ACUI_ASPA1
ID ACUI_ASPA1 Reviewed; 553 AA.
AC A0A1L9WN42;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Serine-type carboxypeptidase acuI {ECO:0000303|PubMed:26374386};
DE EC=3.4.16.- {ECO:0000305|PubMed:26374386};
DE AltName: Full=Aculin biosynthesis cluster protein I {ECO:0000303|PubMed:26374386};
DE Flags: Precursor;
GN Name=acuI {ECO:0000303|PubMed:26374386}; ORFNames=ASPACDRAFT_1904405;
OS Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=690307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 16872 / CBS 172.66 / WB 5094;
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=26374386; DOI=10.1002/cbic.201500210;
RA Petersen L.M., Holm D.K., Gotfredsen C.H., Mortensen U.H., Larsen T.O.;
RT "Investigation of a 6-MSA Synthase Gene Cluster in Aspergillus aculeatus
RT Reveals 6-MSA-derived Aculinic Acid, Aculins A-B and Epi-Aculin A.";
RL ChemBioChem 16:2200-2204(2015).
CC -!- FUNCTION: Serine-type carboxypeptidase; part of the gene cluster that
CC mediates the biosynthesis of aculins (PubMed:26374386). The pathway
CC begins with the synthesis of 6-methylsalicylic acid by the polyketide
CC synthase (PKS) acuA via condensation of acetate and malonate units
CC (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then
CC catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-
CC cresol (also known as 3-methylphenol) (Probable). These first reactions
CC occur in the cytosol (By similarity). The intermediate m-cresol is then
CC transported into the endoplasmic reticulum where the cytochrome P450
CC monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is
CC further converted to gentisyl alcohol by the cytochrome P450
CC monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by
CC the oxidoreductase acuE that probably catalyzes hydroxylation of the
CC aromatic ring (Probable). The aromatic system might then be opened by
CC oxidation through a Baeyer-Villiger type of oxidation, which could be
CC catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced
CC to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is
CC formed, before the dehydrogenase acuH would reduce the double bond
CC between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results
CC in formation of aculinic acid, which exists as two diastereomers (both
CC R/S configurations at C-1) by non-enzymatic hemiacetal formation
CC (Probable). The carboxypeptidase acuI could be involved in the linking
CC of aculinic acid to an aculene A moiety produced by the aculene
CC biosynthesis cluster and which leads to the production of aculin A
CC (Probable). AcuI may also be involved in the attachment of proline to
CC aculinic acid to form epi-aculins A and B (Probable).
CC {ECO:0000250|UniProtKB:A0A075TRC0, ECO:0000269|PubMed:26374386,
CC ECO:0000305|PubMed:26374386}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26374386}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; KV878982; OJJ97583.1; -; Genomic_DNA.
DR RefSeq; XP_020053923.1; XM_020198809.1.
DR AlphaFoldDB; A0A1L9WN42; -.
DR SMR; A0A1L9WN42; -.
DR STRING; 690307.A0A1L9WN42; -.
DR EnsemblFungi; OJJ97583; OJJ97583; ASPACDRAFT_1904405.
DR GeneID; 30972623; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_1904405; -.
DR OrthoDB; 1263103at2759; -.
DR Proteomes; UP000184546; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..553
FT /note="Serine-type carboxypeptidase acuI"
FT /evidence="ECO:0000255"
FT /id="PRO_5011820801"
FT REGION 27..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 450
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 529
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 553 AA; 61789 MW; D07815713DCDE140 CRC64;
MLLPSFPVTG VATALLLRNA VHASQPGSSV QKARAYDRFS SRPTRDHAPR VQSSNTSTYR
FWNDKTKPHL VESLPDVHFD LGEMYSGSIN ITSHRNESRS LFYIFQPKIG EPSDDLTIYL
NGGPGCSSEQ AFFQENGRFT WQPGTYAPVI NQYSWVNLTN MLWVDQPVGT GYSVGTPTAT
NEAEVAADFL EFFSKFQDLY GIKNFRIFVS GESYAGRYVP YISSAMLDKN DTTHFNLSGK
PAHPLHHLAP TNAVCTGALL YDACIGQWDW VQAELPAYPF VQQHASLFNF NETFMTSLAT
TYEECGYQAY FDEYFTFPAS GIQPPKYMNY SECDIYNAIY NEAFSPNPCF NPYRVIDECP
LLWDVLGFPT DLAYEPAPTT YFNRADVKRA LHAPQNIEWE LCSTDPVLVG GDGVSGPEQV
GDDSPNPTEG SLPRVIEATN RVLIANGDWD YLIITNGTLL AIQNMTWHGQ LGFAAAPATP
IDIRMPDLQW AGVFDAQEGY GDLDGPQGVM GVQHYERGLM WAETFQAGHK QAQDQGRVSY
RHLQWLLGEV DSL
