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Database: UniProt
Entry: G6EIL4_9SPHN
LinkDB: G6EIL4_9SPHN
Original site: G6EIL4_9SPHN 
ID   G6EIL4_9SPHN            Unreviewed;       403 AA.
AC   G6EIL4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:EHJ58956.1};
GN   ORFNames=NSU_4185 {ECO:0000313|EMBL:EHJ58956.1};
OS   Novosphingobium pentaromativorans US6-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ58956.1, ECO:0000313|Proteomes:UP000004030};
RN   [1] {ECO:0000313|EMBL:EHJ58956.1, ECO:0000313|Proteomes:UP000004030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=US6-1 {ECO:0000313|EMBL:EHJ58956.1,
RC   ECO:0000313|Proteomes:UP000004030};
RX   PubMed=22275104; DOI=10.1128/JB.06476-11;
RA   Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT   "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT   pentaromativorans US6-1.";
RL   J. Bacteriol. 194:907-907(2012).
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:EHJ58956.1}.
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DR   EMBL; AGFM01000064; EHJ58956.1; -; Genomic_DNA.
DR   AlphaFoldDB; G6EIL4; -.
DR   STRING; 1088721.JI59_02890; -.
DR   PATRIC; fig|1088721.3.peg.4122; -.
DR   eggNOG; COG0183; Bacteria.
DR   Proteomes; UP000004030; 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; IPR020610; Thiolase_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:SF144; ACYL-COA THIOLASE-RELATED; 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:UP000004030};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EHJ58956.1}.
FT   DOMAIN          16..272
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          280..401
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        100
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   403 AA;  41540 MW;  E55C9F1081D0A855 CRC64;
     MQKGKVMAQI SANDPIVILS YARTPMGGLQ GVFADVSATD LGATAVKAAV ERSGVAGEDV
     ERIYMGCVLP AGLGQAPARQ AALKAGLPKS VQATTVNKVC GSGMQTVIMG AEALASGSLD
     LIIAGGMESM TNAPYLSKKH RSGARAGHDT LYDHMFLDGL EDAYEGGSMG SFAQVTADEY
     QLTRENQDDF SIESLRRAQE AITSGAFKDE VVPVTVKTRK GEVVVDTDEQ PPKGNPDKIR
     TLRAAFAKDG TITAASSSSI SDGAAAVVMS RASVAAAKGL KPVATVVGVA AHAHEPAKFT
     TAPVGAITKL LDKVGWQLSD VDLFEVNEAF ACVAMFAMHD LGIPHDKINI HGGATALGHP
     IGASGTRIIV TLINALKDKG LKRGVASLCI GGGEATAIAV ELA
//
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