ID PCCA_MOUSE Reviewed; 724 AA.
AC Q91ZA3; Q80VU5; Q922N3;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-APR-2013, entry version 89.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6;
RX PubMed=11461925; DOI=10.1074/jbc.M105467200;
RA Miyazaki T., Ohura T., Kobayashi M., Shigematsu Y., Yamaguchi S.,
RA Suzuki Y., Hata I., Aoki Y., Yang X., Minjares C., Haruta I., Uto H.,
RA Ito Y., Muller U.;
RT "Fatal propionic acidemia in mice lacking propionyl-CoA carboxylase
RT and its rescue by postnatal, liver-specific supplementation via a
RT transgene.";
RL J. Biol. Chem. 276:35995-35999(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY: ATP + propanoyl-CoA + HCO(3)(-) = ADP +
CC phosphate + (S)-methylmalonyl-CoA.
CC -!- COFACTOR: Biotin.
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).
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC -!- DISEASE: Note=Propionic acidemia due to recessively inherited
CC deficiency of PCCase activity often causes life-threatening
CC ketosis and acidosis.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC -!- SIMILARITY: Contains 1 biotinyl-binding domain.
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DR EMBL; AY046947; AAL02364.1; -; mRNA.
DR EMBL; BC006915; AAH06915.1; -; mRNA.
DR EMBL; BC049802; AAH49802.1; -; mRNA.
DR IPI; IPI00330523; -.
DR RefSeq; NP_659093.2; NM_144844.2.
DR UniGene; Mm.23876; -.
DR ProteinModelPortal; Q91ZA3; -.
DR SMR; Q91ZA3; 59-724.
DR IntAct; Q91ZA3; 1.
DR PhosphoSite; Q91ZA3; -.
DR REPRODUCTION-2DPAGE; Q91ZA3; -.
DR PaxDb; Q91ZA3; -.
DR PRIDE; Q91ZA3; -.
DR Ensembl; ENSMUST00000038374; ENSMUSP00000038763; ENSMUSG00000041650.
DR GeneID; 110821; -.
DR KEGG; mmu:110821; -.
DR CTD; 5095; -.
DR MGI; MGI:97499; Pcca.
DR eggNOG; COG4770; -.
DR GeneTree; ENSGT00550000074675; -.
DR HOGENOM; HOG000008989; -.
DR HOVERGEN; HBG000555; -.
DR InParanoid; Q91ZA3; -.
DR KO; K01965; -.
DR OMA; DEETXVL; -.
DR OrthoDB; EOG4Q58NT; -.
DR UniPathway; UPA00945; UER00908.
DR ChiTaRS; PCCA; mouse.
DR NextBio; 364725; -.
DR ArrayExpress; Q91ZA3; -.
DR Bgee; Q91ZA3; -.
DR Genevestigator; Q91ZA3; -.
DR GermOnline; ENSMUSG00000041650; Mus musculus.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IMP:MGI.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00289; CPSase_L_chain; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 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 2: Evidence at transcript level;
KW ATP-binding; Biotin; Complete proteome; Ligase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1 48 Mitochondrion (By similarity).
FT CHAIN 49 724 Propionyl-CoA carboxylase alpha chain,
FT mitochondrial.
FT /FTId=PRO_0000002838.
FT DOMAIN 58 505 Biotin carboxylation.
FT DOMAIN 177 374 ATP-grasp.
FT DOMAIN 656 723 Biotinyl-binding.
FT ACT_SITE 349 349 By similarity.
FT BINDING 173 173 ATP (By similarity).
FT BINDING 257 257 ATP (By similarity).
FT BINDING 292 292 ATP (By similarity).
FT MOD_RES 690 690 N6-biotinyllysine (By similarity).
FT CONFLICT 497 497 T -> A (in Ref. 1; AAL02364).
FT CONFLICT 542 542 H -> R (in Ref. 2; AAH06915).
FT CONFLICT 555 561 WELSVKL -> VGALGKV (in Ref. 1; AAL02364).
SQ SEQUENCE 724 AA; 79922 MW; 249189EDF9F99274 CRC64;
MAGQWVRTVA LLAARRHWRR SSQQQLLGTL KHAPVYSYQC LVVSRSLSSV EYEPKEKTFD
KILIANRGEI ACRVIKTCKK MGIKTVAIHS DVDASSVHVK MADEAVCVGP APTSKSYLNM
DAIMEAIKKT RAQAVHPGYG FLSENKEFAK RLAAEDVTFI GPDTHAIQAM GDKIESKLLA
KRAKVNTIPG FDGVVKDADE AVRIAREIGY PVMIKASAGG GGKGMRIAWD DEETRDGFRF
SSQEAASSFG DDRLLIEKFI DNPRHIEIQV LGDKHGNALW LNERECSIQR RNQKVVEEAP
SIFLDPETRQ AMGEQAVALA KAVKYSSAGT VEFLVDSQKN FYFLEMNTRL QVEHPVTECI
TGLDLVQEMI LVAKGYPLRH KQEDIPISGW AVECRVYAED PYKSFGLPSI GRLSQYQEPI
HLPGVRVDSG IQPGSDISIY YDPMISKLVT YGSDRAEALK RMEDALDNYV IRGVTHNIPL
LREVIINTRF VKGDISTKFL SDVYPDGFKG HTLTLSERNQ LLAIASSVFV ASQLRAQRFQ
EHSRVPVIRP DVAKWELSVK LHDEDHTVVA SNNGPAFTVE VDGSKLNVTS TWNLASPLLS
VNVDGTQRTV QCLSREAGGN MSIQFLGTVY KVHILTKLAA ELNKFMLEKV PKDTSSTLCS
PMPGVVVAVS VKPGDMVAEG QEICVIEAMK MQNSMTAGKM GKVKLVHCKA GDTVGEGDLL
VELE
//
