PCCB_PIG
ID PCCB_PIG Reviewed; 539 AA.
AC P79384;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Propionyl-CoA carboxylase beta chain, mitochondrial {ECO:0000305|PubMed:13752080};
DE Short=PCCase subunit beta;
DE EC=6.4.1.3 {ECO:0000269|PubMed:13752080};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN Name=PCCB {ECO:0000250|UniProtKB:P05166};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kimura M., Kawakami K., Suzuki H., Hamasima N.;
RT "Cloning of the pig propionyl-CoA carboxylase beta chain precursor gene.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=13752080;
RA Kaziro Y., Ochoa S., Warner R.C., Chen J.Y.;
RT "Metabolism of propionic acid in animal tissues. VIII. Crystalline
RT propionyl carboxylase.";
RL J. Biol. Chem. 236:1917-1923(1961).
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 (PubMed:13752080). Propionyl-CoA carboxylase catalyzes the
CC carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-
CC CoA/(S)-methylmalonyl-CoA (PubMed:13752080). Within the holoenzyme, the
CC alpha subunit catalyzes the ATP-dependent carboxylation of the biotin
CC carried by the biotin carboxyl carrier (BCC) domain, while the beta
CC subunit then transfers the carboxyl group from carboxylated biotin to
CC propionyl-CoA (By similarity). Propionyl-CoA carboxylase also
CC significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to
CC ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate
CC (PubMed:13752080). Other alternative minor substrates include (2E)-
CC butenoyl-CoA/crotonoyl-CoA (PubMed:13752080).
CC {ECO:0000250|UniProtKB:Q168G2, ECO:0000269|PubMed:13752080}.
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:0000269|PubMed:13752080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000305|PubMed:13752080};
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:0000305|PubMed:13752080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000305|PubMed:13752080};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for propanoyl-CoA {ECO:0000269|PubMed:13752080};
CC KM=1.5 mM for butanoyl-CoA {ECO:0000269|PubMed:13752080};
CC pH dependence:
CC Optimum pH is 8.0-8.2 for the propionyl-CoA carboxylase activity as
CC measured with the holoenzyme. {ECO:0000269|PubMed:13752080};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000269|PubMed:13752080}.
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:0000305|PubMed:13752080}.
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; AB000886; BAA19203.1; -; mRNA.
DR RefSeq; NP_999066.1; NM_213901.1.
DR AlphaFoldDB; P79384; -.
DR SMR; P79384; -.
DR STRING; 9823.ENSSSCP00000012423; -.
DR PaxDb; P79384; -.
DR PeptideAtlas; P79384; -.
DR PRIDE; P79384; -.
DR Ensembl; ENSSSCT00040056794; ENSSSCP00040023610; ENSSSCG00040041330.
DR Ensembl; ENSSSCT00065035648; ENSSSCP00065014918; ENSSSCG00065026480.
DR Ensembl; ENSSSCT00070021372; ENSSSCP00070017669; ENSSSCG00070010911.
DR GeneID; 100158147; -.
DR KEGG; ssc:100158147; -.
DR CTD; 5096; -.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_6_0_1; -.
DR InParanoid; P79384; -.
DR OMA; YAYAECT; -.
DR OrthoDB; 402617at2759; -.
DR TreeFam; TF314350; -.
DR Reactome; R-SSC-196780; Biotin transport and metabolism.
DR Reactome; R-SSC-71032; Propionyl-CoA catabolism.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 13.
DR Genevisible; P79384; SS.
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; IDA:UniProtKB.
DR GO; GO:0019626; P:short-chain fatty acid catabolic process; IC:UniProtKB.
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 1: Evidence at protein 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..539
FT /note="Propionyl-CoA carboxylase beta chain, mitochondrial"
FT /id="PRO_0000000295"
FT DOMAIN 32..290
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 294..533
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 32..533
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 325..358
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05166"
FT MOD_RES 99
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 99
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 474
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 474
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 489
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
FT MOD_RES 489
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MN9"
SQ SEQUENCE 539 AA; 58590 MW; 756014F5C357E9DB CRC64;
MAAAVRVTAA RARLRVVVRS LHAGVRSLCT QPVSVNERIE NKRQAALLGG GQRRIDSQHK
RGKLTARERI SLLLDPGSFI ESDMFVEHRC ADFGMAADKN KFPGDSVVTG RGRINGRLVY
VFSQDFTVFG GSLSGAHAQK ICKIMDQAMT VGAPVIGLND SGGARIQEGV ESLAGYADIF
LRNVSASGVI PQISLIMGPC AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT
QEELGGARTH TTMSGVAHRA FDNDVDALCN LREFFNYLPL SNQDPAPIRE CHDPSDRLVP
ELDTVVPLES TRAYDMVDII YSIVDERDFF EIMPNYAKNI IVGFARMNGR TVGIVGNQPK
VASGCLDINS SVKGARFVRF CDAFNIPLIT FVDVPGFLPG TAQEYGGIIR HGAKLLYAFA
EATVPKITVI TRKAYGGAYD VMSSKHLCGD TNYAWPTAEI AVMGAKGAVE IIFKGHENVE
AAQAEYIEKF ANPFPAAVRG FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL
