ID V4PJI5_9CAUL Unreviewed; 316 AA.
AC V4PJI5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Acetyl-CoA C-acetyltransferase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ABENE_18815 {ECO:0000313|EMBL:ESQ85560.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ85560.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ85560.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ85560.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, 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:ESQ85560.1}.
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DR EMBL; AWGB01000057; ESQ85560.1; -; Genomic_DNA.
DR RefSeq; WP_023447416.1; NZ_AWGB01000057.1.
DR AlphaFoldDB; V4PJI5; -.
DR STRING; 1121022.GCA_000376105_01208; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000017837; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000017837};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 6..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..316
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT NON_TER 316
FT /evidence="ECO:0000313|EMBL:ESQ85560.1"
SQ SEQUENCE 316 AA; 32577 MW; 947298CCC4C9FCCD CRC64;
MSVNEVVIVS AARTPVGSFL GSFAAIPAHD LGAHAIKAAI ERAGLQPADI NEVILGQVLQ
AAQGQGPARQ ASVKAGVPYE APAWSLNQIC GSGLRAVALG AAQVALGESA IVVAGGQESM
SMATHAAYIR AGQKMGDLSM IDTMIKDGLW DAFNNYHMGQ TAENVATKFG ISRQEQDEFA
VASQNKAEAA QKAGKFDAEI APYTIKGRKG DTVVDKDEFI RHGVTIDSIS GLKPAFNKEG
TVTAANASGL NDGAAAVVLM SRAEADKRGL KPLARIVSSG ISGVDPAIMG TGPIQATLKA
LAKANWSVGD LDLIEA
//
