ID A0A0K9NPJ9_ZOSMR Unreviewed; 612 AA.
AC A0A0K9NPJ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=ZOSMA_74G00120 {ECO:0000313|EMBL:KMZ58671.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ58671.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ58671.1}.
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DR EMBL; LFYR01001898; KMZ58671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NPJ9; -.
DR STRING; 29655.A0A0K9NPJ9; -.
DR OMA; WDEYMWG; -.
DR OrthoDB; 1347382at2759; -.
DR Proteomes; UP000036987; 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:UP000036987};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..577
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT ACT_SITE 507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 555
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 564
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 612 AA; 68194 MW; FE0F76057976E8A7 CRC64;
MYGRDPWGGP LEICAADSAT DDERSRNLSL ASRQLDETQQ SWLLAGPGEK GRKKKKYVDL
GCVIISKKLF LWGVGVVVTV AVLAGFIDLI VKNVPNKHHH KLPPDDYTVA LHRALMFFNA
QRSGPLPKHN NVTWRGNSGM KDGLSDQSSH KNLVGGFYDG GDAIKFNFPA SFAMTMLSWS
VIEYSAKYEA AGELGHVKEL IKWGTDYLLK TFNNSADSID KLVVQVGDGD IEDRIPNDRY
CWMRPENINY PRPVYECHDC SDLAAGMAAA LSSASIVFRD SKTYSKKLVH GAETLWKFSR
TNRGKYTQLF SDDANFYNST SYWDDYVWGG AWMYYATGNS SYLFIATNPK MAKHAGAFSS
GGSYGVLSWD NKLAGAQVLL SRLRLFLSPG YPYEEMLSAY HNQTNIIMCS YMPFFNSFNR
TKGGLIQLNH GKPKPLQYVV NAAFLASVFS DYLDAADTPG WYCGPNFYST NVLRDFAKTQ
IDYILGKNPR KMSYVVGFSK RYPRHVHHRG ASIPKNGVRY SCKGGWKWRN TKKPNPNTIV
GAMVAGPNKH DGFHDTRSNY NYTEPTLAGN AGLVAALVSL SSKMTGIDKN TIFSAVPPMF
PRAPPPPAPW KP
//
