ID A0A109JVG8_9BRAD Unreviewed; 389 AA.
AC A0A109JVG8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KWV55846.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KWV55846.1};
GN ORFNames=AS156_05405 {ECO:0000313|EMBL:KWV55846.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV55846.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV55846.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV55846.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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:KWV55846.1}.
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DR EMBL; LNCU01000060; KWV55846.1; -; Genomic_DNA.
DR RefSeq; WP_066507117.1; NZ_LNCU01000060.1.
DR AlphaFoldDB; A0A109JVG8; -.
DR OrthoDB; 9790314at2; -.
DR Proteomes; UP000057737; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00829; SCP-x_thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KWV55846.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KWV55846.1}.
FT DOMAIN 5..226
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..353
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 389 AA; 40958 MW; BF0A610BD619A8F3 CRC64;
MTASIVGWAH TPFGKFDAET VEGLVVKVAN EALADAGVAA SDVDEIMLGH FNAGFSPQDF
TASLVLQANP ALRFKPTTRV ENACATGSAA VHQGIRAIEA GAAKIVLVVG VEQMTRTPGP
EIGKNLLKAS YLPEDGDTVG GFAGVFGKIA QSYFQKYGDQ SDALAMIAAK NHKNGVANPY
AQMRKDFGFE FCRAESEKNP YVAGPLKRTD CSLVSDGAAA LVLTDADTAK KLGKAVNIRA
TAHAQDFLPM SKRDILQFEG CTVAWQRALQ KAGLQLSDLS FVETHDCFTV AELIEYEAMG
LTPKGQGARA IKEGWTLKDG KLPVNPSGGL KAKGHPIGAT GVSMHVMTAM QLTGQAPEGM
QLKNAQLGGI FNMGGAAVAN YVSILEPAK
//