ID C3JJP1_RHOER Unreviewed; 532 AA.
AC C3JJP1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Carboxyl transferase domain protein {ECO:0000313|EMBL:EEN88260.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:EEN88260.1};
GN ORFNames=RHOER0001_6006 {ECO:0000313|EMBL:EEN88260.1};
OS Rhodococcus erythropolis SK121.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN88260.1, ECO:0000313|Proteomes:UP000005836};
RN [1] {ECO:0000313|EMBL:EEN88260.1, ECO:0000313|Proteomes:UP000005836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK121 {ECO:0000313|EMBL:EEN88260.1,
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:EEN88260.1}.
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DR EMBL; ACNO01000029; EEN88260.1; -; Genomic_DNA.
DR RefSeq; WP_003941989.1; NZ_ACNO01000029.1.
DR AlphaFoldDB; C3JJP1; -.
DR GeneID; 64139738; -.
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:SF46; METHYLCROTONOYL-COA CARBOXYLASE; 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:EEN88260.1};
KW Transferase {ECO:0000313|EMBL:EEN88260.1}.
FT DOMAIN 22..273
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 277..523
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 532 AA; 57205 MW; 16BC70790579F480 CRC64;
MSVIRSTLDT NSEVYKTATS TMNTKLAEIE VEHAKALAGG GEKYTERHHK RGKLLARERI
ELLLDQDSPF LELCPLAAWG SDFPVGASTV VGIGVVEGVE CLIVANDPTV RGGTSNPWTL
RKGFRANDIA MQNRLPVISL VESGGADLPT QKEVFIPGGR MFRDLTQLSA AGIPTIALVF
GNSTAGGAYI PGMSDHVVMI KERSKVFLAG PPLVKMATGE ESDDEALGGA EMHARKSGLA
DYFAADEQDA IRIGRSIVKR LNWTKKGPAP RAEIIEPLED PEELLGIVPA DLKIPFDPRE
VIARIVDGSD FDEFKPLYGS SLVTGWAELN GYPIGILANA RGVLFSEESQ KATQFIQLAN
RSNTPLLFLH NTTGYMVGKE YEEGGMIKHG SMMINAVANS KVPHISILLG ASYGAGHYGM
CGRAFDPRFL FAWPSSKSAV MGGAQLAGVI SIVGRAAAEA RGQVFDEQAD AGMRAMIENQ
IEAESLPMFL SGRLYDDGVI DPRDTRTVVG MCLSAIATAP IEGTENFGVF RM
//
