ID A0A1I6RHS4_9BACL Unreviewed; 1977 AA.
AC A0A1I6RHS4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
GN ORFNames=SAMN05428962_1834 {ECO:0000313|EMBL:SFS64204.1};
OS Paenibacillus sp. BC26.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1881032 {ECO:0000313|EMBL:SFS64204.1, ECO:0000313|Proteomes:UP000199637};
RN [1] {ECO:0000313|EMBL:SFS64204.1, ECO:0000313|Proteomes:UP000199637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC26 {ECO:0000313|EMBL:SFS64204.1,
RC ECO:0000313|Proteomes:UP000199637};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00000382};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family.
CC {ECO:0000256|ARBA:ARBA00010730}.
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DR EMBL; FPAD01000001; SFS64204.1; -; Genomic_DNA.
DR STRING; 1881032.SAMN05428962_1834; -.
DR OrthoDB; 5480482at2; -.
DR Proteomes; UP000199637; Unassembled WGS sequence.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProt.
DR GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 6.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR011432; Shr-like_HID.
DR PANTHER; PTHR31983; ENDO-1,3(4)-BETA-GLUCANASE 1; 1.
DR PANTHER; PTHR31983:SF0; ENDO-1,3(4)-BETA-GLUCANASE 2; 1.
DR Pfam; PF00754; F5_F8_type_C; 6.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF07550; Shr-like_HID; 4.
DR SMART; SM00231; FA58C; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 6.
DR PROSITE; PS50022; FA58C_3; 6.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1977
FT /note="glucan endo-1,3-beta-D-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038332044"
FT DOMAIN 35..172
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 175..315
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1158..1300
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1383..1521
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1623..1760
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1834..1977
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 193..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1977 AA; 216507 MW; 3ED4E068E7ED96FF CRC64;
MSSFARKVRR KMPLTSKSVL TLSLLLGSWN GSIVAAADAK GAEASHLLTY GGAAYASSTE
GGLTPEKAVD GSTDSRWGSA FSADPQWIYV DLGAHATIDK AVIRWENAYS KSYKIQVSDD
ETDWKDIYTD AKGDGGVDTI SLSGQGRYVR MLSLERSGGY GVSLYEFEVY GTGGRNPIPI
VLGEDVAKNK PVAASSYEKA DKDKPAMPPE NANDGDVTTR WSSAHTSNEW IYVDLGSVHD
IGRIRLNWEN AAGRIYDLQV SDDAANWTTI YREMNGQDGW IDTPVYASGR YVRMKGISRT
TSYGYSLFNF SVYDYVNGDP KPEYTIPTLP TSSTVGVGKG SYLTSDINMP QPRPPMNKSD
ELHAPIPSND WWQSVLIKNF SDSLITLPLK SKYSTLGLGI LNPGAGWVND TGNSQAADGG
PDFYLHAGNI STTNVKNKIT GYGDWSATVA LSDNDTAKMK TTFVKGSPYL YSEFSDPTTS
ELYFPASTRF YDDNGNPVLA AEGAKLTADH IGFAVTNVDG SPQANKVTRN YGVFAPEGSV
FMKVGNKVKI RLGSGQNYLS VASMPAASDL NYFYKHGYAF VTNTVVTPSF DETTSEVATT
FTVEIDRKRS DMEPTTLMAL LPHQWKQTSS SLTPLTYPSI RGTLKLHEGN SFTTKDQFNG
IVPQFTEPGD ASYSREALLD QLSYLDESTS KNIMSGDAYW QGKVLHPLAM GVLIADQIGD
QAYKEAFLSR MRTILTDWYT YTKGEPDYFM YYDPTWGTMY YKNSEFGANT GLTDHHFTYG
YFVFASAVLA TYDQDFKDNY GGMVEHLIRD YGNPSKEDPL YPFLRNFDPY EGHSWAGGYG
DNNNGNNQEA AGESLFGWVG EYMWSLLSGD KATRDIAIYG FTTELKAVEQ YWFNYDNDNW
LPEFAHKSVG QVYGSAYNFG TFFSGDPVNI YGIHWLPTGE YLTSYGFDPA KAADLYNGMV
KDNEGPEDAW QHIVWPIEAL SNPQAVLDKF TVENTQKNEI FNTYWFVHNM ATLGTRTEDI
WASGWSGASV YKKGSTYSAE VWNPTNEAIT VTFHNAAGVT GSAIIGPKSL VKVDPTKVTD
LDANIAPMLS TDKTDNTIKQ PIELTFADHL NWRESIHSVE VNGAALDPSQ YIVQAGKITL
NSSLFPVEGS YSIVVKAADY SDTGVQQVVI TNSTVNLALN KPTFTSDKPN NPGSYAVDGK
LDTRWESAFS DPQFVAVNLK SEYRISHIRL NWENAAGKSY KVLVSTDGQH WTPVYSTTRG
HEGIDDITFP AVNARYVKVE GTERTTNYGY SLWELEVFGS PAGILDAPDL LADTTMNRAG
QPIEIGFEDV AEWRTAIQNV KVNGTPVSAS QYEVAPGKLT LDGSLFPAAG NYNITVESNG
FATTAIQQPI VTNSNINLAL RKPTFTSSAP NQSSSYAVDG NKATRWESKF TDPQSITVDL
GAEDSISRVL LNWENAAGKS YTVEVSTDNK EWKTVYSTTT GKPGIHDIGF SPIAARYVKV
NGTERTTNYG YSLWELEVYG NGTGLPSAPQ LTADTTNTVI GQPIEVTFDD DAAWRNAIEA
VKIDGATINV SNYQVNAGNI TFNASLFKTA KSYVISVQAK DYTEATVQQT VAAQDQPGHQ
DPNPTPDPGT NPNPLNLAFG KETASSPEYP RSASDAVDGR LDRRWESAFA DNQWMSINLG
SVATINRVVL NWENAFGKAY TIEVSLDGES WTTVYATDKG NGGIDDISFA PVQAKYVKMN
GIKRGSPYGF SLWEFEVYAG DKAPLAGPAL TADTTDNTLG KPIDISFTDD SAWRNAINAI
ELNGAPLQAD QYTVTAGKIT LSAELFTESD PYVVTVQAQG YESDSVVQPI AAGINLALNK
NTVTSEGALQ SGQRAVDGNK STRWESAFSD PQWIRVDLGT TNTISRVLLN WENASAKAYT
IEVSQDGESW STVYATAKGD GGIDNIFIAP VEARYVKIQG SARNTQYGYS LFELEVY
//
