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Database: UniProt
Entry: Q19842
LinkDB: Q19842
Original site: Q19842 
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   16-JAN-2019, entry version 146.
DE   RecName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial;
DE            Short=PCCase subunit alpha;
DE            EC=6.4.1.3;
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 330-339; 386-402; 452-472; 482-488; 526-534;
RP   537-545; 549-556; 618-626; 634-641 AND 650-667, AND IDENTIFICATION BY
RP   MASS 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
RT   mammals interact with pyruvate carboxylase and other acetylated
RT   biotin-dependent carboxylases.";
RL   Mitochondrion 13:705-720(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-
CC         methylmalonyl-CoA + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327,
CC         ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P05165};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:P11154};
CC   -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA
CC       degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
CC   -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
CC       alpha subunits and six beta subunits (By similarity). Interacts
CC       with sir-2.2 and sir-2.3 (PubMed:23438705).
CC       {ECO:0000250|UniProtKB:P05165, ECO:0000269|PubMed:23438705}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
DR   EMBL; FO080935; CCD67920.1; -; Genomic_DNA.
DR   PIR; T16187; T16187.
DR   RefSeq; NP_509293.1; NM_076892.4.
DR   UniGene; Cel.6797; -.
DR   ProteinModelPortal; Q19842; -.
DR   SMR; Q19842; -.
DR   STRING; 6239.F27D9.5.2; -.
DR   World-2DPAGE; 0011:Q19842; -.
DR   EPD; Q19842; -.
DR   PaxDb; Q19842; -.
DR   PeptideAtlas; Q19842; -.
DR   PRIDE; Q19842; -.
DR   EnsemblMetazoa; F27D9.5.1; F27D9.5.1; WBGene00017864.
DR   EnsemblMetazoa; F27D9.5.2; F27D9.5.2; 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   eggNOG; COG4770; LUCA.
DR   GeneTree; ENSGT00940000156083; -.
DR   HOGENOM; HOG000008989; -.
DR   InParanoid; Q19842; -.
DR   KO; K01965; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 254436at2759; -.
DR   PhylomeDB; Q19842; -.
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 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; 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   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; Complete proteome; Direct protein sequencing;
KW   Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    724       Propionyl-CoA carboxylase alpha chain,
FT                                mitochondrial.
FT                                /FTId=PRO_0000234102.
FT   DOMAIN       48    495       Biotin carboxylation. {ECO:0000255}.
FT   DOMAIN      167    364       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      649    724       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    339    339       {ECO:0000250|UniProtKB:P05165}.
FT   BINDING     163    163       ATP. {ECO:0000250|UniProtKB:P05165}.
FT   BINDING     247    247       ATP. {ECO:0000250|UniProtKB:P05165}.
FT   BINDING     282    282       ATP. {ECO:0000250|UniProtKB:P05165}.
FT   MOD_RES     690    690       N6-biotinyllysine. {ECO:0000250,
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
//
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