ID A0LRW7_ACIC1 Unreviewed; 510 AA.
AC A0LRW7;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Propionyl-CoA carboxylase {ECO:0000313|EMBL:ABK52177.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:ABK52177.1};
GN OrderedLocusNames=Acel_0403 {ECO:0000313|EMBL:ABK52177.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52177.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK52177.1, 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; ABK52177.1; -; Genomic_DNA.
DR RefSeq; WP_011719240.1; NC_008578.1.
DR AlphaFoldDB; A0LRW7; -.
DR STRING; 351607.Acel_0403; -.
DR KEGG; ace:Acel_0403; -.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_018822_6_1_11; -.
DR InParanoid; A0LRW7; -.
DR OrthoDB; 9803706at2; -.
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 InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22855:SF13; METHYLCROTONOYL-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 Ligase {ECO:0000313|EMBL:ABK52177.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT DOMAIN 1..254
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 253..492
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 510 AA; 54383 MW; CDD20872F3A80F32 CRC64;
MSESGPVDPR DVRERVLRGG PAKYHEANAA RGKLFVRDRI RYLVDPDSFV EDGLFANALA
ADLPADAVVT GTATIDGRPV ALMANDSTVK AGSWGARTVE KIIRIIEYAV RCGLPLVYLV
DSAGARIPDQ VAMFPGRRGA GHIFYSQVRA SGAVPQVCAL FGPSAAGGAY IPAFCDLVVM
VEGNASMYLG SDRMVEMVTG EKTSLEEMGG ARMHCAESGV GHLLVGDEYA ALDAVRRYLS
YLPSNWREEP PSAPPRDPEP VDLGALVPAN ERVAFDMKAF IRGLVDAGSF FEIHPLWARE
IVVGFARLAG QVIGVVANNP LHKGGVLFVD SADKATRFIN LCDAFNVPLL FLADVPGFMV
GTAVEKQGII RHGAKMLTAV AEATVPKFCV VVRKAYGAGL YAMAGPGFAP DATLALPTAK
IAVMGAEAAV NAVHARRLAA IADEAERARV AAQLRADYAA DIDIVRLASE LVVDDIVEPA
ALRMQLIERL ARTRGKNRAF ADRRHGVAPV
//
