ID A0A0Q5MDW0_9BURK Unreviewed; 510 AA.
AC A0A0Q5MDW0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Methylmalonyl-CoA carboxyltransferase {ECO:0000313|EMBL:KQR55540.1};
GN ORFNames=ASF94_03745 {ECO:0000313|EMBL:KQR55540.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR55540.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR55540.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR55540.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR55540.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR55540.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQR55540.1}.
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DR EMBL; LMOV01000012; KQR55540.1; -; Genomic_DNA.
DR RefSeq; WP_056664205.1; NZ_LMOV01000012.1.
DR AlphaFoldDB; A0A0Q5MDW0; -.
DR STRING; 1736280.ASF94_03745; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000051403; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000051403};
KW Transferase {ECO:0000313|EMBL:KQR55540.1}.
FT DOMAIN 1..257
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 261..504
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 249..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 56279 MW; 1B593424F03A7B8F CRC64;
MQDILEQLEQ KRALARLGGG QKRIDAQHKK GKLTARERIE LLLDDGTFEE WDMFVEHRCT
DFGMEANRPP GDGVVAGYGM INGRLVFIFS QDFTVFGGAL SETHAEKICK VMDQAMKVGA
PVIGLNDSGG ARIQEGVASL GGYADVFQKN VLASGVVPQI SMIMGPCAGG AVYSPAMTDF
IFMVKDSSYM FVTGPEVVKT VTHEDVTAEE LGGAITHTTR SGVADMAFEN DVEALMMLRR
LYNYLPLNNR EKPPVRPSND PADRKDLSLD TLVPDNPNKP YDMKELILKT VDDGDFFELQ
PDYAKNIVIG FARMEGQTVG IVANQPLVLA GCLDIKSSIK AARFVRFCDA FNIPVITFVD
VPGFMPGTSQ EYSGIIKHGA KLLYAYAECT VPKITVITRK AYGGAYDVMS SKHLRGDVNL
AWPNAEIAVM GAKGAVEIIF REEKKDPEKL AAREGEYKKR FANPFVASAR GFIDDVILPH
ETRKRICRSL VMLQNKKLEN PWRKHGNIPL
//
