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Database: UniProt
Entry: A0A0G3X9U2_9SPHN
LinkDB: A0A0G3X9U2_9SPHN
Original site: A0A0G3X9U2_9SPHN 
ID   A0A0G3X9U2_9SPHN        Unreviewed;       398 AA.
AC   A0A0G3X9U2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AKM07384.1};
GN   ORFNames=AM2010_1311 {ECO:0000313|EMBL:AKM07384.1};
OS   Pelagerythrobacter marensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Pelagerythrobacter.
OX   NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM07384.1, ECO:0000313|Proteomes:UP000037643};
RN   [1] {ECO:0000313|EMBL:AKM07384.1, ECO:0000313|Proteomes:UP000037643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM07384.1,
RC   ECO:0000313|Proteomes:UP000037643};
RA   Kim K.M.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; CP011805; AKM07384.1; -; Genomic_DNA.
DR   RefSeq; WP_047806398.1; NZ_LMVG01000001.1.
DR   AlphaFoldDB; A0A0G3X9U2; -.
DR   STRING; 543877.AM2010_1311; -.
DR   KEGG; amx:AM2010_1311; -.
DR   PATRIC; fig|543877.4.peg.1331; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000037643; Chromosome.
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; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037643};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AKM07384.1}.
FT   DOMAIN          10..267
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          276..396
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        94
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   398 AA;  41024 MW;  176BB0A8912068D9 CRC64;
     MAQFSANDPV VILSYARTPM GGMQGALAAV SATELGATAV KASVERAGVA GDDIDRVYMG
     CVLPAGLGQA PARQAAIKAG LPKSVQATTV NKVCGSGMQT VIMGSEALAS GTIDIVVAGG
     MESMTNAPYL LKKHRSGARI GHDTAYDHMF LDGLEDAYEE GRAMGTFAQS TANDYQMTRE
     EMDDYAIESL RRANAAIDSG AFADEITPVT FSTRAGETVV DTDEQPGRGK PDKIPTLKPA
     FAKDGTITAA TSSSISDGAA AVVLTRASVA KDKGLAPVAR VVAMAAHAQE PAQFTVAPIG
     AIQKVLDEAG WSVDDVELWE VNEAFACVAM FAMRDIGIPH DKININGGGT ALGHPIGASG
     TRIIVTLLNA LKKQGKKRGI ASLCIGGGEA TAVAVELA
//
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