CESA_RUMFL
ID CESA_RUMFL Reviewed; 768 AA.
AC Q9RLB8;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Multidomain esterase {ECO:0000303|PubMed:10846217};
DE Includes:
DE RecName: Full=Acetylxylan esterase {ECO:0000303|PubMed:10846217};
DE EC=3.1.1.72 {ECO:0000269|PubMed:10846217};
DE Includes:
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305|PubMed:26216754};
DE EC=3.1.1.117 {ECO:0000269|PubMed:26216754};
DE AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:26216754};
DE Short=GE {ECO:0000303|PubMed:26216754};
DE Flags: Precursor;
GN Name=cesA {ECO:0000303|PubMed:10846217};
OS Ruminococcus flavefaciens.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1265;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION OF THE N-TERMINAL DOMAIN AS AN
RP ACETYLXYLAN ESTERASE, CATALYTIC ACTIVITY, PATHWAY, AND DOMAIN.
RC STRAIN=17;
RX PubMed=10846217; DOI=10.1099/00221287-146-6-1391;
RA Aurilia V., Martin J.C., McCrae S.I., Scott K.P., Rincon M.T., Flint H.J.;
RT "Three multidomain esterases from the cellulolytic rumen anaerobe
RT Ruminococcus flavefaciens 17 that carry divergent dockerin sequences.";
RL Microbiology 146:1391-1397(2000).
RN [2]
RP FUNCTION OF THE C-TERMINAL DOMAIN AS A GLUCURONOYL ESTERASE.
RC STRAIN=17;
RX PubMed=26216754; DOI=10.1016/j.febslet.2015.07.019;
RA Biely P., Malovikova A., Uhliarikova I., Li X.L., Wong D.W.;
RT "Glucuronoyl esterases are active on the polymeric substrate methyl
RT esterified glucuronoxylan.";
RL FEBS Lett. 589:2334-2339(2015).
CC -!- FUNCTION: Esterase involved in the degradation of plant cell wall
CC polysaccharides. Catalyzes the deacetylation of chemically acetylated
CC xylan and native, steam-extracted xylan (PubMed:10846217). Seems to act
CC in synergy with the xylanase XynD which produces xylo-oligosaccharides
CC (PubMed:10846217). Also catalyzes the deesterification of methyl esters
CC of 4-O-methyl-D-glucuronic acid (MeGlcA) side residues in synthetic
CC glucuronoxylan methyl ester, suggesting that it may be able to cleave
CC ester linkages between MeGlcA carboxyl and more complex alcohols,
CC including linkages between hemicellulose and lignin alcohols in plant
CC cell walls (PubMed:26216754). {ECO:0000269|PubMed:10846217,
CC ECO:0000269|PubMed:26216754}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000269|PubMed:10846217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-
CC O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+);
CC Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668;
CC EC=3.1.1.117; Evidence={ECO:0000269|PubMed:26216754};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:26216754};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000305|PubMed:10846217}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: Contains a dockerin-like region in addition to its catalytic
CC domains, suggesting that this enzyme forms part of a cellulosome-like
CC multienzyme complex. {ECO:0000305|PubMed:10846217}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC esterase 3 (CE3) family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the carbohydrate
CC esterase 15 (CE15) family. {ECO:0000305}.
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; AJ238716; CAB55348.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RLB8; -.
DR SMR; Q9RLB8; -.
DR STRING; 1265.SAMN02910280_2771; -.
DR ESTHER; rumfl-CESA; Glucuronoyl_esterase.
DR BRENDA; 3.1.1.117; 5478.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Multifunctional enzyme;
KW Polysaccharide degradation; Secreted; Serine esterase; Signal;
KW Xylan degradation.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..768
FT /note="Multidomain esterase"
FT /id="PRO_5004331521"
FT DOMAIN 285..352
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT REGION 41..264
FT /note="Acetylxylan esterase"
FT /evidence="ECO:0000305"
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..768
FT /note="Glucuronoyl esterase"
FT /evidence="ECO:0000305|PubMed:26216754"
FT MOTIF 563..568
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT COMPBIAS 267..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 68
FT /note="Nucleophile; for acetylxylan esterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 240
FT /note="For acetylxylan esterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 243
FT /note="For acetylxylan esterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 565
FT /note="Nucleophile; for glucuronoyl esterase activity"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 569
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 633
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 679
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 768 AA; 84835 MW; 420883356109417E CRC64;
MKKHFVVGET IKRFLRIGTS LALSISTLSL LPSAPRLSSA AGTIKIMPLG DSITYGMADE
GGYRKYLSYF LQQKGYTNVD LVGPEGKDSA SFNYNGQSVK YDDNHAGYSG YTITNLPGGW
FGQLNGILET MQGGDYIKKY SPDIILLQIG TNDVSNGHLD GSEERLHKLL DYLRENMPSN
GKVFLTTIPD LGNSGWGGNS NGDIAKYNEL IKKVANDYSS KNVIYADIHS VIDASKDLAD
GVHPNAGGYE KMGKYWLEQI EGYLKASDGP QQTQPTQPSQ GDSGPELIYG DLDGDKTITS
FDAVIMRKGL INDFKDNNVK KAADIDQNGK AEVADLVQLQ SFIIGKIKEF TVAEKTVTEK
PVFEKSYNFP AVNQLKSSKD IPDPFIFMDG SKVESTDDWW KRQSEISCMY EYYMYGKWID
GSDDETTYSI SGNSMTINVK RKSTGKTASF KAVINLPKNV RHEGGAPVIL GMHKGISEST
ATSNGYAVIT YDSDGMFSAP GTAQDNNQHK GAFYDLYPYG RNWDEQTGDL MAWSWGISRI
LDALYNGAAK ELNINPDSSI VTGVSRYGKA ASVCGAFDTR IKMCAPSCSG AGGLALYRYS
SVGKTYDFSS KGGSSSYTYK ENEPLGSLQA SGEQGWFNGR FMEFRNAEQF PMDQHMLGAL
CCDPDRYLFI IGSCESEDWV NAPSVWMAYL GMKHVWDYVG ISDHLAINIH KSGHAVIAED
IEKMVQYFDY HVYGIQPKMN LEELQTSVFA LPKNKDSFAD TFASKWLY
