ID A0A498JDR1_MALDO Unreviewed; 1113 AA.
AC A0A498JDR1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=DVH24_020524 {ECO:0000313|EMBL:RXH91501.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH91501.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH91501.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH91501.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the chalcone isomerase family.
CC {ECO:0000256|ARBA:ARBA00007166}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC ECO:0000256|RuleBase:RU361166}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH91501.1}.
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DR EMBL; RDQH01000334; RXH91501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498JDR1; -.
DR STRING; 3750.A0A498JDR1; -.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000290289; Chromosome 8.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.890.20; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.50.70.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR016087; Chalcone_isomerase.
DR InterPro; IPR016088; Chalcone_isomerase_3-sand.
DR InterPro; IPR016089; Chalcone_isomerase_bundle_sf.
DR InterPro; IPR036298; Chalcone_isomerase_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF104; ENDOGLUCANASE 16; 1.
DR Pfam; PF16035; Chalcone_2; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF54626; Chalcone isomerase; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361166};
KW Flavonoid biosynthesis {ECO:0000256|ARBA:ARBA00023241};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10059}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT DOMAIN 227..399
FT /note="Chalcone isomerase"
FT /evidence="ECO:0000259|Pfam:PF16035"
FT DOMAIN 459..870
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 71..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 815
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ SEQUENCE 1113 AA; 122610 MW; C1110D942EA74507 CRC64;
MRIKRFGFMD FDEGSPYNSH FTSLADNSLH RCRYFHVPGS LALEGAFNHV SKLAGSLPFF
FSSGPNTNAS REIEGNLHDS EPGHSTSSPQ VKHFTSGRHN LKGFHFGFAL RGESANAVVF
GKISAFVMQF LHREGEKLHS HPMLSLAAGL VPPFGSLSSN VLAVPLENTD VMDQKPCEVE
HHRCAGLPFP DLDWRKQAVE PKTGTEFPMI LDNVLTQESN SSLSSEVLVG TGSKTMTIIK
IKSLKLYAFG FYVHPHSVCK QLGAKYASIS VDELNKRHDF YEDLLRADID MTVRLVVNCN
GMKIDTVRDV FEKSLRDRLV KTNPETDYHC IRTFGSNFTQ DIPLPLGTTI DFQRTADGNL
ITKIEGNQVG AVHSKDLCRA FFDMYLGDVP VSEQTKEEIG RNVVNIIRNI SSTVPDVEDV
DVAGKHYKGN QRGVVAVVVA CLAIFQGLVL SVHGTGFNYK DALTKSIIFL EAQRSGKLPP
NHRPAWRGDS ALDDGKEANY GLPMAFTVTT LSWAAMFYRQ QLQATGELEN VLAGIKWGTD
YFLKAASKNR LYVQVGDPNK DHECWTRPED MQTPRTVLKI DDKTPGTEIA AETSAAMAAS
AIVFRKTDRA YARRLLNKAK LLFQMAKAHK GTYDGECPFY CSYSGYNDEL LWAATWLYIA
TKRPVYLKYI QEEAISATVS EFSWDLKYAG AQVLLAKLFF DGEKSLENYK NGADSYICSN
IPDSPYHQIT MTPGGMIHLR DGANTQYVTG TAHLFAVYSD ILAQHNQKVN CGGKQFDSAA
LMAFAKKQMD YLLGDNPKKR SYMVGFGPNA PQQPHHRGAS VPKSENSLVN CAMSFVYWFK
KDVPNPNELT GAIVGGPDRF DNFEDKRWAS SAAARIGIAP SSGFACGGLL FDSPETRRRV
PAGEVSVSSA SSSSIGKNSD DESERYDGGE NDEAQSSYKG PLDMMNELEE VLPMRRGISK
YYNYKSKSFT SLVGASSSSN IKELAKPDNA YTRKRRNLLA SNHMWEKNRT SLPLRSNGGG
ISKRPIPSSR SALALAVKLG NCSESSTSST SEESNSSSNP TSPRPPLPPG YACPLGGYAA
WRSYSLADLQ ECTTATTANT SRFSAASMTK PNV
//
