ID I4YJ10_WALMC Unreviewed; 396 AA.
AC I4YJ10;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=WALSEDRAFT_30751 {ECO:0000313|EMBL:EIM23952.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM23952.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM23952.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000617};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
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; JH668223; EIM23952.1; -; Genomic_DNA.
DR RefSeq; XP_006955790.1; XM_006955728.1.
DR AlphaFoldDB; I4YJ10; -.
DR STRING; 671144.I4YJ10; -.
DR GeneID; 18471172; -.
DR KEGG; wse:WALSEDRAFT_30751; -.
DR eggNOG; KOG1389; Eukaryota.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; I4YJ10; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 14..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 396 AA; 41104 MW; F4216D3DE54BBBBB CRC64;
MTIKEVLNKN PNDVVIVSAV RTPITRARKG GLAGTLPEKL LAHAFKEAVK RANVDPTLIE
DIAVGNVLPP GGGASLARMA QLYAGIPHTT AINTVNRQCS SGLQAISQIA LEIASGQIDF
GIGAGVESMT AHYGAGALPQ NMDEDVLSNQ EAADCLIPMG ITSENVAKDF GITRAAQDEF
AALSQQRAAA AQKAGKFRDE IAPIMVKNSD GTERLVDKDD GIRDGVTKES LAKLKPAFDA
NGVTHAGNAS QVSDGAAAVL LTRRSHAERL RLPILGKFVA SADVGCPPRI MGIGPAVAIP
KVLEKTGLTT SDVDIYEINE AFASQALYCV QKLGLSPAKV NPNGGAIALG HPLGCTGARQ
IATILSEAKK TGARILCTSM CIGSGMGKAS IIVNEQ
//
