ID A0A421JQN9_9ASCO Unreviewed; 401 AA.
AC A0A421JQN9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=JA1_002363 {ECO:0000313|EMBL:RLV93636.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV93636.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV93636.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV93636.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) 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:RLV93636.1}.
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DR EMBL; NSGQ01000014; RLV93636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JQN9; -.
DR STRING; 2028339.A0A421JQN9; -.
DR Proteomes; UP000285775; 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; -; 2.
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:SF9; ACETYL-COA C-ACETYLTRANSFERASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 13..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..397
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 401 AA; 42400 MW; 749568F661517D53 CRC64;
MSLPLLKKSA SDIVVLSALR TPVTRGTKGG LAKMFPEELL YQVLKGSIER SQIDPELIDD
VLVGTVLQTL GGQKASALAV KKVGFPIKTT VNTINRQCAS SAQAISYSAG TLLTGENKFT
IAAGVESMTH DYFPHRGIPT RIYEPFKQDA SEEAQNVLMP MGITSENVVS KFGISRKAQD
EFAVASHLKA AKAIETGHFA KEIIPIQARQ LDETKTDLVE VSRDDGVRPG STFEKLSTLK
PVFKEDGTTT AGNSSQISDG ASAVILTTRA NAEALGIKPI ARFIGSSVAG VPSGLMGIGP
SAAVPQLLQR LGLETKDIDI FELNEAFASQ SIYCIDKLGL DYDKVNPYGG AIAIGHPLGA
TGGRVTSTLL NGLRAQQKEL GVISMCTSTG QGYAAVFANE A
//
