ID A9Q742_PAEPO Unreviewed; 573 AA.
AC A9Q742;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Cel5B {ECO:0000313|EMBL:ABV08876.1};
DE EC=3.2.1.4 {ECO:0000313|EMBL:ABV08876.1};
OS Paenibacillus polymyxa (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1406 {ECO:0000313|EMBL:ABV08876.1};
RN [1] {ECO:0000313|EMBL:ABV08876.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GS01 {ECO:0000313|EMBL:ABV08876.1};
RX PubMed=18759236; DOI=10.1002/jobm.200700281;
RA Cho K.M., Hong S.J., Math R.K., Islam S.M., Kim J.O., Lee Y.H., Kim H.,
RA Yun H.D.;
RT "Cloning of two cellulase genes from endophytic Paenibacillus polymyxa GS01
RT and comparison with cel 44C-man 26A.";
RL J. Basic Microbiol. 48:464-472(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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DR EMBL; EF621409; ABV08876.1; -; Genomic_DNA.
DR CAZy; CBM46; Carbohydrate-Binding Module Family 46.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR005102; Carbo-bd_X2.
DR InterPro; IPR040946; CBM46.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR016282; Glyco_hydro_5_endoGlcnase_B.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR31297:SF17; ENDOGLUCANASE; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF18448; CBM46; 1.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR PIRSF; PIRSF001043; Endoglucanase_B; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:ABV08876.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..573
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002742385"
FT DOMAIN 69..350
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT DOMAIN 384..464
FT /note="Carbohydrate binding X2"
FT /evidence="ECO:0000259|Pfam:PF03442"
FT DOMAIN 468..571
FT /note="Endoglucanase B carbohydrate binding"
FT /evidence="ECO:0000259|Pfam:PF18448"
SQ SEQUENCE 573 AA; 63729 MW; AFE73C4A24C5058A CRC64;
MLKRRPISLL SLTLAITLLL STFASVAAAA ETDGQAQPAA ATSNMQSYVE AMQPGWNLGN
SLDAVGADET AWGNPRITQA LIQQIAAQGY KSIRIPVTWD KHIGAAPHYT VESAYMNRVE
EVVRWALDAN LYVMINVHHD SWTWVSSMEP KHDEVLARYN ALWTQIADRF KNQPNKLMFE
SINEPRFSEG GTTDEAKMNQ MLHELNVSFH KIVRASGGKN ATRPLVLPGL DTSPAQAKIN
ELYNTITKLN DPNLIATVHY YXFWPFSVNI AGNTTFDKAA QNDIVQTFDN VYNTFVAKGI
PVIVGEYGLL RFDKHTGVIE QGEKLKFFEF LTYYMKEKKV TGMLWDNGQH LNRSTYKWSD
PELFNVIKAS LKGRSSNAAS DLIHLKKGSS VQDTKITLNL NGNQLKSLNA NSKQLKQGTD
YTLSGDTLTF KASLLTSLIT SGKYGENAVI NTKFNKGADW NFRVVVYDTP KLSVVEGTTQ
AFTIPTDFRG SQLATMEAVY TNGGNAGPQD WTPYKEFGNT FAPAYDTNGI KLLPEFFNSV
KDGEVTLKFH FWSGDVVTYK ITKNGTRVTG TTS
//
