ID L1KME0_9ACTN Unreviewed; 747 AA.
AC L1KME0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=STRIP9103_08927 {ECO:0000313|EMBL:EKX61714.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX61714.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX61714.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX61714.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) 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|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10060, 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:EKX61714.1}.
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DR EMBL; AEJC01000571; EKX61714.1; -; Genomic_DNA.
DR RefSeq; WP_009333143.1; NZ_AEJC01000571.1.
DR AlphaFoldDB; L1KME0; -.
DR PATRIC; fig|698759.3.peg.7586; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 30..747
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005138794"
FT DOMAIN 33..154
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 182..265
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 275..738
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 677..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 727
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 747 AA; 80750 MW; D07FE1016E8648AF CRC64;
MKRRRTTLLA VTALLAAALT ALPTGTAQAE EVEQVKNGTF DTTTAPWWTT SNVTAGLTDG
RLCADIPGGT TNRWDAAIGQ NDITLVKGES YRFGFTASGT PQGNVLRAVV GLSVAPYDTY
FEVSPQLNVS GDSYTYTFTS PVDITQGQVA FQLGGNTAPF SFCMDDVSLL GGVPPEVYEP
DTGPRVRVNQ VAYLPAGPKN ATLVTEATGK LPWQLKNSSG AVVAHGQTTP RGVDASSGQN
VHSIDFGSYR KRGTGFTLVA DGETSRPFDI DPSAYERLRL DSLKYYYTQR SGIEISDELR
PGYGRAAGHV DVAPNQGDGN VPCRPGVCDY SLDVTGGWYD AGDHGKYVVN GGISTWEVLS
TYERSLHART GESKKLGDGS LTIPESGNKV PDLLDEVRWE LEFLLKMQVP DGQPLAGMAH
HKIHDEQWTG LPLMPADDPQ KRELHPPSTA ATLNLAATAA QAARLYRPYD RDFAAKTLDA
ARTAWAAALD HPAMYASESD GVGGGTYSDN NVTDEFYWAA AQLYLTTGEK EFADFVLASP
VHTADIFGPI GFDWSRTAAA GRLDLATVPN KLPGRDKVRQ SVIKGADRYL ATLRAHPYGM
PYAPDGNLYD WGSNHQILNN AVVIATAYDI TGASKYREGA LQSMDYLFGR NALNISYVTG
YGDVDARNQH SRWYAHQLDP DLPNPPPGTL AGGPNSSIQD PFAQSRLQGC VGQFCYIDDI
QSWSTNEHTI NWNAALARMA SFVADQI
//
