ID A0A0F8WXI3_9EURO Unreviewed; 903 AA.
AC A0A0F8WXI3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=acetylxylan esterase {ECO:0000256|ARBA:ARBA00013092};
DE EC=3.1.1.72 {ECO:0000256|ARBA:ARBA00013092};
GN ORFNames=ARAM_000727 {ECO:0000313|EMBL:KKK16082.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK16082.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK16082.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK16082.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000256|ARBA:ARBA00001691};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC subfamily. {ECO:0000256|ARBA:ARBA00007052}.
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:KKK16082.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZBS01003113; KKK16082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8WXI3; -.
DR STRING; 308745.A0A0F8WXI3; -.
DR OrthoDB; 10632at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR43037:SF5; FERULOYL ESTERASE B; 1.
DR PANTHER; PTHR43037; UNNAMED PRODUCT-RELATED; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..903
FT /note="acetylxylan esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002529344"
FT DOMAIN 399..557
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 903 AA; 99413 MW; 1BB877E5F04C0B3D CRC64;
MIRRLIFSTL FVAVAFWQKT SASCSTKIPG DQLHTSPAQF PLGGTRPNIY FSKSWQVLGP
FRIGTREAVW GADPLEYQGG FSNLPYDEDA KFSSALAPNG TVQWGVLGAN NTSPMPDQSR
TELIVRFPEV DWTFLQSVYG WSALQYQAWV RGYLQLNELT HQTIAIFTDG ILELIVDGKG
HFGGDFYSYH SAPLILDLAP GEHVIELRLI RDVRAMGGLG EPTVQVVLEA EIRRESLSID
ERSLLVPETT NRKLGSVQLS INVQSNVAEC IQVLSVSSSE VPLVMETAII TISNSAPGVL
VSPEGTLRTL SFLVELVEKS LSQPQRLTYL HPAGIVSYAI LRPPPLNSVC TDQQNNSMPV
IVALHGAGLE ADNKEVREML DAAYGVCAWM LFPSGVTSWS GDDWHTWGVA DVKAAINAVS
QWITAVGWTG PGISSEDWIV VGHSNGGQGA WFLATHYPDN VIAVAPVSGY SSIENYVPYS
VWRDSEPLLS AVLQRSRSSF KHESLLENIG GIPILQQHGS NDTNVPVYHS RLMHELLGEV
GWSSEYNELP GKGHWYAGLM TTPSLLDFYE SSLVSLPLKT PLAYTLIIPS SGDVTSKGGI
YVDQLQSPDI NGLLKVSKDT ENGVWLVKTR NVHRFHLTAT VCQTQRPVSL VLDDTPHRFE
VDPDQCNSTW YVKNSEAEWT SSRQSGWQHL SQRYGRQVGA MDAILRTWGV FTIVTCSANI
DHIALQISRN LLQYFNADSR ITSQCPSITT TGLPGQSTIP GNVITLAIGD SLPSAALSSF
PIRINERKVF LFQRSVQFDP DQKINLDIAG KHPPYTYDYE QGLGALFLRP LENEALELVV
WGADLYGLEQ AARLVPTLTG AGQPEFLILG DSCRWKGHAG LYAAGHLDKF WQISPGSYVN
TDR
//
