CHLE_USTMD
ID CHLE_USTMD Reviewed; 585 AA.
AC A0A060S684;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Chlorogenic acid esterase {ECO:0000303|Ref.1};
DE EC=3.1.1.42 {ECO:0000269|Ref.1};
DE Flags: Precursor;
GN Name=chlE {ECO:0000303|Ref.1};
OS Ustilago maydis (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=5270;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=17144;
RX DOI=10.1128/AEM.02911-14;
RA Nieter A., Haase-Aschoff P., Kelle S., Linke D., Krings U., Popper L.,
RA Berger R.G.;
RT "A chlorogenic acid esterase with a unique substrate specificity from
RT Ustilago maydis.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
CC -!- FUNCTION: Extracellular chlorogenic acid esterase that displays a
CC surprisingly broad substrate profile (Ref.1). The enzyme's unique
CC properties may contribute to the specific environmental interaction
CC between the pathogenic fungus and its host, Zea mays (Ref.1).
CC Additionally, the release of caffeic, p-coumaric, and ferulic acids
CC from agroindustrial by-products such as destarched wheat bran (DSWB)
CC and coffee pulp (CP) renders this enzyme an attractive candidate for
CC the generation of natural aroma precursors and antioxidants (Ref.1).
CC {ECO:0000269|Ref.1}.
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|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20690;
CC Evidence={ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.6 uM for chlorogenic acid {ECO:0000269|Ref.1};
CC KM=64.1 uM for methyl p-coumarate {ECO:0000269|Ref.1};
CC KM=72.5 uM for methyl caffeate {ECO:0000269|Ref.1};
CC KM=101.8 uM for methyl ferulate {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000303|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. {ECO:0000303|Ref.1};
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; HG970190; CDO67308.1; -; mRNA.
DR SMR; A0A060S684; -.
DR ESTHER; ustma-A0A0D1CFG4; Fungal_carboxylesterase_lipase.
DR VEuPathDB; FungiDB:UMAG_00182; -.
DR BRENDA; 3.1.1.42; 6587.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..585
FT /note="Chlorogenic acid esterase"
FT /id="PRO_5005102577"
FT ACT_SITE 228
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 98..114
FT /evidence="ECO:0000250|UniProtKB:P21836"
FT DISULFID 285..293
FT /evidence="ECO:0000250|UniProtKB:P21836"
SQ SEQUENCE 585 AA; 63689 MW; 760AB6F6115DFC28 CRC64;
MRLPNLTLLV WAATSVGLVS ALPQVSYKAD ATASAPTVKL HQGTVRGLAD DNYGLEQFFG
IPYAKPPVGS LRFAKPQPLG PASSHKTVID ATRFGDICMQ TVAPSPLYNM SEDCLNLNVV
RPKGTTAKDK LPVLVWIYGG AFRQGSTPIY NASELVQKSV EIGKPIVFVA ISYRVGPFGF
IGGSEIADSD SATSNAGLYD QRLGLKWIRH NIGKFGGDKN RVTLFGQSAG AMSIALQNFA
YDGNNHGLWH AAIMNSGGIA PGPLLTPKHP TVEQSFKRLA NGVGCTGGSL LRCLRKANAS
EVQTVASNLT AQAGGTFPIP GALAWLPLVD YELITNYPSV NLPQGKLADI PVIQGNALDE
GTSFAQKQLN SSADFERWVR SAAVIHNTSY TEQALQKVFE LYPDVPEQGS PFYNAETATS
AATTSDLNSR QYPPLTSNQY KRSAAFFGDF TFQAQRRTYL KAATLGWKKN KAKVWSYEFQ
QNDKFANGTG SLLGPYHGAD VKYYFIRPDG RQKDPVLADR MPRAYISFVY HHDPTVLGGF
EWPPYGKGKK LLQMKGDNTT VIEDAYRKEA MDALTNRKAA KVFGF
