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Database: UniProt
Entry: G7MJQ2_MACMU
LinkDB: G7MJQ2_MACMU
Original site: G7MJQ2_MACMU 
ID   G7MJQ2_MACMU            Unreviewed;       570 AA.
AC   G7MJQ2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Propionyl-CoA carboxylase beta chain, mitochondrial {ECO:0000256|ARBA:ARBA00041138};
DE            EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
DE   AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00042797};
GN   ORFNames=EGK_12081 {ECO:0000313|EMBL:EHH16744.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH16744.1};
RN   [1] {ECO:0000313|EMBL:EHH16744.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-5 {ECO:0000313|EMBL:EHH16744.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
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:0000256|ARBA:ARBA00001715};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC         Evidence={ECO:0000256|ARBA:ARBA00001715};
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:0000256|ARBA:ARBA00000634};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC         Evidence={ECO:0000256|ARBA:ARBA00000634};
CC   -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC       succinyl-CoA from propanoyl-CoA: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00005060}.
CC   -!- SUBUNIT: The holoenzyme is a dodecamer composed of 6 PCCA/alpha
CC       subunits and 6 PCCB/beta subunits. {ECO:0000256|ARBA:ARBA00038567}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
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DR   EMBL; CM001254; EHH16744.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7MJQ2; -.
DR   Proteomes; UP000013456; Chromosome 2.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR   PANTHER; PTHR43842:SF3; PROPIONYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          32..321
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          325..564
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   570 AA;  61714 MW;  5FB4C02DC4BE1EE5 CRC64;
     MAAALRVAAA GARLSVLASG LRAAIRGLCS QATSVNERIE NKRRTALLGG GQRRIDAQHK
     RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN KFPGDSVVTG RGRINGRLVY
     VFSQIQVSAM LPWLVSDSWI QAIRLPWPPK VLGLQDFTVF GGSLSGAHAQ KICKIMDQAI
     TVGAPVIGLN DSGGARIQEG VESLAGYADI FLRNVTASGV IPQISLIMGP CAGGAVYSPA
     LTDFTFMVKD TSYLFITGPD VVKSVTNEDV TQEELGGAKT HTTMSGVAHR AFENDVDALC
     NLRDFFNYLP LSNQDSAPVR ECHDPSDRLV PELDTIVPLE STKAYNMVDI IHSVVDEREF
     FEIMPNYAKN IIVGFARMNG RTVGIVGNQP KVASGCLDIN SSVKGARFVR FCDAFNIPLI
     TFVDVPGFLP GTAQEYGGII RHGAKLLYAF AEATVPKVTV ITRKAYGGAY DVMSSKHLCG
     DTNYAWPTAE IAVMGAKGAV EIIFKGHENV EAAQAEYIEK FANPFPAAVR GFVDDIIQPS
     STRARICCDL DVLASKKVQR PWRKHANIPL
//
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