ID A0A1L9BQD3_9RHOB Unreviewed; 534 AA.
AC A0A1L9BQD3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:OJH44368.1};
GN ORFNames=IE00_11460 {ECO:0000313|EMBL:OJH44368.1};
OS Paracoccus sp. SM22M-07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1520813 {ECO:0000313|EMBL:OJH44368.1, ECO:0000313|Proteomes:UP000183790};
RN [1] {ECO:0000313|EMBL:OJH44368.1, ECO:0000313|Proteomes:UP000183790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM22M-07 {ECO:0000313|EMBL:OJH44368.1,
RC ECO:0000313|Proteomes:UP000183790};
RA Carlos C., Ottoboni L.;
RT "Draft sequencing and comparative genomics of Paracoccus sp. SM22M-07
RT isolated from coral mucus: Insights into bacteria-host interactions.";
RL Submitted (JUL-2014) 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:OJH44368.1}.
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DR EMBL; JPKW01000006; OJH44368.1; -; Genomic_DNA.
DR RefSeq; WP_072297206.1; NZ_JPKW01000006.1.
DR AlphaFoldDB; A0A1L9BQD3; -.
DR STRING; 1520813.IE00_11460; -.
DR Proteomes; UP000183790; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000183790}.
FT DOMAIN 21..277
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 274..526
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 33..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 57258 MW; ECB45E2324352205 CRC64;
MKLTSQALPS SDQFRANRQA HLDLLDTVRQ AADQAAAGGG SAATERHVSR GKMPPRERVA
NLLDPGSPFL EIGATAAHGM YDGAAPGAGV IAGIGRVHGQ DVMVVANDAT VKGGTYYPMT
VKKHLRAQEI AEECELPCVY LVDSGGANLP NQDEVFPDRD HFGRIFFNQA RMSAKGIPQI
AVVMGSCTAG GAYVPAMSDV TIIVRGQGTI FLAGPPLVKA ATGEVVTSED LGGGDVHTRL
SGVADYLAED DAHALAQARR AVANLNRRRP ETVLWQSPEA PAYDPDELFG VVPADLRTPY
DIREVIARIV DGSRFDEFKA RFGETLVTGF AHVEGCPVGI VANNGVLFSE AAQKGAHFIE
LCSARGIPLV FLQNITGFMV GRKYENEGIA RHGAKMVTAV ATTNVPKITM LVGGSFGAGN
YGMSGRAYSP RFLWTWPNSR ISVMGGEQAA GVLATVRRDG IERKGGTWSA EEEAAFKRPT
VEMFDRQSHP LYASARLWDD GIIDPRKSRE VLALSLRASL NAPIQPTRFG IFRM
//
