ID C1H1Y9_PARBA Unreviewed; 448 AA.
AC C1H1Y9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Homoserine O-acetyltransferase {ECO:0000313|EMBL:EEH33876.2};
GN ORFNames=PAAG_04925 {ECO:0000313|EMBL:EEH33876.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH33876.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH33876.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000256|ARBA:ARBA00006886}.
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DR EMBL; KN294003; EEH33876.2; -; Genomic_DNA.
DR RefSeq; XP_015699639.1; XM_015845413.1.
DR AlphaFoldDB; C1H1Y9; -.
DR STRING; 502779.C1H1Y9; -.
DR GeneID; 9096506; -.
DR KEGG; pbl:PAAG_04925; -.
DR VEuPathDB; FungiDB:PAAG_04925; -.
DR eggNOG; ENOG502QRIX; Eukaryota.
DR HOGENOM; CLU_028760_5_0_1; -.
DR OMA; SYLHYQG; -.
DR OrthoDB; 2600616at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEH33876.2}.
FT DOMAIN 49..392
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 204..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 359
FT /evidence="ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 388
FT /evidence="ECO:0000256|PIRSR:PIRSR000443-1"
SQ SEQUENCE 448 AA; 49609 MW; B6028D7BFAC42882 CRC64;
MPLPSPLNPE SHYAMSLSHI QQEENYQPLE TIADVSDWWG PLLGGPGQAF DVTRFFVVCL
NSLGSPYGSA SAVTSRDGDK NKGIYGPEFP LTTIRDDVRI HKLVLDDLGV RQIASVVGGS
MGGMLVLEYA FFGKDYVRSI VPIATSSRHS AWGISWGEAQ RQSIYSDPKY EDGYYSFDDP
PATGLGAARM SALLTYRSRN SFESRFGRNV PDPSKRQNIN GTLRLPTPPN EHWAVHNDGH
RSTRSPPAPN NSGPESNEVF TDPQFNGATL FTAPSSPTST APSERSWRPT TYFSAQSYLR
YQGQKFVKRF DSNCYIAITR KLDTHDVSRH RADPDSTTPV KDALSQIQQP ALVIGIESDG
LFTFAEQQEL ADGIPNSRLK NIDSPEGHDA FLLQFEQVNR YILEFFREVL PDIMNASGND
TDGVVDHVGQ LTKSSTFGEA EVEDITAW
//