ID A0A1W2D722_9PSEU Unreviewed; 580 AA.
AC A0A1W2D722;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=SAMN05660733_02789 {ECO:0000313|EMBL:SMC93014.1};
OS Lentzea albidocapillata.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=40571 {ECO:0000313|EMBL:SMC93014.1, ECO:0000313|Proteomes:UP000192840};
RN [1] {ECO:0000313|Proteomes:UP000192840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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DR EMBL; FWYC01000006; SMC93014.1; -; Genomic_DNA.
DR RefSeq; WP_030478548.1; NZ_JOEA01000014.1.
DR AlphaFoldDB; A0A1W2D722; -.
DR STRING; 40571.SAMN05660733_02789; -.
DR eggNOG; COG5297; Bacteria.
DR OrthoDB; 309899at2; -.
DR Proteomes; UP000192840; 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; IPR018366; CBM2_CS.
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; PS00561; CBM2_A; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 35..580
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5010600625"
FT DOMAIN 31..142
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 138..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 295
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT ACT_SITE 519
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 580 AA; 60601 MW; EBF6A650011CA207 CRC64;
MKLNGQRRWA ATGVVVATTA ATIAVALVAP PAGAAPGCRV DYTANNWGGG GFGASVKITN
LGDAISGGWT LKFALPGSQR VAQGWSATWT QSGANVTAAS MSWNGSLGTS ASIDIGFNGS
GAASGDVNPT TFTLNGTVCT GAPPTSTTTT TTTTTTTSNN PDPGNRVDNP YVGAKQYVNP
DWAAKANAEP GGSRIANQPT AVWMDRIAAI NGTPGARGLA SHLDEAVRQA AGSPLTIQVV
IYNLPGRDCA ALASNGELKP TEIDRYKTEY IDPIAAILAR PAYASLRIVT VVEIDSLPNL
ITNVTPRPTQ TPQCDVMKAN GNYVTGVGYA LAKLGAVPNT YNYIDIGHHG WLGWDDNFGP
SAELLFQAAN ASGSTKANVH GFVANTANYG ILTEPNFSID ESINGTPVRQ SKWVDWNRYT
GELPYAQAFR QRAVQAGFDA NVGMLIDTSR NGWGGTARPS GPGPRTSVDA YVDGGRLDRR
IHLGNWCNQA GAGIGERPKA APAAGVDAYV WIKPPGESDG ASEEIPNNEG KGFDRMCDPT
YTGNARNGNS MSGSLGNAPL AGHWFPAQLQ ELMRNAYPAL
//
