PCCB_BOVIN
ID PCCB_BOVIN Reviewed; 539 AA.
AC Q2TBR0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Propionyl-CoA carboxylase beta chain, mitochondrial {ECO:0000305|PubMed:14398975};
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:0000250|UniProtKB:P05166};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=14398975;
RA Halenz D.R., Lane M.D.;
RT "Properties and purification of mitochondrial propionyl carboxylase.";
RL J. Biol. Chem. 235:878-884(1960).
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:0000305|PubMed:14398975}.
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; BC109784; AAI09785.1; -; mRNA.
DR RefSeq; NP_001033637.1; NM_001038548.2.
DR AlphaFoldDB; Q2TBR0; -.
DR SMR; Q2TBR0; -.
DR BioGRID; 172525; 1.
DR STRING; 9913.ENSBTAP00000020252; -.
DR PaxDb; Q2TBR0; -.
DR PeptideAtlas; Q2TBR0; -.
DR PRIDE; Q2TBR0; -.
DR GeneID; 515902; -.
DR KEGG; bta:515902; -.
DR CTD; 5096; -.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_6_0_1; -.
DR InParanoid; Q2TBR0; -.
DR OrthoDB; 402617at2759; -.
DR TreeFam; TF314350; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000009136; Unplaced.
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 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..539
FT /note="Propionyl-CoA carboxylase beta chain, mitochondrial"
FT /id="PRO_0000284067"
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; 58311 MW; F6CB6C7BB3328CB8 CRC64;
MAAAMRVAVA GARLSVVLRS LRGAGRSLCT QPVSVNERIE NKRQAALLGG GQRRIDAQHK
RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN KFPGDSVVTG RGRINGRLVY
VFSQDFTVFG GSLSGAHAQK ICKIMDQALT VGAPVIGLND SGGARIQEGV ESLAGYADIF
LRNVTASGVI PQISLIMGPC AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT
QEELGGARTH TTMSGVAHRA FENDVDALCN LREFFNYLPL SNQDPAPVLE CHDPSDRLVP
ELDTIVPLES TKAYNMVDII HAVVDEREFF EIMPNYAKNI IVGFARMNGR TVGIVGNQPK
VASGCLDINS SVKGARFVRF CDSFNIPLIT FVDVPGFLPG TAQEYGGIIR HGAKLLYAFA
EATVPKVTVI TRKAYGGAYD VMSSKHLCGD TNYAWPTAEI AVMGAKGAVE IIFKGHENVE
AAQAEYIEKF ANPFPAAVRG FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL
