ID A0A1Q5AUZ8_9ACTN Unreviewed; 581 AA.
AC A0A1Q5AUZ8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=A6A27_26960 {ECO:0000313|EMBL:OKI62837.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI62837.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI62837.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI62837.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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:OKI62837.1}.
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DR EMBL; LWLS01000071; OKI62837.1; -; Genomic_DNA.
DR RefSeq; WP_073835961.1; NZ_LWLS01000071.1.
DR AlphaFoldDB; A0A1Q5AUZ8; -.
DR STRING; 1718947.A6A27_26960; -.
DR OrthoDB; 309899at2; -.
DR Proteomes; UP000186700; 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:UP000186700};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 35..581
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5039740517"
FT DOMAIN 34..143
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 128..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..168
FT /note="Pro 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 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 208
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 581 AA; 60842 MW; 15F0A558A7A80737 CRC64;
MNLWRRLSGR SRTLALTGAG VLVAGGLVTL PVTAAQAATQ CSVDYTTNDW PGGFTATVTI
KNLGDPLSAW TLGFTFPTSS QSVVNGWSAR WSQSGQNVTA QNESYNGSLA TGASTTIGFN
GAWSGANPKP TQFTLNGTVC TGGTPPTTPP PSSPPPSSPP PSSPPPGQKA DNPYVGAKGY
VNPDWKAKAD AEPGGSRVSS NPTGVWMDRI AAINGTPGAR GIRAHLDEAL RQGAGYIQFV
IYNLPGRDCA ALASNGELGP NDLPRYKAEY IDPIAAIQAD PKYANLRIIN IIEIDSLPNL
VTNTSGQAGG TAMCDTVKAN GAYVNGVGYA LAKLGAIGNV YNYIDAAHHG WIGWDSNSGP
TADMLKSAAV ASGSTVRNVH GFIVNTANYS ALREPYVKIT DSVNGTSVRQ SKWIDWNQYV
DELSFAQAFR QKLVSVGFDS GIGMLIDTSR NGWGGSARPT GPGATTNVDT YVNGGRIDRR
IHAGNWCNQA GAGLGERPKA APEAGIDAYA WIKPPGESDG SSSAIPNDEG KGFDRMCDPT
YTGNARNGNN PSGALPNAPV SGHWFSAQFQ ELMRNAYPPL S
//
