GUNA_BACPU
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 25-MAY-2022, entry version 64.
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; Firmicutes; 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; -; 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 Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49384; SSF49384; 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