CE2A_CELJU
ID CE2A_CELJU Reviewed; 358 AA.
AC B3PIB0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=CjCE2A {ECO:0000303|PubMed:19338387};
DE Flags: Precursor;
GN Name=axe2C {ECO:0000312|EMBL:ACE84991.1};
GN OrderedLocusNames=CJA_0450 {ECO:0000312|EMBL:ACE84991.1};
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 (1.80 ANGSTROMS) OF 21-358, FUNCTION, CATALYTIC
RP ACTIVITY, 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 equal efficiency, and of the synthetic
CC substrate 4-nitrophenyl acetate (4-NPAc). Does not bind cellulose,
CC cellohexaose and beta-glucan. {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=339 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:19338387};
CC KM=1.5 mM for acetylated birchwood xylan
CC {ECO:0000269|PubMed:19338387};
CC KM=4.2 mM for acetylated glucomannan {ECO:0000269|PubMed:19338387};
CC Note=kcat is 7717 min(-1) for the deacetylation of 4-nitrophenyl
CC acetate. kcat is 69 min(-1) for the deacetylation of birchwood xylan.
CC kcat is 163 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: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 2 (CE2) family.
CC {ECO:0000305|PubMed:19338387}.
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DR EMBL; CP000934; ACE84991.1; -; Genomic_DNA.
DR RefSeq; WP_012486130.1; NC_010995.1.
DR PDB; 2WAA; X-ray; 1.80 A; A=21-358.
DR PDBsum; 2WAA; -.
DR AlphaFoldDB; B3PIB0; -.
DR SMR; B3PIB0; -.
DR STRING; 498211.CJA_0450; -.
DR EnsemblBacteria; ACE84991; ACE84991; CJA_0450.
DR KEGG; cja:CJA_0450; -.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_042506_2_0_6; -.
DR OMA; ACIAARM; -.
DR OrthoDB; 1247435at2; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; B3PIB0; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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; Cell membrane; Glycosidase;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Polysaccharide degradation;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..358
FT /note="Acetylxylan esterase / glucomannan deacetylase"
FT /id="PRO_0000434123"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:19338387"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:19338387"
FT ACT_SITE 335
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:19338387"
FT SITE 205
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:19338387"
FT SITE 255
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:19338387"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 61..80
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 103..122
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:2WAA"
FT TURN 160..168
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2WAA"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2WAA"
FT HELIX 338..356
FT /evidence="ECO:0007829|PDB:2WAA"
SQ SEQUENCE 358 AA; 39779 MW; C12DB2C29F4B819E CRC64;
MKLLFPILLL TGSYFLSACN NTQSLMSSTH TIAASDPHIQ VMGRTHINDD ASLTFGYPGV
SLSTIVAGSR LTAEMQSSNG NSWIDVIIDN HPPTSIKLDA QQQTVELFHF PNSGEHRVEI
IHRSENWHGQ VTLKQLTLTG TQFLPAPVLP QRKILVLGDS VTCGEAIDRV AGEDKNTRWW
NARESYGMLT AKALDAQVQL VCWGGRGLIR SWNGKTDDAN LPDFYQFTLG DTGQAPQWDH
HRYQPDLIIS AIGTNDFSPG IPDRATYINT YTRFVRTLLD NHPQATIVLT EGAILNGDKK
AALVSYIGET RQQLHSNRVF YASSSHHPGD NSDAHPTKDQ HAAMARELTP QLRQIMDW
