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Database: UniProt
Entry: M6ZVX5_9ACTN
LinkDB: M6ZVX5_9ACTN
Original site: M6ZVX5_9ACTN 
ID   M6ZVX5_9ACTN            Unreviewed;       407 AA.
AC   M6ZVX5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 2.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   ORFNames=ISGA_4903 {ECO:0000313|EMBL:EMP10206.2};
OS   Gordonia sp. NB41Y.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP10206.2, ECO:0000313|Proteomes:UP000011989};
RN   [1] {ECO:0000313|EMBL:EMP10206.2, ECO:0000313|Proteomes:UP000011989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP10206.2,
RC   ECO:0000313|Proteomes:UP000011989};
RX   PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA   Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT   "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT   to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL   Microbiology 159:1618-1628(2013).
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:EMP10206.2}.
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DR   EMBL; APHK02000088; EMP10206.2; -; Genomic_DNA.
DR   RefSeq; WP_053778178.1; NZ_CP132196.1.
DR   AlphaFoldDB; M6ZVX5; -.
DR   STRING; 1241906.ISGA_4903; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000011989; Unassembled WGS sequence.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
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   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:EMP10206.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011989};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EMP10206.2}.
FT   DOMAIN          7..273
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          282..404
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        362
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   407 AA;  42087 MW;  386ACDE6B0D64DC1 CRC64;
     MATGTDIVIC SPLRTPVGRM GGVLASQTVT DLATTLLREL ASRTGLGEGD VDDVILGQGY
     ANGESPAIGR MAALDAGLGV GVPGMQVDRR CGSGLQAVLS GAAQVASGGA SLVIAGGAES
     MSNVEHYALG LRTGIRQGGV ELMDRLDRGR LTAGGSSHPI PGGMIETAEN LRARYHLGRA
     EQDEFAVESH RRAIAAQDAG KFDDEIVPVT IPGRRGKPDV VVERDEHPRA DASVEGLSKL
     RAIRAKIDPD STVTAGNASG QNDGAAMCVV TTRAEAERRG LTPLLALKSW AVTGCAPEEM
     GIGPVGATAA ALQRADLTLD EIDLIELNEA FAAQVLAVLA EWKIDAGDER LNPNGSGISL
     GHPIGATGAR ILATAAHEAR RRESRYVLET MCIGGGQGLA AIFEAIR
//
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