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Database: UniProt
Entry: A0A0Q5CF24_9BURK
LinkDB: A0A0Q5CF24_9BURK
Original site: A0A0Q5CF24_9BURK 
ID   A0A0Q5CF24_9BURK        Unreviewed;       540 AA.
AC   A0A0Q5CF24;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:KQQ30984.1};
GN   ORFNames=ASF61_17280 {ECO:0000313|EMBL:KQQ30984.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ30984.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ30984.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ30984.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ30984.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ30984.1};
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:KQQ30984.1}.
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DR   EMBL; LMNW01000036; KQQ30984.1; -; Genomic_DNA.
DR   RefSeq; WP_056160834.1; NZ_LMNW01000036.1.
DR   AlphaFoldDB; A0A0Q5CF24; -.
DR   STRING; 1736266.ASF61_17280; -.
DR   OrthoDB; 9803706at2; -.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
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;
FT   DOMAIN          22..283
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          286..532
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   540 AA;  57660 MW;  7CFBE33DC29A43FE CRC64;
     MPQIDTKLNP RSEDFRTNTA AMQAVVDDLR AKVAAIAQGG GAAASAKHVA RGKLLPRDRV
     QMLLDPGTPF LELSQMAAYG MYQDASGVDA APAAGIITGI GRVAGQECVI VCNDATVKGG
     TYYPVTVKKH LRAQEIADQN HLPCIYLVDS GGANLPNQDD VFPDRDHFGR IFYNQANLSA
     KGIPQIAVVM GSCTAGGAYV PAMSDESIIV KEQGTIFLGG PPLVKAATGE VVTAEDLGGG
     DVHTRLSGVA DHLAQNDLHA LSLARTIVAN LNRIKPQQGA LRPVVAPKYP AEELYGVIPV
     DTRKPFDVRE VIARIVDGSE FDEFKARFGA TLVCGFAHIF GMKVGIIANN GILFSESAVK
     GAHFIELCAQ RKIPLVFLQN ITGFMVGRKY ENEGIARHGA KMVTAVATAA VPKFTVIIGG
     SFGAGNYGMC GRAFSPRFMW MWPNARISVM GGDQAASVLA TVKRDGIEAK GGSWSAEEEA
     AFKQPIRQQY EEQGHPYYAT ARLWDDGVID PADTRTVLGL GLSAALNAPI DDTRFGVFRM
//
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