ID A0A094EEM1_9PEZI Unreviewed; 1221 AA.
AC A0A094EEM1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00012352};
DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
GN ORFNames=V499_03399 {ECO:0000313|EMBL:KFY77141.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY77141.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY77141.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY77141.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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:KFY77141.1}.
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DR EMBL; JPKB01000526; KFY77141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EEM1; -.
DR HOGENOM; CLU_268634_0_0_1; -.
DR Proteomes; UP000029295; 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 GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd00829; SCP-x_thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
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 PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..120
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 288..394
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 527..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 133369 MW; 600B921CC4147C9A CRC64;
MSQPTYIAGV GMTPFKSPKN SAKSARNPDS DYFDLAVEAA VKALLDAGLT YDDVDSGVGC
YVFGDSTCAQ RVFYALGMTG IPITNVNNYC SSGSTGLYLA NQAIRSGQSE CVLVIGFDKM
YPGALPQIFN DRTNPLSRIL DLSKTLIPEA DKGKKSPGWT PQLYANAQAE YLQRYGNAGA
KNEHFAKITS VNRAHGVNNP YSQLAKTVST KEVMNSPVIT GEITRLQCCP SSTGAAAAIV
CSEQFLKSHP HLAGSAVQIA GQAMSTDTPL LFEPPSAIEL IGSNMTRLAA KEAYKQANIT
PRDVTIVELH DCFTTNEMCA LEGLGLADEG KAWKLVQDGG ISYGPGGGVG LDGKGWIVNP
SGGLISKGHP LGATGLAQCT ELVWHLRGWA TTRAVDQTKY CLQHNMGLGG ATVVTIYKRA
DGKPVPKAED IKAEDDGRHR LGYNPAVEAR SISKADWEAV KSRSGGSSKW ATAHLPWASA
GQGQEVGMDA LCARPDALRI DCVYVPVAPR RSRAASSAAS ASLNAEIRNS PSQSQNGNSP
GSPQTSATGA SCFPNTPSGE PSAKGQEVVV TPSSGTTLGA GQYPSPTPYE HFYAPEQIFS
NQSEGDATFQ YQAPSNANHN GSSNSVDGAA TAMPVSMDTS LCPPNFDGFF NVPNLGSTFA
TFAFSDSQAF PGSEVPYNFN LVHGSALSQG RSGMHASPPN LPSNGNNAMP IASSTAAKDS
HAQITTETDF LPLKDETRAY LITYFKRSTR PPASLVSVDP AGWYQMQQYL LRTASSHSVV
MDALLALTQL FSVCESTLRS SSSSQWRMAF ELQQRSCMGL RERRIDEKSQ NALLAAIFLL
AWFEVICDEQ DAHRSNFPTE LAESVIRGSA RWNSASRRLL QWLNSFDAKA SHLGGRQLLT
PKSLEVVLQH RFERSYRTVD SGDSENETVS NDSEEDSRNG SAAVFTQERK RRASSRSFPT
RSFITPREIK MNVFNAIMQP ALEFHLVSQS YSRKIGTHDR HHRSRNTVED EYEVVTACKT
IDTELKKLWR QRPRVLDLTA KDLSGVVCED IAERLDELFA VYIATFWAHF LYIHRVAWWG
LPHSSTAKEA LDEFWRMMCR SVRETEDNKD NHLLVMDRQK VIHPGLMWPM FMFGCEVEIG
EKQQWSVTQL RLLGERTATP DTEQQHSDSL PPYRLGQKGA QNAIRASVLL NELVKRQNET
GARVDGKYLS QELFGCQFTI I
//
