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Database: UniProt
Entry: A0A0D9ZMM7_9ORYZ
LinkDB: A0A0D9ZMM7_9ORYZ
Original site: A0A0D9ZMM7_9ORYZ 
ID   A0A0D9ZMM7_9ORYZ        Unreviewed;       641 AA.
AC   A0A0D9ZMM7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM04G17460.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM04G17460.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM04G17460.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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 glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   AlphaFoldDB; A0A0D9ZMM7; -.
DR   STRING; 40148.A0A0D9ZMM7; -.
DR   EnsemblPlants; OGLUM04G17460.1; OGLUM04G17460.1; OGLUM04G17460.
DR   Gramene; OGLUM04G17460.1; OGLUM04G17460.1; OGLUM04G17460.
DR   eggNOG; ENOG502QSIM; Eukaryota.
DR   HOGENOM; CLU_008926_1_3_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF64; ENDOGLUCANASE 7; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059}; Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          111..601
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        531
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        588
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   641 AA;  71117 MW;  3F8FFE377AD88FFD CRC64;
     MYSANHWGGS FEIAADGAAE DDHSRNMDLD RGALSARQHQ LDETQQSWLL GPPEAKKKDK
     YVDLGCVVVK RKLLWWVLWT LLAAFILIGL PVIIAKSIPK KKPHAPPPDQ YTDALHKALL
     FFNAQKSLLS LTNNFGHVSF SALTAGRLPK NNGIKWRGNS GLSDGSDLTD VKGGLVGGYY
     DAGDNIKFHF PLAFSMTMLS WSVIEYSAKY KAVGEYDHVR ELIKWGTDYL LLTFNSSAST
     IDKVYSQVGI AKINGTQPDD HYCWNRPEDM AYPRPVQTAG SAPDLGGEMA AALAAASIVF
     RDNAAYSKKL VNGAAAVYKF ARSSGRRTPY SRGNQYIEYY YNSTSYWDEY MWSAAWMYYA
     TGNNTYITFA TDPRLPKNAK AFYSILDFSV FSWDNKLPGA ELLLSRLRMF LNPGYPYEES
     LIGYHNTTSM NMCTYFPRFG AFNFTKGGLA QFNHGKGQPL QYTVANSFLA ALYADYMESV
     NVPGWYCGPY FMTVDDLRSF ARSQVNYILG DNPKKMSYVV GYGKKYPRRL HHRGASTPHN
     GIKYSCTGGY KWRDTKGADP NVLVGAMVGG PDKNDQFKDA RLTYAQNEPT LVGNAGLVAA
     LVALTNSGRG AGVTAVDKNT MFSAVPPMFP ATPPPPSKWK P
//
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