ID A0A495X382_9PSEU Unreviewed; 887 AA.
AC A0A495X382;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JUN-2023, entry version 11.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=DFJ66_1530 {ECO:0000313|EMBL:RKT68347.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT68347.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT68347.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT68347.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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:PRU10059, 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:RKT68347.1}.
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DR EMBL; RBXR01000001; RKT68347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495X382; -.
DR OrthoDB; 9758662at2; -.
DR Proteomes; UP000272729; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_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 InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00942; CBM_3; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 2.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51172; CBM3; 2.
DR PROSITE; PS50853; FN3; 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|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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 32..887
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5019613848"
FT DOMAIN 492..639
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 650..736
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 737..887
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 887 AA; 95264 MW; 75DF9E9D6F48B0C2 CRC64;
MRRRMSGAAA GTLAVLVGAL TLTPLQPVAT AAPAFNYGEA LQKSIWFYDA QRSGDLPADN
RVNWRGDSAM RDGSDVGLDL TGGFYDAGDH VKFGLPFGAS MTMLAWGAVE NRDAYEGSGQ
LKYLLSNLKW GTDWIVKAHP SPNVVYGQVG AGNPDHAWWG PAEVMRMARP SYKVDASCPG
SDLAGEYAAA LAASSMVFKP TDPTYAATLL THAKQLYTFA DTYRGKYSSC ITDAANFYNS
WSGYQDELVW GAIWLYRATG DTSYLTKAKA EYPKLGTEPQ STTRSYKWTI AWDDKSYGAY
ALMAKLTGEA EYVADANRWL DYWTTGYNGN RIRYSPGGQA VLDTWGSLRY AANTAFVALL
YSDWLRATDA TRAATYHDFG VKQINYALGD NPRNSSYVVG FGANAPRNPH HRTAHGAWAD
SIQEPVTSRH TLYGALVGGP STNDDKYTDS RQDYVANEVA LDYNAGFTGA LARLYKEYGG
TPLANFPVAE TPDGPELTVQ ASVTQSSAQF SEFKAFILNK SAWPARTFNG SLRYYFTLDG
STTPEQITVT TNYNQCGTAS GPVRFSGNVY YVDIPCADVY PGGQSAYRHE VQFRITSAGT
WDPTNDWSYT GLGSGNTVVQ TDRVVLRESG NVVWGKEPGE VPVDREAPTV PSGLTATTIT
GSSATLTWTA STDDVGVAGY DVLRPDGTVA ATASGTTAQV TGLTPDTSYT FSVRAKDTSG
NVSAASTAVT FRTKTGSVTG GLVAQQRGNG GATSNQIGTT LNLVNRGTSA VGLDTVTLRY
WFTGDAANAN YQVFCDWAVV GCGNVRATVV KLATARTGAD AYLQVTFAAG TLNAGAQTGD
IQLRVAKSDW SSFDQTNDYS YRVSSTLTDF DRVTAHTGGA LVWGVEP
//
