GUN1_SAIFL
ID GUN1_SAIFL Reviewed; 341 AA.
AC Q04469;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Endoglucanase 1;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethyl-cellulase 1;
DE Short=CMCase 1;
DE Short=Cellulase 1;
DE AltName: Full=Endo-1,4-beta-glucanase 1;
DE Flags: Precursor;
GN Name=CMC1;
OS Saitozyma flava (Cryptococcus flavus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=5416;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1368837; DOI=10.1271/bbb.56.1230;
RA Cui Z., Mochizuki D., Matsuno Y., Nakamura T., Liu Y., Hatano T., Fukui S.,
RA Miyakawa T.;
RT "Cloning and molecular analysis of cDNA encoding a carboxymethylcellulase
RT of the yeast Cryptococcus flavus.";
RL Biosci. Biotechnol. Biochem. 56:1230-1235(1992).
CC -!- FUNCTION: Has endoglucanase activity on carboxymethyl-cellulose (CMC).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D13967; BAA03070.1; -; mRNA.
DR EMBL; S45137; AAC60541.1; -; Genomic_DNA.
DR PIR; JC1201; JC1201.
DR AlphaFoldDB; Q04469; -.
DR SMR; Q04469; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EGL5A_CRYFL; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cellulose degradation;
KW Cleavage on pair of basic residues; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000007855"
FT CHAIN 31..341
FT /note="Endoglucanase 1"
FT /id="PRO_0000007856"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 35717 MW; 4A62E45C952DD120 CRC64;
MKTATLLAAL SVLAGALAAP LAGDSALHRR SLPRLGGVNL AGCDFGIDIY GNSGTPACPG
TEQVGHFIAD GANLFRLPAG WQYLVGNNQA STSLAPDFFA QYDALVQAVI SKGAYAIIDV
HNYARWNGAI IGQGGPSNQD FANLWTLLAT KVTSNDPNVI FGLMNEPHDL DVSTWAGSVQ
AAVNAIRAAG ATSQYILIPG TGFTNANAWF QGQDNALLGV TDPVGGTDKL LLDVHRYNDV
DFSGTHAECT TNSLDVLSSL DSWLKGNGRK AIVSETGGGH TTSCETDLGE FLNGIKEDYP
SVLGFAVWAA GSFDPSYVLS ITPTNGVDNQ LFDIAVKPNL P