ID A0A1M6UXC0_9ACTN Unreviewed; 590 AA.
AC A0A1M6UXC0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=SAMN05421803_13044 {ECO:0000313|EMBL:SHK73937.1};
OS Nocardiopsis flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=758803 {ECO:0000313|EMBL:SHK73937.1, ECO:0000313|Proteomes:UP000184452};
RN [1] {ECO:0000313|EMBL:SHK73937.1, ECO:0000313|Proteomes:UP000184452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHK73937.1,
RC ECO:0000313|Proteomes:UP000184452};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQZK01000030; SHK73937.1; -; Genomic_DNA.
DR RefSeq; WP_073383959.1; NZ_FQZK01000030.1.
DR AlphaFoldDB; A0A1M6UXC0; -.
DR STRING; 758803.SAMN05421803_13044; -.
DR OrthoDB; 309899at2; -.
DR Proteomes; UP000184452; Unassembled WGS sequence.
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 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.
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:UP000184452};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 33..590
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5039751662"
FT DOMAIN 38..146
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 145..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT ACT_SITE 528
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 495
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 590 AA; 61767 MW; 62418D5E54094318 CRC64;
MSRIHSAATP GPSRARRGPA ALSALVVGAA LAVVPAAPAS ADSGCAVEYT VNDWGSGFTA
NVEITNLGAA VNGWTLDWSF PGNQQVTNLW GGTHTQSGAN VSVSDAGYNS SISTDGAVSF
GFNGSYSGSN AAPLAFELNG VLCDGAVDPG EPGEPGEPGE PGEPGEPGTS RVDNPYSGAD
VYVNPVWSAN AAAEPGGEAV ANEPTGVWLD RIGAIEGNDS PTTGSMGLRD HLDEAVEQSG
GEPLVFQVVI YNLPGRDCAA LASNGELGPD EIDRYRDEYI DPIADILADY EDTELRIVTT
IEIDSLPNLV TNVSPRATAT PECDEMLANG NYVEGVGYAL ATLGDIDNVY NYVDAGHHGW
IGWEDNFVPS AQIFYQAANA AGATPADVHG FIANTANYSA LEEENFSIGQ TIAGVPVRQS
SWVDWNNYVD ELSFSQALRT ELVSQGFPSD IGMLIDTSRN GWGGADRPTG PGPQTDVDAY
VDGGRYDRRV NPGNWCNQAG AGLGERPQTA PAAGIDAYVW MKPPGESDGS SELIDNDEGK
GFDRMCDPTY EGNVRNGNSP SGALGDAPIS GHWFSAQFQE LLDNAYPPLD
//