ID A0A2W2DKN5_9ACTN Unreviewed; 406 AA.
AC A0A2W2DKN5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:PZG05665.1};
GN ORFNames=C1I95_32555 {ECO:0000313|EMBL:PZG05665.1};
OS Micromonospora craterilacus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1655439 {ECO:0000313|EMBL:PZG05665.1, ECO:0000313|Proteomes:UP000248924};
RN [1] {ECO:0000313|EMBL:PZG05665.1, ECO:0000313|Proteomes:UP000248924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA12 {ECO:0000313|EMBL:PZG05665.1,
RC ECO:0000313|Proteomes:UP000248924};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella sp. NA12.";
RL Submitted (JAN-2018) 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}.
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:PZG05665.1}.
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DR EMBL; POTY01000380; PZG05665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2DKN5; -.
DR OrthoDB; 5167532at2; -.
DR Proteomes; UP000248924; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:PZG05665.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248924};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PZG05665.1}.
FT DOMAIN 8..258
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..389
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 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 406 AA; 42915 MW; D362E54149623A42 CRC64;
MPREVRDVVF VDGVRTPFGR AGGMYANTRA DDLVIRCIRE LLRRNPQLPP DRVEEVAIAA
TTQIGDQGLT IGRTAALLAG LPKTVPGFAI DRMCAGAMTA VTTVASGIAV GAYDVAIAGG
VEHMGRHPMG EGVDPNPRIV AEKLVDPSAL VMGATAENLH DRVPHITKER TDAFALASQQ
KTAKAYANGK LQDDLVPVAI RDPETGWGLA TVDEAPRDTS MEKLASLKTP FRPHGKVTAG
NAAGLNDGAT ASLLVAEEVA RELGLPIAMR LVSYGFVGVE PEVMGVGPIP STEKALRIAG
LSIDDIGLFE LNEAFAVQVL AFLDHFGIAD DDPRVNQWGG AIAIGHPLAS SGVRLMTQLA
RQFAEHPEVR YGITAMCIGI GMGGTVIWEN PHWTESGQSA QGEGNK
//
