ID V9XGS6_9NOCA Unreviewed; 403 AA.
AC V9XGS6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=Y013_13405 {ECO:0000313|EMBL:AHD21578.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21578.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD21578.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD21578.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD21578.1; -; Genomic_DNA.
DR RefSeq; WP_024102334.1; NC_023150.1.
DR AlphaFoldDB; V9XGS6; -.
DR GeneID; 29936474; -.
DR KEGG; rpy:Y013_13405; -.
DR PATRIC; fig|1435356.3.peg.2700; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_11; -.
DR Proteomes; UP000018781; Chromosome.
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:AHD21578.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AHD21578.1}.
FT DOMAIN 4..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..401
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 403 AA; 41777 MW; 51BDFA04113A0A3C CRC64;
MTDVVICEPL RTPVGRFGGV LKDIAPEDLA ATVIRELVAR TGITGSDIDD VFLGQASPNG
EAPALGRVAA LNAGLGVDVP GLQVDRRCGS GLQAIVQAVM QVQTGASDLI LAGGAESMSQ
AEFYATGMRW GVKGEAVALS DRLARARVTA GGRDFPVPGG MIETAENLRA EFSISREDQD
ALAVQSHQRA VAAQKNGVFA QEIVSVSVPQ RKGDPLVVDT DEHPRADTSM ETLAKLRPIR
GKIDPESTVT AGNASGQNDG AALAIVTTTE KAAALGLRPL ARLASWAVAG VPPRTMGIGP
VPASEKALGR LGLTLADMDV IELNEAFAAQ ALAVTRSWGI EADDSRLNPN GSGISLGHPV
GATGGRILAT LLRELDRREG RYGLETMCIG GGQGLAAVFE RIA
//
