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Database: UniProt
Entry: A0A2G8KWU1_STIJA
LinkDB: A0A2G8KWU1_STIJA
Original site: A0A2G8KWU1_STIJA 
ID   A0A2G8KWU1_STIJA        Unreviewed;       492 AA.
AC   A0A2G8KWU1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
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=BSL78_10685 {ECO:0000313|EMBL:PIK52435.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK52435.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK52435.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK52435.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK52435.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK52435.1}.
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DR   EMBL; MRZV01000329; PIK52435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8KWU1; -.
DR   STRING; 307972.A0A2G8KWU1; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..236
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          247..489
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   492 AA;  53486 MW;  35BDB23654B0F3AB CRC64;
     MECLSSQGKL TARERINLLV DPGSFVEFDM FAEHRCSDFG MDSDEKRHPG DGVVTGHGLI
     NGRVTYVFSQ DFTVHGGTLS SAHAKKICKI MDHALNTGAP VIRPQDSGGA RIQEGVESLA
     GYADIFHRNV MASGVIPQIS LIMGPCAGGA VYSPALTDFT FMIKDTSYLF ITGPDVVKAV
     TQEDVTHEQL GGAKTHTSVS GVAHGAFEND IDGLTKLREL FSYLPLSNRD PAQSYSQMTL
     PSQVITTGNR LVPVLDHIVP FESIKPYDML DVIHAIVDNR SFFEIMPAYA KNIVIGFARM
     NGRTVGIVGN QPKVASGCLD INSSVKGARF VRFCDAFNIP LITFVDVPGF LPGTSQEYGG
     IIRHGAKLLY AYSEATVPKI TVITRKAYGG AYDVMSSKHI GGDINYTWPT AEVAVMGAQG
     AVKIIFRGES DIAQAEQEYI EKFANPFPAA VRGFVDDIIQ PSTTRVRLCR DLDLLSTKKK
     ENPTKKHANM PL
//
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