EG5A_PHACH
ID EG5A_PHACH Reviewed; 386 AA.
AC Q66NB7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Manganese dependent endoglucanase Eg5A {ECO:0000303|PubMed:26173955};
DE EC=3.2.1.4 {ECO:0000269|PubMed:26173955};
DE AltName: Full=Carboxymethyl-cellulase 5A {ECO:0000305|PubMed:26173955};
DE Short=CMCase 5A {ECO:0000305|PubMed:26173955};
DE Short=Cellulase 5A {ECO:0000305|PubMed:15888348};
DE AltName: Full=Endo-1,4-beta-glucanase Eg5A {ECO:0000305|PubMed:26173955};
DE Flags: Precursor;
GN Name=Eg5A {ECO:0000303|PubMed:26173955};
GN Synonyms=cel5A {ECO:0000303|PubMed:15888348};
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15888348; DOI=10.1016/j.jbiotec.2005.03.010;
RA Wymelenberg A.V., Sabat G., Martinez D., Rajangam A.S., Teeri T.T.,
RA Gaskell J., Kersten P.J., Cullen D.;
RT "The Phanerochaete chrysosporium secretome: database predictions and
RT initial mass spectrometry peptide identifications in cellulose-grown
RT medium.";
RL J. Biotechnol. 118:17-34(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP BIOTECHNOLOGY.
RX PubMed=26173955; DOI=10.1016/j.jbiosc.2015.06.009;
RA Huy N.D., Nguyen C.L., Park H.S., Loc N.H., Choi M.S., Kim D.H., Seo J.W.,
RA Park S.M.;
RT "Characterization of a novel manganese dependent endoglucanase belongs in
RT GH family 5 from Phanerochaete chrysosporium.";
RL J. Biosci. Bioeng. 121:154-159(2016).
CC -!- FUNCTION: Secreted manganese dependent endoglucanase that acts by
CC cleaving the beta-1,4-glucose linkage (PubMed:26173955). Exhibits high
CC activity toward carboxymethyl-cellulose (CMC), barley glucan, and
CC glucomannan (PubMed:26173955). Displays low activity on larminarin and
CC xyloglucan but does not hydrolyze hemicellulose substrates such as
CC birchwood xylan, arabinoxylan, and arabinan (PubMed:26173955).
CC {ECO:0000269|PubMed:26173955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000269|PubMed:26173955};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26173955};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for carboxymethyl-cellulose (CMC)
CC {ECO:0000269|PubMed:26173955};
CC Vmax=208 umol/min/mg enzyme toward carboxymethyl-cellulose (CMC)
CC {ECO:0000269|PubMed:26173955};
CC pH dependence:
CC Optimum pH is 4.5-6.0. {ECO:0000269|PubMed:26173955};
CC Temperature dependence:
CC Optimum temperature is 50-60 degrees Celsius.
CC {ECO:0000269|PubMed:26173955};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15888348}.
CC -!- BIOTECHNOLOGY: Displays a synergistic action with cellobiase resulting
CC in an increase of the saccharification of NaOH-pretreated barley straw,
CC promising a further use of this enzyme in biomass saccharification
CC purpose (PubMed:26173955). {ECO:0000269|PubMed:26173955}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; AY682743; AAU12275.2; -; mRNA.
DR AlphaFoldDB; Q66NB7; -.
DR SMR; Q66NB7; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR VEuPathDB; FungiDB:AGR57_10566; -.
DR BRENDA; 3.2.1.4; 1380.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..386
FT /note="Manganese dependent endoglucanase Eg5A"
FT /id="PRO_5004269074"
FT DOMAIN 18..53
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:26173955"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:26173955"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 386 AA; 40412 MW; F52006CA88CEE055 CRC64;
MLKYASIALA LATLGVAQQQ QWGQCGGIGW TGATTCVAGS VCSVLNPYYS QCIPGAATVT
SSSAPSTPTP PAGALPRLGG VNTAGYDFSV ATDGSFTGTG VSPPVSQFSH FSSQGANLYR
IPFAWQLMTP TLGGTISQSF LSRYDQTVQA ALNSGPNVFV IIDLHNYARW NGGIIAQGGP
TDAQFQSIWT QLAQKYGSNQ RVIFGIMNEP HDIPSISTWV NSVQGAVNAI RAAGATNYLL
LPGSSWSSAQ AFPTEAGPLL VKVTDPLGGT SKLIFDVHKY LDSDNSGTHP DCTTDNVQVL
QTLVQFLQAN GNRQAILSET GGGNTSSCES LLANELAYVK SAYPTLAGFS VWAAGAFDTT
YVLTVTPNAD GSDQPLWVDA VKPNLP
