ID A0LT87_ACIC1 Unreviewed; 474 AA.
AC A0LT87;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Propionyl-CoA carboxylase {ECO:0000313|EMBL:ABK52647.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:ABK52647.1};
GN OrderedLocusNames=Acel_0874 {ECO:0000313|EMBL:ABK52647.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52647.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK52647.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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DR EMBL; CP000481; ABK52647.1; -; Genomic_DNA.
DR RefSeq; WP_011719710.1; NC_008578.1.
DR AlphaFoldDB; A0LT87; -.
DR STRING; 351607.Acel_0874; -.
DR KEGG; ace:Acel_0874; -.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_018822_6_2_11; -.
DR InParanoid; A0LT87; -.
DR OrthoDB; 5240504at2; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 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 Ligase {ECO:0000313|EMBL:ABK52647.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT DOMAIN 1..229
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 228..461
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 48829 MW; 6FB42AFB55225D1F CRC64;
MTHDAHDTRP GTSGPQDLDP RTPTARLGAF FDPGTFQPIS PLDDCGVLAG VGTVAGTHTV
AFASDPTIQG GAMGSVGCSV IVGAYDRALA DGAPIVGLWH SGGARLREGV ESLDGVGRVF
AAMTRASGKI PQISVVLGPA AGGAAYGPAL TDIVIMGPAG RIFVTGPDVV RSVTGEDVDM
ERLGGAEVHG RRSGVVHLLA DSDEQALGYA RDVVALLGNQ GKLGDAPLVD VDLADRIPEA
AKRAYDVHPL VDGLLDSPGV ELHPKWAPNI VTTLGRLAGR TVGVIANNPL RLGGCLDTTS
AEKAARFVRM CDAFGVPLVV VVDVPGYLPG LGQEWDGVVR RGAKLLHAFA EAVVPRITLI
TRKAYGGAYI AMNSRALGAT RVLAWPGAEV AVMGAVAAVR ILHRRKLAEV GEALRPSLEL
ELAAEHEKIA GGIEKAVALG VVDDVVDPAR TRSAIADAIA AAPPVRGEHG NIPL
//
