ID   GUN4_BACS5              Reviewed;         636 AA.
AC   P28622; O50589;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-MAY-2023, entry version 103.
DE   RecName: Full=Endoglucanase 4;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 4;
DE   AltName: Full=EG-IV;
DE   AltName: Full=Endo-1,4-beta-glucanase 4;
DE   Flags: Precursor;
OS   Bacillus sp. (strain KSM-522).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=120046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9438981; DOI=10.1271/bbb.61.2004;
RA   Hitomi J., Hatada Y., Kawaminami S., Kawai S., Ito S.;
RT   "Amino acid sequence and stereoselective hydrolytic reaction of an
RT   endo-1,4-beta-glucanase from a Bacillus strain.";
RL   Biosci. Biotechnol. Biochem. 61:2004-2009(1997).
RN   [2]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534.
RX   PubMed=2113383; DOI=10.1016/0006-291x(90)90382-w;
RA   Shoseyov O., Foong F., Hamamoto T., Doi R.H.;
RT   "Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes.";
RL   Biochem. Biophys. Res. Commun. 169:667-672(1990).
RN   [3]
RP   SHOWS THAT SEQUENCE DID NOT ORIGINATE FROM C.CELLULOVORANS.
RA   Doi R.H.;
RL   Unpublished observations (JAN-2000).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Clostridium
CC       cellulovorans and was termed endoglucanase C (engC).
CC       {ECO:0000305|PubMed:2113383}.
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DR   EMBL; AB004098; BAA24918.1; -; Genomic_DNA.
DR   PIR; JC5874; JC5874.
DR   AlphaFoldDB; P28622; -.
DR   SMR; P28622; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 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; 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:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..636
FT                   /note="Endoglucanase 4"
FT                   /id="PRO_0000007952"
FT   DOMAIN          478..635
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        447
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   CONFLICT        530..534
FT                   /note="AKGFT -> CEGIH (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   636 AA;  72245 MW;  76718BF57A8EF6A2 CRC64;
     MTRRWSFLVQ CFTFKKKEGV RSRYMSDYNY VEVLQKSILF YEAQRSGKLP ESNRLNWRGD
     SGLEDGKDVG HDLTGGWYDA GDHVKFGLPM AYSAAVLAWT VYEYREAYEE AELLDDMLDQ
     IKWATDYFLK AHTGPNEFWA QVGDGNADHG WWGPAEVMPM NRPAFKIDEH CPGTEVAAQT
     AAALAAGSII FKETDAPYAA KLLTHAKQLY AFADQYRGEY TDCVTNAQPF YNSWSGYIDE
     LIWGGIWLYL ATNDQTYLNK ALKAVEEWPK DWDYTFTMSW DNTFFLSQIL LARITKEKRF
     IESTERNLDY WSTGFVQNGK VERITYTPGG LAWLDQWGSL RYTANAAFLA FVYADWVSDQ
     EKKNRYQTFA IRQTHYMLGD NPQNRSYVVG FGKNPPMHPH HRTAHGSWSN QLTTPSSHRH
     TLYGPLVGGP NRQDQYTDDI SDYVSNEVAT DYNAAFTGNG AAVWSGQSKL PNFPPKEKVE
     DEFFVEAAVM SNDTTSTQIK AILYNRSGWP ARSSQSLSFR YYVNLSEIFA KGFTDKDIQV
     TAVYNEGASL SPLTVYDASS HIYFTEIDFT GVAIFPGGES LHKKEIQFRL SAPNGANIWD
     ASNDYSFQGL TSNMQKTARI PVFDQGDLVF GTLPNK
//