ID   AXFA_PRER2              Reviewed;         671 AA.
AC   D5EXZ4;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Carbohydrate acetyl esterase/feruloyl esterase;
DE   Includes:
DE     RecName: Full=Carbohydrate acetyl esterase;
DE              EC=3.1.1.- {ECO:0000269|PubMed:21742923};
DE   Includes:
DE     RecName: Full=Feruloyl esterase {ECO:0000303|PubMed:21742923};
DE              EC=3.1.1.73 {ECO:0000269|PubMed:21742923};
DE     AltName: Full=Ferulic acid esterase;
DE   Flags: Precursor;
GN   Name=axe1-6A {ECO:0000303|PubMed:21742923}; OrderedLocusNames=PRU_2707;
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:ADE82678.1}
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, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   DOMAIN, PATHWAY, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBSTRATE
RP   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       Bifunctional esterase that possesses both acetyl esterase and ferulic
CC       acid esterase activities. Has deacetylase activity towards acetylated
CC       xylo-oligosaccharides smaller than xylo-heptaose, as well as from
CC       glucose-pentaacetate. Is also able to release ferulic acid from
CC       methylferulate, and from the more natural substrates wheat bran, corn
CC       fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-
CC       acetyl and ferulic acid esters. {ECO:0000269|PubMed:21742923}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC         EC=3.1.1.73; Evidence={ECO:0000269|PubMed:21742923};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5 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 35 degrees Celsius with glucose-pentaacetate
CC         as substrate. Active from 20 to 50 degrees Celsius. Still exhibits 40
CC         to 70% of the maximum activity after 20 hours of incubation at 50
CC         degrees Celsius. {ECO:0000269|PubMed:21742923};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000269|PubMed:21742923}.
CC   -!- INDUCTION: By growth on ester-enriched corn oligosaccharides.
CC       {ECO:0000269|PubMed:21742923}.
CC   -!- DOMAIN: Is predicted to have two esterase domains corresponding to
CC       distinct carbohydrate esterase families, CE1 and CE6. It can be
CC       hypothesized that the release of acetic acid is related to the CE6
CC       domain, while the release of ferulic acid may relate to the CE1 domain.
CC       {ECO:0000269|PubMed:21742923}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC       esterase 6 family. {ECO:0000305}.
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DR   EMBL; CP002006; ADE82678.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5EXZ4; -.
DR   SMR; D5EXZ4; -.
DR   STRING; 264731.PRU_2707; -.
DR   EnsemblBacteria; ADE82678; ADE82678; PRU_2707.
DR   KEGG; pru:PRU_2707; -.
DR   eggNOG; COG2382; Bacteria.
DR   HOGENOM; CLU_015241_0_0_10; -.
DR   OMA; ENTAHEW; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000927; Chromosome.
DR   GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000801; Esterase-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR005181; SASA.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF00756; Esterase; 1.
DR   Pfam; PF03629; SASA; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Reference proteome; Signal; Xylan degradation.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..671
FT                   /note="Carbohydrate acetyl esterase/feruloyl esterase"
FT                   /id="PRO_0000422404"
FT   REGION          1..296
FT                   /note="Carbohydrate acetyl esterase"
FT   REGION          297..671
FT                   /note="Feruloyl esterase"
FT   ACT_SITE        55
FT                   /note="For acetyl esterase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        271
FT                   /note="For acetyl esterase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        274
FT                   /note="For acetyl esterase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   671 AA;  74683 MW;  4F394DBFEF820898 CRC64;
     MYQSTLKTIL LASALLILPA SMSAQKRKAA PKKAATEQVG KPDPNFYIFL CFGQSNMEGN
     ARPEAQDLTS PGPRFLLMPA VDFPEKGRKM GEWCEASAPL CRPNTGLTPA DWFGRTLVAS
     LPENIKIGVI HVAIGGIDIK GFLPDSIQNY LKVAPNWMKG MLAAYDNNPY ERLVTLAKKA
     QKDGVIKGIL MHQGETNTGD PKWAGMVKQV YDNLCGDLNL KPEEVNLYAG NIVQADGKGV
     CIGCKKQIDE LPLTLHTSQV ISSDGCTNGP DRLHFDAAGY RELGCRYGEA VARHLGYEPK
     RPYIEMPKQI EVPADAFIAE TTVPGNEFPK VDKEGRAYFR IAAPEARKVV LDICNKKYDM
     QRDGKGNFMA VTDPLPVGFH YYFLNINGVN FIDPSTETFF GCNRESGGIE IPEGSEGDYY
     RPQQGVPAGQ VRSIYYYSNE QQTWRHAMVY TPAEYELAKN AKKRYPVLYL QHGMGEDETG
     WSKQGHMQHI MDNAIAKGEA VPMIVVMESG DIKAPFGGGN NQAGRSAYGA SFYPVLLNDL
     IPYIDSNYRT KSDRENRAMA GLSWGGHQTF DVVLTNLDKF AWLGTFSGAI FGLDVKTAYD
     GVFANADEFN KKIHYMYMNW GEEDFIKSGD IVKQLRELGI KVDSNESKGT AHEWLTWRRG
     LNEFIPHLFK K