CHLE_ASPNG
ID CHLE_ASPNG Reviewed; 512 AA.
AC A7YN26;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Chlorogenic acid esterase {ECO:0000303|PubMed:17630312};
DE EC=3.1.1.42 {ECO:0000269|PubMed:17630312};
DE AltName: Full=Chlorogenic acid hydrolase {ECO:0000303|PubMed:17630312};
DE Short=CGA hydrolase {ECO:0000303|PubMed:17630312};
DE Flags: Precursor;
GN Name=chlE {ECO:0000303|PubMed:17630312};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=17630312; DOI=10.1128/aem.00374-07;
RA Benoit I., Asther M., Bourne Y., Navarro D., Canaan S., Lesage-Meessen L.,
RA Herweijer M., Coutinho P.M., Asther M., Record E.;
RT "Gene overexpression and biochemical characterization of the
RT biotechnologically relevant chlorogenic acid hydrolase from Aspergillus
RT niger.";
RL Appl. Environ. Microbiol. 73:5624-5632(2007).
CC -!- FUNCTION: Extracellular chlorogenic acid esterase that releases caffeic
CC acid from chlorogenic acid (CGA) contained in natural substrates such
CC as apple marc and coffee pulp (PubMed:17630312). Shows no activity
CC towards 5-O-p-coumaroyl quinic acid, another quinic ester derivative,
CC and rosmarinic acid, another caffeic ester derivative
CC (PubMed:17630312). {ECO:0000269|PubMed:17630312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorogenate + H2O = (E)-caffeate + H(+) + L-quinate;
CC Xref=Rhea:RHEA:20689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29751, ChEBI:CHEBI:57644, ChEBI:CHEBI:57770; EC=3.1.1.42;
CC Evidence={ECO:0000269|PubMed:17630312};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20690;
CC Evidence={ECO:0000269|PubMed:17630312};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 uM for chlorogenic acid {ECO:0000269|PubMed:17630312};
CC Vmax=250 nmol/sec/mg enzyme towards chlorogenic acid
CC {ECO:0000269|PubMed:17630312};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000303|PubMed:17630312};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000303|PubMed:17630312};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17630312}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; DQ993161; ABK62698.1; -; Genomic_DNA.
DR ESTHER; aspnc-a2qn56; Fungal_carboxylesterase_lipase.
DR VEuPathDB; FungiDB:An07g04470; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1184088; -.
DR VEuPathDB; FungiDB:ATCC64974_46350; -.
DR VEuPathDB; FungiDB:M747DRAFT_360378; -.
DR BioCyc; MetaCyc:MON-16433; -.
DR BRENDA; 3.1.1.42; 518.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047745; F:chlorogenate hydrolase activity; IEA:RHEA.
DR Gene3D; 3.40.50.1820; -; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..512
FT /note="Chlorogenic acid esterase"
FT /id="PRO_5005121924"
FT ACT_SITE 230
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT ACT_SITE 351
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT ACT_SITE 416
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 92..120
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT DISULFID 281..292
FT /evidence="ECO:0000250|UniProtKB:P21836"
SQ SEQUENCE 512 AA; 55265 MW; D01000FECC9E8D49 CRC64;
MLLRLCIIAT LLVSHCVAVS TSPATRDTNG EGLLVQTSSG PIQGFFNQTA PDVRQWLGVP
FAEPPVGDLR FSSPVKKQPN GTVNAFALPS SCIQQTSNSS TIYTTYETGF LISGGDSEDC
LYLSIWAPRI ENIQSQQRPL PVLLYIPGGG FTSGGEASLY KIPDKWVQRT QSHIVVIMNY
RVNVFGFPNA EGLSEPNVGL LDQRMAVEWV AANIANFGGD PARIALWGQS AGAASVTAYS
YGYPEDPIVA ALIADSGAPN IVDNEDYAHT NFTFLASLVG CDGLSSTEEL SCMRNVSARK
LQTALSTYSG SPSISFTPAV DNKTFFANWT ERAITGKVAK IPLITGSNTN EGAGFVSFTP
AGPSKSTLFE ITESIIACPV AEEVKNRNLA NLTTYRYQYA GNFTNISPLP WFGAYHSAEL
PILFGTHYEY GGPSTQYEWD VSYAMQALWL SFVEDPTRGP VRLAVGNVPA NPTNESYFAW
PAFEQGSDDL LVFAEGGKVM QLVGAGRIDD YC
