ID R9PII5_AGAAL Unreviewed; 851 AA.
AC R9PII5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=AALB_1237 {ECO:0000313|EMBL:GAD01157.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD01157.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD01157.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(2013).
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|ARBA:ARBA00000966};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC {ECO:0000256|ARBA:ARBA00009209}.
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:GAD01157.1}.
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DR EMBL; BARX01000006; GAD01157.1; -; Genomic_DNA.
DR RefSeq; WP_016400925.1; NZ_BARX01000006.1.
DR AlphaFoldDB; R9PII5; -.
DR STRING; 1331007.AALB_1237; -.
DR OrthoDB; 9766708at2; -.
DR Proteomes; UP000014461; 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:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.3440; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR018366; CBM2_CS.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002037; Glyco_hydro_8.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR Pfam; PF17963; Big_9; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01270; Glyco_hydro_8; 1.
DR Pfam; PF18911; PKD_4; 1.
DR PRINTS; PR00735; GLHYDRLASE8.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS50093; PKD; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000313|EMBL:GAD01157.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:GAD01157.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAD01157.1};
KW Polysaccharide degradation {ECO:0000313|EMBL:GAD01157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014461};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:GAD01157.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..851
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004478287"
FT DOMAIN 660..746
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 746..851
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 851 AA; 91574 MW; 313758A4AB807FE0 CRC64;
MISNKPVLAL LSLALWSPLS SAELLQKFEL ENGSLLPGYS SAIDSPFNGV AAYANNDGVQ
ATAQISNTPG QFRLDISGAS SANNAAGISV YLDDKKIGAT EFVGTAASLG SFSFKLDSMP
LNSSLSFKLE TDDGSNDTYL DWFELHRVGD IAALPAAPVL PSDGAYNTGV YRNMFAELGY
SKAEVEARVQ AVYDQLFHST DTANKAIFIP VGDDMAYIWD VGNNDVRSEG MSYGLMMAVQ
MNRQDDFNKL WKWAHTYSLN KSGVNKGYFA WKVSTAGDVQ DAYPAPDGEE YFATALFFAS
HRWGDGTGIY NYSAQANQIL DDMYGNGEMR YNNQGQLEEI SLFDHNEKQI VFSPATPSDR
NWTDPSYHLP AFYELWARWA NNNNQFWADI ATTSRAFLKT TVNPANGLSP DYAYFDGTPH
GEFQAWKTTF QYDAWRTVGN AAMDFAWWQK DPWQTQYVNS LQAFFKSEGI DSYSSLYELN
GTPYQNNSDH SPGLVAMNAL ASLAANDQQA WEFVQALWDT PVPSGQWRYY DGTLYMFGML
ALSGNYQIYC PAGECDAVVP PTENRSPVAV NDSVTTAQDT PLVVSVLQND SDPDGDAISI
VSFTQASNGS VSQVGDGLSY SPNSNYSGSD SFSYTISDGQ LEASATVSVT VTDTTVNNPP
SACFTVSIDA ATVGQSIDFD ASCANDVDGD ALSYAWNFGD NNGATGATAS HSYSAAGTYQ
ASLTVSDGKG ASDVYSVSID VSNSDNGPGG AVCSYTVDND WNSGFVASIT ISNQGTTAIN
GWQVSWAYSD GSSVTSSWNS TLTGSQPYVA SSLSWNSTIQ PGQSVTFGLQ GSKGTVNTPA
EVVTLGGSSC N
//
