PCCA_CAEEL
ID PCCA_CAEEL Reviewed; 724 AA.
AC Q19842;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial {ECO:0000305|PubMed:9851916};
DE Short=PCCase subunit alpha;
DE EC=6.4.1.3 {ECO:0000250|UniProtKB:P05165};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit alpha;
DE Flags: Precursor;
GN Name=pcca-1; ORFNames=F27D9.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP PROTEIN SEQUENCE OF 330-339; 386-402; 452-472; 482-488; 526-534; 537-545;
RP 549-556; 618-626; 634-641 AND 650-667, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [3]
RP INTERACTION WITH SIR-2.2 AND SIR-2.3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
RA Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
RA Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
RT "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals
RT interact with pyruvate carboxylase and other acetylated biotin-dependent
RT carboxylases.";
RL Mitochondrion 13:705-720(2013).
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:P05165, ECO:0000250|UniProtKB:P0DTA4,
CC ECO:0000250|UniProtKB:Q5LUF3}.
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:P05165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000250|UniProtKB:P05165};
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:P0DTA4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000250|UniProtKB:P0DTA4};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000250|UniProtKB:P05165}.
CC -!- SUBUNIT: The holoenzyme is a dodecamer composed of 6 alpha subunits and
CC 6 beta subunits (By similarity). Interacts with sir-2.2 and sir-2.3
CC (PubMed:23438705). {ECO:0000250|UniProtKB:P05165,
CC ECO:0000269|PubMed:23438705}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P05165}.
CC -!- DOMAIN: Consists of an N-terminal biotin carboxylation/carboxylase (BC)
CC domain that catalyzes the transient carboxylation of the biotin
CC covalently attached to the C-terminal biotinyl-binding/biotin carboxyl
CC carrier (BCC) domain. {ECO:0000250|UniProtKB:Q5LUF3}.
CC -!- PTM: The biotin cofactor is covalently attached to the C-terminal
CC biotinyl-binding domain and is required for the catalytic activity.
CC {ECO:0000250|UniProtKB:P05165}.
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DR EMBL; FO080935; CCD67920.1; -; Genomic_DNA.
DR PIR; T16187; T16187.
DR RefSeq; NP_509293.1; NM_076892.4.
DR AlphaFoldDB; Q19842; -.
DR SMR; Q19842; -.
DR BioGRID; 45950; 18.
DR STRING; 6239.F27D9.5; -.
DR World-2DPAGE; 0011:Q19842; -.
DR EPD; Q19842; -.
DR PaxDb; Q19842; -.
DR PeptideAtlas; Q19842; -.
DR EnsemblMetazoa; F27D9.5.1; F27D9.5.1; WBGene00017864.
DR GeneID; 181026; -.
DR KEGG; cel:CELE_F27D9.5; -.
DR UCSC; F27D9.5; c. elegans.
DR CTD; 181026; -.
DR WormBase; F27D9.5; CE04451; WBGene00017864; pcca-1.
DR eggNOG; KOG0238; Eukaryota.
DR GeneTree; ENSGT00940000156083; -.
DR HOGENOM; CLU_000395_3_3_1; -.
DR InParanoid; Q19842; -.
DR OMA; ITHFHTP; -.
DR OrthoDB; 254436at2759; -.
DR PhylomeDB; Q19842; -.
DR BRENDA; 6.4.1.3; 1045.
DR Reactome; R-CEL-196780; Biotin transport and metabolism.
DR Reactome; R-CEL-71032; Propionyl-CoA catabolism.
DR UniPathway; UPA00945; UER00908.
DR PRO; PR:Q19842; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017864; Expressed in embryo and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR041265; PCC_BT.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18140; PCC_BT; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biotin; Direct protein sequencing; Ligase; Lipid degradation;
KW Lipid metabolism; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..724
FT /note="Propionyl-CoA carboxylase alpha chain,
FT mitochondrial"
FT /id="PRO_0000234102"
FT DOMAIN 48..495
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 167..364
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 649..724
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 339
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P05165"
FT BINDING 195..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P05165"
FT BINDING 282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P05165"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 337
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 395
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:Q5LUF3"
FT MOD_RES 690
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05165,
FT ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 724 AA; 79762 MW; E09832FB65AABA45 CRC64;
MLRAASSIRA VANRGLATAA VARPGVPLDE REGKEIYTTV GIDYNEPKFD KILIANRGEI
ACRVIKTARA MGIKTVAVHS DVDSNSLHVK MADEAVCVGE APTAKSYLRA DRILQAVEDT
GAQAVHPGYG FLSENTKFAA ELEKAGAKFI GPNSKAILDM GDKIHSKKIA TAARVSMIPG
YDGEIADEDM CVKVSRDIGY PVMIKASAGG GGKGMRVAWN DKQAREGYRL SKQEAASSFG
DDRMLVEKFI DNPRHIEMQV LCDKHGNALW LNERECSIQR RNQKVIEEAP SSFVPPEMRR
KMGEQAVQLA KAVGYDSAGT VEFLVDSQRN FYFLEMNTRL QVEHPITECI TGIDIVQQML
RVSYGHPLPI TQEQVPLNGW AFESRVYAED PYKGFGLPSV GRLSRYVEPK HVDGVRCDSG
IREGSEISIY YDPLICKLVT HGDNREQALN RMQEALDNYV IRGVTHNIPL LRDIVQEKRF
RTGDITTKYL PEVYPEGFQG TSLSPKEQDV VIAFASALNA RKLARANQFL NQNKQRSTHV
ASFSKTYKFV SSLPVKEGER PTEHAVEVEF VEGSANKAQV RIGGKTVTIS GDLNLSHPVN
SIEVDGEHIT TQIVGKRAGE ITVLYKGTPF KVKVLPEQAV KYLQYMKEKA KVDLSTVVLS
PMPGAIKNVN VKPGDMVSEG QELVVMEAMK MQNSLHAGKT GRVKAVNVKV GATVDEGEVL
VELE
