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Database: UniProt
Entry: A0A1I1VY13_9BURK
LinkDB: A0A1I1VY13_9BURK
Original site: A0A1I1VY13_9BURK 
ID   A0A1I1VY13_9BURK        Unreviewed;       534 AA.
AC   A0A1I1VY13;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=3-methylcrotonyl-CoA carboxylase beta subunit {ECO:0000313|EMBL:SFD86968.1};
GN   ORFNames=SAMN04489710_107223 {ECO:0000313|EMBL:SFD86968.1};
OS   Paracidovorax konjaci.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=32040 {ECO:0000313|EMBL:SFD86968.1, ECO:0000313|Proteomes:UP000199517};
RN   [1] {ECO:0000313|EMBL:SFD86968.1, ECO:0000313|Proteomes:UP000199517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7481 {ECO:0000313|EMBL:SFD86968.1,
RC   ECO:0000313|Proteomes:UP000199517};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOMQ01000007; SFD86968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1VY13; -.
DR   STRING; 32040.SAMN04489710_107223; -.
DR   OrthoDB; 9803706at2; -.
DR   Proteomes; UP000199517; 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          21..277
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          280..526
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   534 AA;  57418 MW;  5061C4D4C4344B5D CRC64;
     MILESRLNSR SADFQANAAA MRTLVQDLRE RAAQVALGGS EAARAKHTAR GKLLPRDRVR
     ELLDPGSPFL EIAPLAALGM YGDEAPGAGL IAGIGRVSGV DCMVVCNDAT VKGGTYYPLT
     VKKHLRAQEI AQQNRLPCIY LVDSGGANLP NQDEVFPDRD HFGRIFYNQA QMSAQGIAQI
     AVVMGSCTAG GAYVPAMSDE SIIVKGQGTI FLGGPPLVKA ATGEVVTAED LGGGDVHTRL
     SGVADHLAQN DLHALQLARN AVRNLNRNRP HAAGFIGPDA PLFEAEELYG VIPVDTRKPF
     DVREIIARIV DGSEFDEFKA RYGTTLVTGF ARIEGMPVGI IANNGILFSE SALKGAHFIE
     LCCQRKIPVV FLQNITGFMV GRKYENEGIA RNGAKMVTAV ATAAVPKFTI VIGGSFGAGN
     YGMCGRAYSP RFLWMWPNAR ISVMGGEQAA SVLATVRRDG IEAKGAAWSL EEEEAFKAPI
     RRQYEEQGHP YYATARLWDD GVIDPADTRR VLALGLAAAR NAPVEDTKFG IFRM
//
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