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Multidomain esterase [Includes: Acetylxylan esterase (EC 3.1.1.72); 4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.-) (Glucuronoyl esterase) (GE)]

 CESA_RUMFL              Reviewed;         768 AA.
Q9RLB8;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 60.
RecName: Full=Multidomain esterase {ECO:0000303|PubMed:10846217};
Includes:
RecName: Full=Acetylxylan esterase {ECO:0000303|PubMed:10846217};
EC=3.1.1.72 {ECO:0000269|PubMed:10846217};
Includes:
RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305|PubMed:26216754};
EC=3.1.1.- {ECO:0000269|PubMed:26216754};
AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:26216754};
Short=GE {ECO:0000303|PubMed:26216754};
Flags: Precursor;
Name=cesA {ECO:0000303|PubMed:10846217};
Ruminococcus flavefaciens.
Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
Ruminococcus.
NCBI_TaxID=1265;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION OF THE N-TERMINAL DOMAIN
AS AN ACETYLXYLAN ESTERASE, CATALYTIC ACTIVITY, PATHWAY, AND DOMAIN.
STRAIN=17;
PubMed=10846217;
Aurilia V., Martin J.C., McCrae S.I., Scott K.P., Rincon M.T.,
Flint H.J.;
"Three multidomain esterases from the cellulolytic rumen anaerobe
Ruminococcus flavefaciens 17 that carry divergent dockerin
sequences.";
Microbiology 146:1391-1397(2000).
[2]
FUNCTION OF THE C-TERMINAL DOMAIN AS A GLUCURONOYL ESTERASE.
STRAIN=17;
PubMed=26216754; DOI=10.1016/j.febslet.2015.07.019;
Biely P., Malovikova A., Uhliarikova I., Li X.L., Wong D.W.;
"Glucuronoyl esterases are active on the polymeric substrate methyl
esterified glucuronoxylan.";
FEBS Lett. 589:2334-2339(2015).
-!- FUNCTION: Esterase involved in the degradation of plant cell wall
polysaccharides. Catalyzes the deacetylation of chemically
acetylated xylan and native, steam-extracted xylan
(PubMed:10846217). Seems to act in synergy with the xylanase XynD
which produces xylo-oligosaccharides (PubMed:10846217). Also
catalyzes the deesterification of methyl esters of 4-O-methyl-D-
glucuronic acid (MeGlcA) side residues in synthetic glucuronoxylan
methyl ester, suggesting that it may be able to cleave ester
linkages between MeGlcA carboxyl and more complex alcohols,
including linkages between hemicellulose and lignin alcohols in
plant cell walls (PubMed:26216754). {ECO:0000269|PubMed:10846217,
ECO:0000269|PubMed:26216754}.
-!- CATALYTIC ACTIVITY: Deacetylation of xylans and xylo-
oligosaccharides. {ECO:0000269|PubMed:10846217}.
-!- PATHWAY: Glycan degradation; xylan degradation.
{ECO:0000305|PubMed:10846217}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- DOMAIN: Contains a dockerin-like region in addition to its
catalytic domains, suggesting that this enzyme forms part of a
cellulosome-like multienzyme complex.
{ECO:0000305|PubMed:10846217}.
-!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
esterase 3 (CE3) family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the carbohydrate
esterase 15 (CE15) family. {ECO:0000305}.
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EMBL; AJ238716; CAB55348.1; -; Genomic_DNA.
ProteinModelPortal; Q9RLB8; -.
SMR; Q9RLB8; -.
UniPathway; UPA00114; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.1110; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR016134; Dockerin_dom.
InterPro; IPR036439; Dockerin_dom_sf.
InterPro; IPR001087; GDSL.
InterPro; IPR036514; SGNH_hydro_sf.
Pfam; PF00657; Lipase_GDSL; 1.
SUPFAM; SSF52266; SSF52266; 2.
SUPFAM; SSF63446; SSF63446; 1.
PROSITE; PS51766; DOCKERIN; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Hydrolase; Multifunctional enzyme;
Polysaccharide degradation; Secreted; Serine esterase; Signal;
Xylan degradation.
SIGNAL 1 40 {ECO:0000255}.
CHAIN 41 768 Multidomain esterase.
/FTId=PRO_5004331521.
DOMAIN 285 352 Dockerin. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
REGION 41 264 Acetylxylan esterase. {ECO:0000305}.
REGION 353 768 Glucuronoyl esterase.
{ECO:0000305|PubMed:26216754}.
MOTIF 563 568 GXSYXG catalytic site motif.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 68 68 Nucleophile; for acetylxylan esterase
activity. {ECO:0000250|UniProtKB:Q00017}.
ACT_SITE 240 240 For acetylxylan esterase activity.
{ECO:0000250|UniProtKB:Q00017}.
ACT_SITE 243 243 For acetylxylan esterase activity.
{ECO:0000250|UniProtKB:Q00017}.
ACT_SITE 565 565 Nucleophile; for glucuronoyl esterase
activity. {ECO:0000250|UniProtKB:G2QJR6}.
BINDING 569 569 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 633 633 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 679 679 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
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


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