ID   GUNA_BACPU              Reviewed;         659 AA.
AC   Q5YLG1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-MAY-2023, entry version 67.
DE   RecName: Full=Endoglucanase A;
DE            EC=3.2.1.4;
DE   AltName: Full=Endo-1,4-beta-glucanase A;
GN   Name=eglA;
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=CL16;
RX   PubMed=15538558; DOI=10.1007/s00253-004-1740-1;
RA   Lima A.O.S., Quecine M.C., Fungaro M.H.P., Andreote F.D.,
RA   Maccheroni W. Jr., Araujo W.L., Silva-Filho M.C., Pizzirani-Kleiner A.A.,
RA   Azevedo J.L.;
RT   "Molecular characterization of a beta-1,4-endoglucanase from an endophytic
RT   Bacillus pumilus strain.";
RL   Appl. Microbiol. Biotechnol. 68:57-65(2005).
CC   -!- FUNCTION: Active on carboxymethyl cellulose and carboxymethyl
CC       cellulose-RBB but not avicel, xanthan gum, carboxymethyl-curdulan-RBB
CC       or carboxymethyl-xylan-RBB. {ECO:0000269|PubMed:15538558}.
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:0000269|PubMed:15538558};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by ZnCl(2) and by EDTA.
CC       {ECO:0000269|PubMed:15538558}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5-8. {ECO:0000269|PubMed:15538558};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Retains more than 90%
CC         activity after 24 hours at 50 degrees Celsius.
CC         {ECO:0000269|PubMed:15538558};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15538558}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR   EMBL; AY339624; AAQ91573.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YLG1; -.
DR   SMR; Q5YLG1; -.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted.
FT   CHAIN           1..659
FT                   /note="Endoglucanase A"
FT                   /id="PRO_5000091857"
FT   DOMAIN          501..658
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REGION          1..500
FT                   /note="Catalytic"
FT   REGION          413..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   659 AA;  74985 MW;  13DE360B374DA139 CRC64;
     MLIFETYLIL FKTVQITKRR IERRRLRLLN QCFTKKEGVS NREMASYNYV EVLQKSMLFY
     EAQRSGRLPE SNRLNWRGDS GLKDGKDVGH DLTGGWYDAG DHVKFGLPMA YSAAVLAWTV
     YEYREAYEEA ELLDEILDQI KWATDYFLKA HTGPNEFWAQ VGDGNADHAW WGPAEVMPMN
     RPAFKIDEHC PGTEVAAQTA AALAAGSIIF KETDASYAAK LLTHAKQLYA FADRYRGKYT
     DCVTNAQPFY NSWSGYVDEL IWGGIWLYLA TNEETYLNKA LKAVEEWPQD WDYTFTMSWD
     NTFFASQILL ARITKENRFI ESTERNLDYW TTGLVQNGKV ERITYTPGGL AWLDQWGSLR
     YAANAAFLAF VYADWVSDQE KKNRYQSFAI KQTHYMLGDN PLNRSYVVGF GQNSPKHPHH
     RTAHGSWSNQ LTNPPSHRHT LYGALVGGPN AQDQYDDDIS DYISNEVATD YNAAFTGNIA
     KMVQLFGEGQ SKLPNFPPKE QVEDEFFVEA AVMHNDTTST QVKAVLYNRS GWPARSSQTL
     SFRYYVNLSE VFAKGFTEKD IQVTAAYNEG ASLSPLKVYD ASSRVYFAEI DFTGVVISPR
     GESEHKKEIQ FRLSAPNGSN IWDASNDYSY QGLTSNMQKT TKIPVFEDGV LVFGTLPDK
//