GenomeNet

Database: UniProt
Entry: Q612F5
LinkDB: Q612F5
Original site: Q612F5 
ID   PCCA_CAEBR              Reviewed;         738 AA.
AC   Q612F5; A8XPR3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   16-JAN-2019, entry version 97.
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=CBG16755;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A.,
RA   D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
RA   Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
RA   Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
RA   Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
RA   Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
RA   Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for
RT   comparative genomics.";
RL   PLoS Biol. 1:166-192(2003).
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. Interacts with sir-2.2.
CC       {ECO:0000250|UniProtKB:P05165, ECO:0000250|UniProtKB:Q19842}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
DR   EMBL; HE600942; CAP34639.1; -; Genomic_DNA.
DR   RefSeq; XP_002645081.1; XM_002645035.1.
DR   ProteinModelPortal; Q612F5; -.
DR   SMR; Q612F5; -.
DR   STRING; 6238.CBG16755; -.
DR   EnsemblMetazoa; CBG16755; CBG16755; WBGene00036608.
DR   GeneID; 8587079; -.
DR   KEGG; cbr:CBG16755; -.
DR   CTD; 8587079; -.
DR   WormBase; CBG16755; CBP18815; WBGene00036608; Cbr-pcca-1.
DR   eggNOG; KOG0238; Eukaryota.
DR   eggNOG; COG4770; LUCA.
DR   HOGENOM; HOG000008989; -.
DR   InParanoid; Q612F5; -.
DR   KO; K01965; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 254436at2759; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000008549; Chromosome X.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   ATP-binding; Biotin; Complete proteome; Ligase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    738       Propionyl-CoA carboxylase alpha chain,
FT                                mitochondrial.
FT                                /FTId=PRO_0000234101.
FT   DOMAIN       62    509       Biotin carboxylation. {ECO:0000255}.
FT   DOMAIN      181    378       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      663    738       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    353    353       {ECO:0000250|UniProtKB:P05165}.
FT   BINDING     177    177       ATP. {ECO:0000250|UniProtKB:P05165}.
FT   BINDING     261    261       ATP. {ECO:0000250|UniProtKB:P05165}.
FT   BINDING     296    296       ATP. {ECO:0000250|UniProtKB:P05165}.
FT   MOD_RES     704    704       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   738 AA;  81477 MW;  5CDA6528D16D64A1 CRC64;
     MLRAASNFRA VANREFACAK RQLSKTTRKN ATAAATRPGV PRDEREGKEI YTTVGIDHNE
     PKFDKILIAN RGEIACRVIK TAKAMGIKTV AVHSDVDSNS LHVKMADEAI CVGEAPTAKS
     YLRVDRILQA VEDTGAQAVH PGYGFLSENT KFAAELEKAG AKFIGPNSKA ILDMGDKIHS
     KKIATAARVS MIPGYDGEIP EEDFCVKVSR EIGYPVMIKA SAGGGGKGMR VAWNDKQARE
     GYRLSKQEAA SSFGDDRMLV EKFIDNPRHI EMQILCDKHG NALWLNEREC SIQRRNQKVI
     EEAPSSFVPP EMRRKMGEQA VQLAKAVGYD SAGTVEFLVD SQRNFYFLEM NTRLQVEHPI
     TECITGIDIV QQMLRVAYGH SLPLTQEQVP LNGWAFESRV YAEDPYKGFG LPSVGRLSKY
     VEPRHVDGVR CDSGIREGSE ISIYYDPLIC KLVTHGDNRQ QALDRMQEAL DNYVIRGVTH
     NIPLLRDIVQ EKRFRSGDIT TKYLPEVYPE GFQGTVLTHA EEKTVIAFAA ALNARKLARA
     NQFLNQNRQR STHVASFSKT YKFVSSLPAK EGQRPTEHAV EVSFVDGDAN KAKVSIGGKV
     IDISGNLSLS LPVNSIEVNG EHITTQIVGK RAGEITVLYK GTPFKVQVLP EQAVKYLQYM
     KEKAKVDLST VVLSPMPGAI KNVNVKPGDM VSEGQELVVM EAMKMQNSLH AGKTGRVKAV
     NVKVGATVDE GEVLVELE
//
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