XYFA_PRER2
ID XYFA_PRER2 Reviewed; 726 AA.
AC D5EY13; C0LJN0;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Endo-1,4-beta-xylanase/feruloyl esterase {ECO:0000303|PubMed:19304844, ECO:0000303|PubMed:21742923};
DE Includes:
DE RecName: Full=Endo-1,4-beta-xylanase;
DE EC=3.2.1.8 {ECO:0000269|PubMed:19304844};
DE Includes:
DE RecName: Full=Feruloyl esterase;
DE EC=3.1.1.73 {ECO:0000269|PubMed:19304844};
DE AltName: Full=Ferulic acid esterase;
DE Flags: Precursor;
GN Name=xyn10D-fae1A {ECO:0000312|EMBL:ACN78954.1};
GN OrderedLocusNames=PRU_2728; ORFNames=ORF02827;
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:ACN78954.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, SUBSTRATE SPECIFICITY, DOMAIN,
RP GENE NAME, SUBUNIT, AND MUTAGENESIS OF GLU-280 AND SER-629.
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:19304844};
RX PubMed=19304844; DOI=10.1128/jb.01628-08;
RA Dodd D., Kocherginskaya S.A., Spies M.A., Beery K.E., Abbas C.A.,
RA Mackie R.I., Cann I.K.;
RT "Biochemical analysis of a beta-D-xylosidase and a bifunctional xylanase-
RT ferulic acid esterase from a xylanolytic gene cluster in Prevotella
RT ruminicola 23.";
RL J. Bacteriol. 191:3328-3338(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ADE83639.1}
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 [3] {ECO:0000305, ECO:0000312|EMBL:ACN78954.1}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, IDENTIFICATION BY MASS
RP 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 Has endo-xylanase activity towards substrates such as oat spelt xylan
CC (OSX), acetylated xylo-oligosaccharides and acetylated xylan, producing
CC primarily xylobiose; cannot hydrolyze xylobiose to xylose. Also has
CC feruloyl esterase activity, releasing ferulic acid from methylferulate,
CC and from the more natural substrates wheat bran, corn fiber, and
CC XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and
CC ferulic acid esters. Exhibits negligible acetyl esterase activity on
CC sugar acetates. Acts synergistically with Xyl3A to increase the release
CC of xylose from xylan. Does not possess endoglucanase or mannanase
CC activities since it is not able to hydrolyze carboxymethyl cellulose
CC and locust bean gum. {ECO:0000269|PubMed:19304844,
CC ECO:0000269|PubMed:21742923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19304844,
CC ECO:0000269|PubMed:21742923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000269|PubMed:19304844,
CC ECO:0000269|PubMed:21742923};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0 for xylanase activity.
CC {ECO:0000269|PubMed:19304844};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}.
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:19304844}.
CC -!- INDUCTION: By growth on ester-enriched corn oligosaccharides.
CC {ECO:0000269|PubMed:21742923}.
CC -!- DOMAIN: The two catalytic domains appear to be functionally coupled.
CC {ECO:0000269|PubMed:19304844}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC hydrolase 10 (cellulase F) family. {ECO:0000255}.
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DR EMBL; FJ713437; ACN78954.1; -; Genomic_DNA.
DR EMBL; CP002006; ADE83639.1; -; Genomic_DNA.
DR RefSeq; WP_013065621.1; NC_014033.1.
DR AlphaFoldDB; D5EY13; -.
DR SMR; D5EY13; -.
DR STRING; 264731.PRU_2728; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR EnsemblBacteria; ADE83639; ADE83639; PRU_2728.
DR GeneID; 31502259; -.
DR KEGG; pru:PRU_2728; -.
DR eggNOG; COG2382; Bacteria.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_385739_0_0_10; -.
DR OrthoDB; 1828423at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000927; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
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; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00756; Esterase; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW Polysaccharide degradation; Reference proteome; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..726
FT /note="Endo-1,4-beta-xylanase/feruloyl esterase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422405"
FT DOMAIN 27..369
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 370..726
FT /note="Feruloyl esterase"
FT ACT_SITE 161
FT /note="Proton donor; for xylanase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /note="Nucleophile; for xylanase activity"
FT /evidence="ECO:0000305|PubMed:19304844"
FT ACT_SITE 629
FT /note="Nucleophile; for esterase activity"
FT /evidence="ECO:0000305|PubMed:19304844"
FT MUTAGEN 280
FT /note="E->S: Marked decrease in xylanase activity. Shows
FT approximately 3-fold increase in feruloyl esterase
FT activity."
FT /evidence="ECO:0000269|PubMed:19304844"
FT MUTAGEN 629
FT /note="S->A: Marked decrease in feruloyl esterase
FT activity."
FT /evidence="ECO:0000269|PubMed:19304844"
SQ SEQUENCE 726 AA; 82289 MW; 8C8641934CF95EA3 CRC64;
MKKLLVALSL IAGSLTASAQ WGRPVDYAAG PGLKDAYKDY FTVGVAVNKF NISDPAQTAI
VKKQFNSVTA ENAWKPGEIH PKEGVWNFGL ADSIANFCRE NGIKMRGHCL CWHSQFADWM
FTDKKGKPVK KEVFYQRLRE HIHTVVNRYK DVVYAWDVVN EAMADDGRPF EFVDGKMVPA
SPYRQSRHFK LCGDEFIAKA FEFAREADPT GVLMYNDYSC VDEGKRERIY NMVKKMKEAG
VPIDGIGMQG HYNIYFPDEE KLEKAINRFS EIVNTIHITE LDLRTNTESG GQLMFSRGEA
KPQPGYMQTL QEDQYARLFK IFRKHKDVIK NVTFWNLSDK DSWLGVNNHP LPFDENFKAK
RSLQIIRDFD AAMDNRKPKE DFVPNPMNQP GQEYPMVNSE GYARFRVEAP DAKSVIVSLG
LGGRGGTVLR KDKNGVWTGT TEGPMDPGFH YYHLTIDGGV FNDPGTHNYF GSCRWESGIE
IPAKDQDFYA YRKDINHGNI QQVTFWSEST GKMQTANVYL PYGYGKVVKG KQERYPVLYL
QHGWGENETS WPVQGKAGLI MDNLIADGKI KPFIVVMAYG LTNDFKFGSI GKFTAEEFEK
VLIDELIPTI DKNFLTKADK WNRAMAGLSM GGMETKLITL RRPEMFGYWG LLSGGTYMPE
EIKDPKAVKY IFVGCGDKEN PEGINKSVEA LKAAGFKAEG LVSEGTAHEF LTWRRCLEKM
AQSLFK
