ID A0A0M8YFK4_9PSEU Unreviewed; 801 AA.
AC A0A0M8YFK4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=ADK67_16165 {ECO:0000313|EMBL:KOX25911.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX25911.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX25911.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX25911.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX25911.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGED01000169; KOX25911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8YFK4; -.
DR STRING; 1415542.ADK67_16165; -.
DR PATRIC; fig|1415542.3.peg.3524; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
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 CDD; cd00063; FN3; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; 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; 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; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 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 Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 34..801
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005732454"
FT DOMAIN 610..702
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 699..801
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 571
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 580
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 801 AA; 83136 MW; E0072BBFEFBFCB30 CRC64;
MSVRTHHQLR RGVAVAAALA LAAVALTPPA ALAAPDAGPA VKVNQVAYVP GLPKQATVVN
GSGSPVAWTL RNAAGATVAS GQTTVRGADS LSGDNVHVAD FSSFDAPGTG YVLSVAGTNS
APFDISADPL KRLRYDALAF FYHQRSGTPI LAEHVGSQYA RPAGHLNASP NRGDNGVPCR
VSCGYTSDVR GGWYDAGDHG KYGVNTGIAA WQLINEYERT LHVNGADRAA LGDGKLAIPE
RGNGVPDILD EARWGVEFLL KMQVPQGRAD AGMVRHKVSD ENWTALPMRP DQDPEPRLLS
AVTTAATLNL AAVAAQAARV WKDIDAGFAS RALTAAQLAY TAAKANPTRY ADANDGNGGG
TYVDNNVTDE FFWAAAELFT TTGAGNYRAD VTGSSFFRGR GFDQGGFDWW WTAGLGDTTL
ALVPNGLSAS DVSATRAAFA SYGDRLLNQA ATQGYPAPAS GYYWGSNGVV ANAANVLALA
HDFTGQAKYR TGVYQALDYL FGRNPFNHSY VTGYGERATR NSHHRFWANQ LNPSLPIPPA
GLLAGGPNVD LQDPVAQQQL AGCKPQKCYL DDINAWSVNE VALNWNSALA WLSAWAAEKA
GPGSPADTTA PSTPSGLTAS ASGGAVTLSW AASTDDVGVT GYDVLRATGT SGSFTQVATA
SGTSHTDSGL GAGTYRYQVR ARDAAGNTSP VSSAVPVTVP GGGAGCTVAA TVQSQWGTGY
VVQPVRVTNT GTSTITWVVT FTLPSGHSIP GSWNATVITN GQTVTARAIR PLEPGATAEF
GFQASRPNGN SAMPSGYTCA G
//
