UniProt: A0A2G9HXK3

Database: UniProt
Entry: A0A2G9HXK3_9LAMI

LinkDB:  A0A2G9HXK3_9LAMI 
Original site:  A0A2G9HXK3_9LAMI

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   A0A2G9HXK3_9LAMI        Unreviewed;       617 AA.
AC   A0A2G9HXK3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=CDL12_05044 {ECO:0000313|EMBL:PIN22247.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN22247.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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}.
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:PIN22247.1}.
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DR   EMBL; NKXS01000796; PIN22247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9HXK3; -.
DR   STRING; 429701.A0A2G9HXK3; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000231279; 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:SF36; ENDOGLUCANASE 25; 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:UP000231279};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        72..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..581
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        511
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        559
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   617 AA;  68733 MW;  F83456813CDFD521 CRC64;
     MSMYGRDPWG GPLEIAADSA TDDDRSRNLQ DYDRAALSRP LDETQQSWLL GPGEQKKKKY
     VDLGCIIVSR KIFVWTVGTI LAAGFLAGFI TLIVKTVPRH HHRPPPPDNY TLALNKALMF
     FNAQRSGKLP KHNNVSWRGN SCLNDGKSES SPLFKDLIGG YYDAGDAIKF NFPQSFAMTM
     LSWSVIEYSA KYEAAGELNH VKDIIKWGTD YFLKTFNHTA DSIDRIVAQV GIGDTSGGPE
     PNDHYCWVRP EDIDYARPVT ECSSCSDLAA EMAAALASAS IVFKDNKAYS QKLVHGAKTL
     FKFSRDQRGR YSVGNEASIF YNSTSYWDEF VWGATWLYYA TGNSSYLQLA TTPGIAKHAG
     AFWGGPYYGV LSWDNKLAGA QVLLSRMRLF LSPGYPYEEI LRTFHNQTSI FMCSFLPYYT
     SFNRTKGGLI QLNHGAPQPL QYVVNAAFLA TVFSDYMKAA DTPGWYCGPH FYSADVLREF
     AQTQMNYILG KNPRKMSYVV GFGNHYPKRV HHRGASIPKN KVRYNCKGGW KWRDSKKPNP
     NTIVGAMVAG PDRHDGFHDV RTNYNYTEPT LAGNAGLVAA LVALSGDTNV GVDKNTIFSA
     VPPMFPTPPP PPAPWKP
//

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