ID A0A0D2X5E3_CAPO3 Unreviewed; 562 AA.
AC A0A0D2X5E3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CAOG_007769 {ECO:0000313|EMBL:KJE97659.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE97659.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; KE346375; KJE97659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2X5E3; -.
DR STRING; 595528.A0A0D2X5E3; -.
DR EnsemblProtists; KJE97659; KJE97659; CAOG_007769.
DR eggNOG; KOG0540; Eukaryota.
DR InParanoid; A0A0D2X5E3; -.
DR PhylomeDB; A0A0D2X5E3; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000008743};
KW Transferase {ECO:0000313|EMBL:KJE97659.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 58..312
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 317..549
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 562 AA; 60510 MW; 1AED61C7E567BEE3 CRC64;
MLSRTLVSSA AVTRAAACTA APVAAVKAAA AVSAGVSAPQ QARSIATAAS VARAAQEGRS
IQERIAEKVT AAKLGGGQDR IDKQHKQGKL TARERLEVLL DPGSFREYDM FAEHNCTDFG
MQKYTGDGVV TGHGRINGRL VYVFSQDFTV FGGSLSSAHA KKICKIMDKA LLVGAPVIGL
NDSGGARIQE GVESLAGYAD IFQRNVDASG VIPQISVIMG PCAGGAVYSP AMTDFVFMVR
DTSYMFVTGP DVVKTVTNET VTQEELGGAK THTAKSGVAH RAFENDMEAL QRLREFFDFL
PLSNKDAAPV RATALVDPSR PVPALDTLIP SDSLQPYDMK EVIHKVVDFE HFFELMPDYA
KNLIVGFARM NGRTVGIVAN QPLEASGCLD INSSVKGARF VRFCDAFNIP IITFVDVPGF
LPGTAQEYGG IIRHGAKLLY AYAEASVPKI TVITRKAYGG AYDVMSSKHL RGDVNYAWPN
AEIAVMGAKG AVSIIFRGQK DMAASEKEYI EKFSNPFPAA QRGFIDDIIT PSTTRERIIE
DLTVLDTKDY QGHKKKHGNI PL
//
