ID G2NIH2_STREK Unreviewed; 909 AA.
AC G2NIH2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SACTE_3717 {ECO:0000313|EMBL:AEN11565.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN11565.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN11565.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN11565.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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}.
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DR EMBL; CP002993; AEN11565.1; -; Genomic_DNA.
DR AlphaFoldDB; G2NIH2; -.
DR STRING; 862751.SACTE_3717; -.
DR KEGG; ssx:SACTE_3717; -.
DR PATRIC; fig|862751.12.peg.3861; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_006010_0_0_11; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
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; 2.60.40.290; -; 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; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_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 PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 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; PS51173; CBM2; 1.
DR PROSITE; PS00698; GH9_3; 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:UP000001397};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 800..909
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 767
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 909 AA; 96338 MW; 24C17A7C4ACAF058 CRC64;
MWCHPYLRLR TSGRKVSSVN ALPPPARPAP VRPRSRYGRR VLGMSAAALL CAGALAVPGT
AMADDAEPGP GPEQITNGDF ATGTSAPWWW TPNASAAVSE GRLCVEVPAG TANAWDVIVG
QNDVPIVAGE SYELSYTARS TVPLTVQTRV QEAVEPYTTV LATADPVGAE DTRVARTFTA
SVDQPAASVQ LQIGGGERAT TFCLDDVSLR GGAEPPVYVP DTGSPVRVNQ VGYLPRGPKS
GTVVTDAEAP LTWTVKAEDG STAATGTTVP RGEDPSSRRR VHTFDFGDLT TAGDGYTVEV
DGEVSEPFSI RGDLYDSLRS DALAYFYHNR SGIEIDADLV GEQYARPAGH IGVAPNKGDT
DVPCRPGVCD YRLDVSGGWY DAGDHGKYVV NGGISVAQLM ATYERTLTAP DAESAELGDG
ALRVPERDNG VPDILDEARW EMDFLIKMQV PAGEQLAGMV HHKMHDAEWT GLPMKPHLDP
QQRELHPPST AATLNLAATA AQCARLYAPF DADFADRCLR AAETAWDAAK RHPDVLADPN
DGIGGGAYND DDVSDEFYWA AAELFTTTGK DIYRQAVLSS AWHGDAGAVF PAGGGISWGS
TAGLGVLTLA TVPNALTSDQ LAQVRTVVTE GADRYAAQSR EQAYGLPYAP RGEDYVWGSN
SQVLNNMVVL ATAHDLTGDA AYQDAVLRGA DYLLGRNPLN QSYVTGYGER DSHNQHHRFW
AHQNDPSLPN PAPGSIAGGP NLTAIASGDP VAAEKLSGCA PAMCYVDDIG SWATNEITIN
WNAPLAFIAS YLDDAGEGGQ TAAARTCQVT YSSHPWNSGS TVTVRVENTG SDPVSPWALT
WLLPGEQRLS HTWSAEFDQH GRTVSARPLS WNRTLAPGAA VDFGFNTSAA GSSPEPGAFK
LNGRACSAG
//
