ID G8S5N0_ACTS5 Unreviewed; 591 AA.
AC G8S5N0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN OrderedLocusNames=ACPL_5345 {ECO:0000313|EMBL:AEV86232.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV86232.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003170; AEV86232.1; -; Genomic_DNA.
DR RefSeq; WP_014692303.1; NZ_LT827010.1.
DR AlphaFoldDB; G8S5N0; -.
DR STRING; 134676.ACPL_5345; -.
DR KEGG; ase:ACPL_5345; -.
DR PATRIC; fig|134676.3.peg.5258; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_015488_3_1_11; -.
DR OrthoDB; 309899at2; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR34876; -; 1.
DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361186};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361186};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361186};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 24..591
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5039743980"
FT DOMAIN 31..140
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 140..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 306
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT ACT_SITE 529
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 591 AA; 61433 MW; D0E5683A7B074274 CRC64;
MRPISTRARA LTAAAAVSVV AGAGAVAIAS EASAAAGCRV DYSVNQWSTG FTGNVTVTNL
GDPISGGWNL TWDFPGNQTI TQGWSATIAQ SGQHVTATNP SWATSIGTNG TANFGFNANY
SGTNTAPAAF KLNGLACTGT VPNSPPPSSS GPSTGPSTGP STGPSTGPST NPGTKVDNPY
AGVKGYVNPE WKAKADAEPG GSRVSNNPTA VWLDRIAAIA GTSDSSSNGS MGLRDHLNAA
LAQGAGYIQL VIYDLPGRDC AALASNGELG PDDLPRYKSE YIDPIAAIEA DAKYKNLRII
NIVEIDSLPN LVTNTSGQAG GTAMCDTMKA NGGYVNGIGY ALNKLGAIGN VYNYVDAAHH
GWIGWDSNFG PTADIMLSAA KASGNVNNVT GFITDTANYS ALREPFVQPT TTVNGQSVRQ
SKWVDWNQYT DELTFAQAFR QKLISIGFNS NIGMLIDTSR NGWGGSARPT RASTSTDVNT
YVNESRIDRR IHAGNWCNQA GAGLGERPTA APEPGIDAYV WVKPPGESDG SSSLIPNDEG
KGFDRMCDPT YTGNARNGNS MSGALPNAPI SGAWFSAQFQ QLMANAYPPL S
//
