CE2B_CELJU
ID CE2B_CELJU Reviewed; 360 AA.
AC B3PDE5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Acetylxylan esterase / glucomannan deacetylase {ECO:0000305|PubMed:19338387};
DE EC=3.1.1.- {ECO:0000269|PubMed:19338387};
DE EC=3.1.1.72 {ECO:0000269|PubMed:19338387};
DE AltName: Full=CjCE2B {ECO:0000303|PubMed:19338387};
DE Flags: Precursor;
GN Name=ce2C {ECO:0000312|EMBL:ACE85322.1};
GN OrderedLocusNames=CJA_3103 {ECO:0000312|EMBL:ACE85322.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
RX PubMed=19338387; DOI=10.1371/journal.pbio.1000071;
RA Montanier C., Money V.A., Pires V.M., Flint J.E., Pinheiro B.A., Goyal A.,
RA Prates J.A., Izumi A., Stalbrand H., Morland C., Cartmell A., Kolenova K.,
RA Topakas E., Dodson E.J., Bolam D.N., Davies G.J., Fontes C.M.,
RA Gilbert H.J.;
RT "The active site of a carbohydrate esterase displays divergent catalytic
RT and noncatalytic binding functions.";
RL PLoS Biol. 7:E71-E71(2009).
CC -!- FUNCTION: Involved in the degradation of plant cell wall
CC polysaccharides. Catalyzes the deacetylation of acetylated birchwood
CC xylan and glucomannan, with a large preference for the latter, and of
CC the synthetic substrate 4-nitrophenyl acetate (4-NPAc).
CC {ECO:0000269|PubMed:19338387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19338387};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=262 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:19338387};
CC KM=4.6 mM for acetylated birchwood xylan
CC {ECO:0000269|PubMed:19338387};
CC KM=0.84 mM for acetylated glucomannan {ECO:0000269|PubMed:19338387};
CC Note=kcat is 49820 min(-1) for the deacetylation of 4-nitrophenyl
CC acetate. kcat is 66 min(-1) for the deacetylation of birchwood xylan.
CC kcat is 1348 min(-1) for the deacetylation of glucomannan.
CC {ECO:0000269|PubMed:19338387};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000269|PubMed:19338387}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 2 (CE2) family.
CC {ECO:0000305|PubMed:19338387}.
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DR EMBL; CP000934; ACE85322.1; -; Genomic_DNA.
DR RefSeq; WP_012488681.1; NC_010995.1.
DR PDB; 2W9X; X-ray; 2.00 A; A/B=1-360.
DR PDBsum; 2W9X; -.
DR AlphaFoldDB; B3PDE5; -.
DR SMR; B3PDE5; -.
DR STRING; 498211.CJA_3103; -.
DR EnsemblBacteria; ACE85322; ACE85322; CJA_3103.
DR KEGG; cja:CJA_3103; -.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_042506_1_0_6; -.
DR OMA; TWPGTGV; -.
DR OrthoDB; 1247435at2; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; B3PDE5; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase activity; IDA:UniProtKB.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:2000884; P:glucomannan catabolic process; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR CDD; cd01831; Endoglucanase_E_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR040794; CE2_N.
DR InterPro; IPR037461; CtCE2-like_dom.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF17996; CE2_N; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..360
FT /note="Acetylxylan esterase / glucomannan deacetylase"
FT /id="PRO_0000434124"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:19338387"
FT SITE 199
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:B3PIB0"
FT SITE 247
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:B3PIB0"
FT SITE 336
FT /note="Increases nucleophilicity of active site Ser"
FT /evidence="ECO:0000305|PubMed:19338387"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:2W9X"
FT TURN 155..159
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 262..283
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:2W9X"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2W9X"
FT HELIX 339..354
FT /evidence="ECO:0007829|PDB:2W9X"
SQ SEQUENCE 360 AA; 40063 MW; 6F589FE17E026C9F CRC64;
MKPHALIGLL AGMLLSSSLY AADSTKPLPL HIGGRVLVES PANQPVSYTY SWPAVYFETA
FKGQSLTLKF DDDQNIFRLI VDDKAPVVIN KPGKVDYPVE SLAPGKHRVR LEKLTETQST
SGRFLGFYTD PSAKPLALPK RKRQIEFIGD SFTVGYGNTS PSRECTDEEL FKTTNSQMAF
GPLTAKAFDA DYQINASSGF GIVRNYNGTS PDKSLLSLYP YTLNNPDQLY HNKHWKPQVI
VIGLGTNDFS TALNDNERWK TREALHADYV ANYVKFVKQL HSNNARAQFI LMNSDQSNGE
IAEQVGKVVA QLKGGGLHQV EQIVFKGLDY SGCHWHPSAN DDQLLANLLI THLQQKKGIW
