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Carbohydrate esterase MZ0003 (EC 3.1.1.-)

 CE15_UNKP               Reviewed;         432 AA.
A0A0K2VM55;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
11-NOV-2015, sequence version 1.
12-APR-2017, entry version 4.
RecName: Full=Carbohydrate esterase MZ0003 {ECO:0000305|PubMed:27433797};
EC=3.1.1.- {ECO:0000269|PubMed:27433797};
Flags: Precursor;
Name=MZ0003 {ECO:0000312|EMBL:CDW92038.1};
Unknown prokaryotic organism.
Bacteria; environmental samples.
NCBI_TaxID=2725;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tian C., Fan X.;
"Three species of the Botryosphaeriales overlap on five unrelated
trees in China, with a novel species.";
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, ESTERASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
SPECIFICITY, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION,
3D-STRUCTURE MODELING, MUTAGENESIS OF 152-LYS-GLU-153; SER-268;
CYS-291 AND HIS-409, AND ACTIVE SITE.
PubMed=27433797; DOI=10.1371/journal.pone.0159345;
De Santi C., Willassen N.P., Williamson A.;
"Biochemical characterization of a family 15 carbohydrate esterase
from a bacterial marine arctic metagenome.";
PLoS ONE 11:E0159345-E0159345(2016).
-!- FUNCTION: Displays some glucuronoyl esterase activity in vitro,
since it is able to hydrolyze methyl 4-O-methyl-D-
glucopyranosyluronate, allyl D-glucuronate, benzyl D-glucuronate
and D-glucuronic acid methyl ester. However, esters of glucuronic
acid are probably not its biological substrate, as they are not
present in the marine environment. Can also hydrolyze a range of
other esters, including p-nitrophenyl acetate. More likely
biologically-relevant substrates for MZ0003 and other marine
bacterial CE15s are algal cell wall polysaccharides, as these
would be readily available in this environment and could be used
as energy sources. {ECO:0000269|PubMed:27433797}.
-!- COFACTOR:
Note=Does not require metal ions for activity.
{ECO:0000269|PubMed:27433797};
-!- ENZYME REGULATION: Is inhibited by PMSF and by NaF in vitro, which
is consistent with the catalytic nucleophile being a serine.
{ECO:0000269|PubMed:27433797}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.71 mM for p-nitrophenyl acetate (in the absence of NaCl)
{ECO:0000269|PubMed:27433797};
KM=0.97 mM for p-nitrophenyl acetate (in the presence of 1M
NaCl) {ECO:0000269|PubMed:27433797};
Note=kcat is 8.9 sec(-1) with p-nitrophenyl acetate as substrate
(in the absence of NaCl). kcat is 12.78 sec(-1) with p-
nitrophenyl acetate as substrate (in the presence of 1M NaCl).
{ECO:0000269|PubMed:27433797};
pH dependence:
Optimum pH is 8.0. Shows more than 60% of its maximum activity
in the pH range of 7.0-9.5. 20% of the activity is retained at
low pH range and at pH 10.5, while no catalytic activity is
found at pH 5.0 or 10.5. {ECO:0000269|PubMed:27433797};
Temperature dependence:
Optimum temperature is 35 degrees Celsius with p-nitrophenyl
acetate as substrate. Above 35 degrees Celsius, activity
significantly decreases, while 30% of the maximum activity is
recorded at 10 degrees Celsius. {ECO:0000269|PubMed:27433797};
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:27433797}.
-!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
{ECO:0000305|PubMed:27433797}.
-----------------------------------------------------------------------
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EMBL; LM651246; CDW92038.1; -; Genomic_DNA.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Hydrolase; Periplasm;
Polysaccharide degradation; Serine esterase; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 432 Carbohydrate esterase MZ0003.
/FTId=PRO_0000439191.
MOTIF 266 271 GXSYXG catalytic site motif.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 268 268 Nucleophile.
{ECO:0000305|PubMed:27433797}.
ACT_SITE 409 409 Charge relay system.
{ECO:0000305|PubMed:27433797}.
BINDING 272 272 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 359 359 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
MUTAGEN 152 153 KE->AA: No effect on esterase activity.
{ECO:0000269|PubMed:27433797}.
MUTAGEN 268 268 S->A: Loss of esterase activity.
{ECO:0000269|PubMed:27433797}.
MUTAGEN 291 291 C->A: No effect on esterase activity.
{ECO:0000269|PubMed:27433797}.
MUTAGEN 409 409 H->A: Loss of esterase activity.
{ECO:0000269|PubMed:27433797}.
SEQUENCE 432 AA; 48457 MW; 57E02D3A26F662F7 CRC64;
MQRTCVLIVL IVTSTMWTPD PDVYAQPRGF NYDEAQVPKY TLPDPLVMVD GTKVTSAKQW
NDKRRDEVQQ LFEAYMYGKV PDGETELIFT DAKGERALGG AAIRKQVKIS FGEKEDAPAM
DLLIYLPADA KVRVPVFLGL NFHGNHTIHK DKEIWLTESW VRTNKKFGIT KNKANELSRG
VAAGRWQIEK AIAKGYGVAT IYCGDIDPDF NFPSNGIQAY YYKKDQTIPE KGQWGTIAAW
AFGLSCAMDY FETDTDIDHK KVAVLGHSRL GKTSLWAGAI DTRFALTISN CSGCGGAALS
RRRFGETVRR INTSFPHWFC SRFHQYNDKE DKLPIDQHML IALCAPRPVL INSATEDKWA
DPHGEFLAAQ GADAVYRMLG TGGLDAKKWP EPNKLVKSTI GYHLRPGKHD VTARDWDVYI
EFADHHMTGG AE


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