ID   AXEA1_PRER2             Reviewed;         480 AA.
AC   D5EV35;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Acetylxylan esterase;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA1 {ECO:0000303|PubMed:21742923}; OrderedLocusNames=PRU_2212;
OS   Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=264731;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADE83449.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:20585943};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP   INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:21742923};
RX   PubMed=21742923; DOI=10.1128/aem.05321-11;
RA   Kabel M.A., Yeoman C.J., Han Y., Dodd D., Abbas C.A., de Bont J.A.,
RA   Morrison M., Cann I.K., Mackie R.I.;
RT   "Biochemical characterization and relative expression levels of multiple
RT   carbohydrate esterases of the xylanolytic rumen bacterium Prevotella
RT   ruminicola 23 grown on an ester-enriched substrate.";
RL   Appl. Environ. Microbiol. 77:5671-5681(2011).
CC   -!- FUNCTION: Involved in degradation of plant cell wall polysaccharides.
CC       Is an acetyl esterase with broad substrate specificity, releasing
CC       acetic acid from acetylated xylo-oligosaccharides and acetylated xylan
CC       as well as xylose-tetraacetate, 4-O-methylumbelliferyl acetate,
CC       glucose-pentaacetate, and cephalosporin C. Appears to have greater
CC       activity on oligosaccharides than on polymeric substrates. Is also able
CC       to release acetic acid from xylo-oligosaccharides with 4-O-
CC       methylglucuronic acid side groups proximally located to O-acetyl
CC       esters. Preferentially targets xylo-oligosaccharides possessing three
CC       or more O-acetyl groups, but following their depletion it is active on
CC       the less acetylated portion of the substrate.
CC       {ECO:0000269|PubMed:21742923}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72; Evidence={ECO:0000269|PubMed:21742923};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0 with glucose-pentaacetate as substrate. Active from
CC         pH 5.0 to 8.0. {ECO:0000269|PubMed:21742923};
CC       Temperature dependence:
CC         Optimum temperature is 30 to 35 degrees Celsius with glucose-
CC         pentaacetate as substrate. Active from 20 to 50 degrees Celsius.
CC         Still exhibits 40 to 70% of the maximum activity after 20 hours of
CC         incubation at 50 degrees Celsius. {ECO:0000269|PubMed:21742923};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000269|PubMed:21742923}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:21742923}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; CP002006; ADE83449.1; -; Genomic_DNA.
DR   RefSeq; WP_013065432.1; NC_014033.1.
DR   AlphaFoldDB; D5EV35; -.
DR   SMR; D5EV35; -.
DR   STRING; 264731.PRU_2212; -.
DR   EnsemblBacteria; ADE83449; ADE83449; PRU_2212.
DR   GeneID; 31501757; -.
DR   KEGG; pru:PRU_2212; -.
DR   eggNOG; COG0657; Bacteria.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_043392_0_0_10; -.
DR   OMA; THFSDEG; -.
DR   OrthoDB; 1247435at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000927; Chromosome.
DR   GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..480
FT                   /note="Acetylxylan esterase"
FT                   /id="PRO_0000422402"
SQ   SEQUENCE   480 AA;  53109 MW;  F0B64248010172E1 CRC64;
     MNRKLFMTGL LMLAMTMQAQ TAKKFTLNLS DDGKAQMVCF LPENPSGRAI VGVPGGGYSM
     LSNTHEGYQA SDWLNKQGIA YFVVNYRLPH GDRTIPVGDV EQGFRIVRDS AKVWNINPND
     VGIMGFSAGG HLSSVISTMS PYEVRPNFSI LFYPVISMDE RVSHKWSCIN FLGKEGYKDP
     KLIGQYSTQN AVRSHLTPPA CIISANDDRL VPVVTNGIQY YSAMRNAGNE CSLFIYPSGD
     HGFGFGTWFK YHDQLLQDLG NWLKSIPAPK EDAIRVACIG NSITDGFGID MRAKYGYPAQ
     LQGILGDGYW VKNFGVSART MLNKGDFPYM NEMAWKDALA FKPDVVVIKL GTNDSKPENW
     QYGSEFRQDL EQMIKALRPD LAQPAKKGKK KAKAAAQPAG PKILLCTPIP AFKPSWNIND
     KVITDEIIPI QQEVAKQYGL QIIDLHALML NDGDKVVDDG IHPNEKGAKK MAEIIAAAIK