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Database: UniProt
Entry: A0A0Q9L121_9MICO
LinkDB: A0A0Q9L121_9MICO
Original site: A0A0Q9L121_9MICO 
ID   A0A0Q9L121_9MICO        Unreviewed;       520 AA.
AC   A0A0Q9L121;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Carboxylase {ECO:0000313|EMBL:KRE43759.1};
GN   ORFNames=ASG74_02665 {ECO:0000313|EMBL:KRE43759.1};
OS   Knoellia sp. Soil729.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE43759.1, ECO:0000313|Proteomes:UP000051965};
RN   [1] {ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE43759.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE43759.1,
RC   ECO:0000313|Proteomes:UP000051965};
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:KRE43759.1}.
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DR   EMBL; LMSA01000001; KRE43759.1; -; Genomic_DNA.
DR   RefSeq; WP_056138682.1; NZ_LMSA01000001.1.
DR   AlphaFoldDB; A0A0Q9L121; -.
DR   STRING; 1736394.ASG74_02665; -.
DR   OrthoDB; 9803706at2; -.
DR   Proteomes; UP000051965; 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   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          6..261
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          261..502
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   520 AA;  55826 MW;  C8BA80F67C3A5F22 CRC64;
     MPVSESDPKV ADVRRRLDAA HAASASAPEK AAAKLASQGK LYVRDRIALL VDEGSFVEDG
     RYANALAKGL PADGVVTGRG TVDDRPVIVI ANDPTVKAGS WGARTVEKIV RATEMALREE
     LPVFWFVDSA GARITDQVEM FPGRRGAGRI FHNQVALSGK VPQICCLFGP SAAGGAYIPS
     FTDLLIMVEG NASMYLGSPR MAEMVVGERV SLEEMGGARM HCTVSGVGDI LVQDDAEAIE
     MARLYFSYVP QNWRTPGPSY AVESPSAPLT RTSVPERESQ PFDVHEVIDG LVDDDSFFEI
     KALFAPELVI GLGRMDGETV GIVANNSMVK GGVLFTDSAD KAARFIWLCD AYSIPLVYLA
     DVPGFMIGFE VERGGIIRHG AKMVSAVSSA TVPQFCVVVR KAYGAGLYAM GGPGFGPDAT
     IALPTARIAV MGPEAAVNAV YANKIAEVEA AEGAAARDAF VAQKRSEYEE DVDLERLAAD
     LVIDQVVEPE DLRDELLRRL RYAAHRDRTF ATKRRGIPPV
//
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