ID C3JJG0_RHOER Unreviewed; 529 AA.
AC C3JJG0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Carboxyl transferase domain protein {ECO:0000313|EMBL:EEN88198.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:EEN88198.1};
GN ORFNames=RHOER0001_5925 {ECO:0000313|EMBL:EEN88198.1};
OS Rhodococcus erythropolis SK121.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN88198.1, ECO:0000313|Proteomes:UP000005836};
RN [1] {ECO:0000313|EMBL:EEN88198.1, ECO:0000313|Proteomes:UP000005836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK121 {ECO:0000313|EMBL:EEN88198.1,
RC ECO:0000313|Proteomes:UP000005836};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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:EEN88198.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACNO01000029; EEN88198.1; -; Genomic_DNA.
DR RefSeq; WP_003941927.1; NZ_ACNO01000029.1.
DR AlphaFoldDB; C3JJG0; -.
DR Proteomes; UP000005836; Unassembled WGS sequence.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EEN88198.1};
KW Transferase {ECO:0000313|EMBL:EEN88198.1}.
FT DOMAIN 16..272
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 263..521
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 529 AA; 56740 MW; E8E838196C1A771E CRC64;
MTPSGITQGT GYRSDHTVLV DELKKKLAQA ALGGNERSRE RHVSRGKLLP RDRVDSLLDQ
GSPFLELSPL AANGLYDDEC PGAGVITGIG RVSGRECVIV ANDATVKGGT YYPMTVKKHL
RAQEVALQNN LPCIYLVDSG GAFLPRQDEV FPDREHFGRI FYNQATMSAK GIPQIAAVLG
SCTAGGAYVP AMSDEAVIVR NQGTIFLGGP PLVKAATGEI VTAEELGGGD LHSKVSGVTD
HLAEDDRDAL RIVRNIIATL GPRSERPWDV ISTVPPVADQ SELYDVVPTD PRTPYDVHEV
ITKLVDGGAF QEFKAEYGKT LVTGFAHIEG HPVGIIANNG VLFGESAMKG AHFIELCDKR
SVPLLFLQNI AGFMVGRDYE AGGIAKHGAK MVTAVACARV PKLTVVIGGS YGAGNYSMCG
RAYSPRFLWM WPNARISVMG GEQAASVLST VRSEQLDSAG NPWSAEDEES FKAPIREQYE
AQGNPYYSTA RLWDDGVIDP ADTRTVLGLA LSVCANAPIE PVSYGVFRM
//
