SAT_STABO
ID SAT_STABO Reviewed; 259 AA.
AC G0YF19;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Sophorolipid acetyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=Carboxyhydrate transacetylase;
GN Name=at;
OS Starmerella bombicola (Yeast) (Candida bombicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Starmerella.
OX NCBI_TaxID=75736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX PubMed=21702032; DOI=10.1002/bit.23248;
RA Saerens K.M., Saey L., Soetaert W.;
RT "One-step production of unacetylated sophorolipids by an acetyltransferase
RT negative Candida bombicola.";
RL Biotechnol. Bioeng. 108:2923-2931(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX PubMed=23964782; DOI=10.1021/pr400392a;
RA Ciesielska K., Li B., Groeneboer S., Van Bogaert I., Lin Y.C., Soetaert W.,
RA Van de Peer Y., Devreese B.;
RT "SILAC-based proteome analysis of Starmerella bombicola sophorolipid
RT production.";
RL J. Proteome Res. 12:4376-4392(2013).
RN [3]
RP FUNCTION.
RX PubMed=23516968; DOI=10.1111/mmi.12200;
RA Van Bogaert I.N., Holvoet K., Roelants S.L., Li B., Lin Y.C.,
RA Van de Peer Y., Soetaert W.;
RT "The biosynthetic gene cluster for sophorolipids: a biotechnological
RT interesting biosurfactant produced by Starmerella bombicola.";
RL Mol. Microbiol. 88:501-509(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=26298016; DOI=10.1093/femsyr/fov075;
RA Saerens K.M., Van Bogaert I.N., Soetaert W.;
RT "Characterization of sophorolipid biosynthetic enzymes from Starmerella
RT bombicola.";
RL FEMS Yeast Res. 15:0-0(2015).
CC -!- FUNCTION: Catalyzes the optional acetylation of acidic sophorolipids
CC (SLs) at the 6' and/or 6'' carbon atom of the sophorose head group to
CC produce acetylated acidic SLs in sophorolipid biosynthesis
CC (PubMed:21702032, PubMed:23516968, PubMed:26298016). Has no activity
CC toward lactonic sophorolipids, confirmimg that acetylation must precede
CC lactonization (PubMed:26298016). {ECO:0000269|PubMed:21702032,
CC ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:26298016}.
CC -!- INDUCTION: Induced in early stationary phase (at protein level).
CC {ECO:0000269|PubMed:23964782}.
CC -!- DISRUPTION PHENOTYPE: Produces purely unacetylated sophorolipids.
CC Yields mainly lactonic SLs, in addition to minor amounts of acidic SLs.
CC {ECO:0000269|PubMed:21702032}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; HQ670751; AEK28753.1; -; Genomic_DNA.
DR AlphaFoldDB; G0YF19; -.
DR SMR; G0YF19; -.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR024688; Mac_dom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF12464; Mac; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Repeat; Transferase.
FT CHAIN 1..259
FT /note="Sophorolipid acetyltransferase"
FT /id="PRO_0000443099"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 129
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 186
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 204
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 209..210
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 224
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 227
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT SITE 129
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07464"
SQ SEQUENCE 259 AA; 28581 MW; EFB0E95B55A2EC64 CRC64;
MVVNSSKDPQ NKGMTPRKEI DQEMVSWAKK NLKNTPGNEN YEKMVSGVPY NPYDPDLMFR
ALATSEKVRE FNTIASESRT FESNHAAYIK KVEILKDTFG QTKDIVWLTA PFSVDFGFNI
SVGEHFYANF NVCFLDSAPI IFGDEVIVGP NTTFVTATHP ISPEKRARRI VYALPIKVGN
NVWIGANVTV LPGVTIGDGS TIAAGAVVRE DVPPRTVVGG VPARILKHIP EEDPDEAEGE
ELEFLLPVEM NVNTANQKV
