ID U0EQD7_9NOCA Unreviewed; 391 AA.
AC U0EQD7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Methylmalonyl-CoA carboxyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N806_31435 {ECO:0000313|EMBL:ERB55628.1};
OS Rhodococcus sp. P27.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1384060 {ECO:0000313|EMBL:ERB55628.1, ECO:0000313|Proteomes:UP000016008};
RN [1] {ECO:0000313|EMBL:ERB55628.1, ECO:0000313|Proteomes:UP000016008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P27 {ECO:0000313|EMBL:ERB55628.1,
RC ECO:0000313|Proteomes:UP000016008};
RX PubMed=24072865;
RA Gouvea Taketani R., Domingues Zucchi T., Soares de Melo I., Mendes R.;
RT "Whole-Genome Shotgun Sequencing of Rhodococcus erythropolis Strain P27, a
RT Highly Radiation-Resistant Actinomycete from Antarctica.";
RL Genome Announc. 1:e00763-13(2013).
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:ERB55628.1}.
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DR EMBL; AVCO01000005; ERB55628.1; -; Genomic_DNA.
DR AlphaFoldDB; U0EQD7; -.
DR PATRIC; fig|1384060.5.peg.364; -.
DR Proteomes; UP000016008; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
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 3: Inferred from homology;
FT DOMAIN 5..253
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 262..391
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 15..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 41459 MW; AFF78232BC4D485F CRC64;
MTTTTAEKLA ELREKLEKAK EPGSARAIAK RDAAGHSTPR QRIDMLLDPG SFVEVGALVK
MAGEDNPYSD GVMTGHGTVD GRPVAVFAHD QTVFGGAAGE MFGRKVAAVN DFALKVGCPV
VGINDSGGAR IQDAVSSLAW YANMGSRQEP LSGVCPQISV ILGKCAGGAV YAPINTDVVV
ATEESYMFVT GPDVIKSVTG EEVSLEDLGG ARKQAEYGNI HHVAPDEKAA FDWVREYLSF
MPSSCTEKAP LINPGLEPEI TESDLELNAF MPDADNAGYD MHDIILRIFD DGTFHEIGAQ
VAHNVITGFS RVDGLPVGVV ANQPRTSVAP SMRTAPTRLP ILCACATLSA SRSFLSSTHQ
AFFPASIRKR SVSSSVAGVS CSRTSKPLSR R
//
