVTASG VIPQISLIMG PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EFVKSVTNED
VTQEQLGGAK THTTVSGVAH RAFDNDVDAL CNLREFLNFL PLSNQDPASI RECHDPSDRL
VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPNYAK NIVIGFARMN GRTVGIVGNQ
PNVASGCLDI NSSVKGARFV RFCDAFSIPL ITFVDVPGFL PGTAQEYGGI IRHGAKLLYA
FAEATVPKIT VITRKAYGGA YDVMSSKHLL GDTNYAWPTA EIAVMGAKGA VEIIFKGHED
VEAAQAEYVE KFANPFPAAV RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANVP
L
