UniProt: A0A087HPR7

Database: UniProt
Entry: A0A087HPR7_ARAAL

LinkDB:  A0A087HPR7_ARAAL 
Original site:  A0A087HPR7_ARAAL

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (12)   

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ID   A0A087HPR7_ARAAL        Unreviewed;       517 AA.
AC   A0A087HPR7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   OrderedLocusNames=AALP_Aa1g218000 {ECO:0000313|EMBL:KFK44119.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK44119.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
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   EMBL; CM002869; KFK44119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087HPR7; -.
DR   EnsemblPlants; KFK44119; KFK44119; AALP_AA1G218000.
DR   Gramene; KFK44119; KFK44119; AALP_AA1G218000.
DR   eggNOG; ENOG502QQZQ; Eukaryota.
DR   OMA; YLINCHP; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000029120; Chromosome 1.
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; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF114; ENDOGLUCANASE 2; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 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   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:UP000029120};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          50..503
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   517 AA;  56973 MW;  9EC357E38576DCA7 CRC64;
     MGAKSSSRCC CCSWFIGIIV LIAVILAVVF TLRHRANHSD DAPGSIDKKY SDALKIAMQF
     FDIQKSGKLV NNKISWRGDS GLKDGSEASL DLSKGLYDAG DHMKFGFPMA FTATVLSWSI
     LEYGDQMDSV KLLDHAKESL KWTTDFFINA HPSANVLYIQ VGDPETDHKC WDRPETMSRK
     RTLTKIDTET PGSEVAAEIA AAMAAASLVF KESDAKYSAT LLKHAKQLFD FADNNRGSYS
     VNIPEVQKYY NSTGYGDELL WAASWLYHAT EDKTYLDFVS KNGEEFGNFG SPSWFSWDNK
     LPGTHVLLSR LTFFKKGLSG SKGLQGYKET AEAVMCGLIP SSPTATESRT DGGLIWVSEW
     NALQHPVSSG FLASLYSDYM LTSGIEKLSC SDQDFKPSDL RKFAKSQADY MLGKNPEKMS
     YLVGYGEKYP EFVHHRGASI PGDANVGCKD GFKWLNSEEP NPNVAYGALV GGPFMNETFI
     DARNNSMQNE PSTYNSALVV GLLSSLVTTS SSLESFI
//

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