ID A0A2A4KCZ5_9ACTN Unreviewed; 944 AA.
AC A0A2A4KCZ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CIB93_33675 {ECO:0000313|EMBL:PCG81774.1};
OS Streptomyces sp. WZ.A104.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2023771 {ECO:0000313|EMBL:PCG81774.1, ECO:0000313|Proteomes:UP000217525};
RN [1] {ECO:0000313|EMBL:PCG81774.1, ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|EMBL:PCG81774.1,
RC ECO:0000313|Proteomes:UP000217525};
RA Xu L., He S., Yan X.;
RT "Isolation and Genomic Analysis of a Bioactive Actinomycete Associated with
RT Cyanobacterium Lyngbya cf. aestuarii.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|Proteomes:UP000217525};
RA Jiao Y., Han B.;
RL Submitted (SEP-2017) 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}.
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:PCG81774.1}.
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DR EMBL; NWVL01000100; PCG81774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4KCZ5; -.
DR OrthoDB; 5480482at2; -.
DR Proteomes; UP000217525; 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 InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR040720; GH81_C.
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; PF17652; Glyco_hydro81C; 1.
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, ECO:0000313|EMBL:PCG81774.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000217525}.
FT DOMAIN 381..690
FT /note="Glycosyl hydrolase family 81 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17652"
FT REGION 53..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 99745 MW; ED834CEAC675A716 CRC64;
MIEVLLVRTS LSGLASRGAP RTTTRPAAAA LLAVAVAAVG LGPAASPAAA ATIPAGSGSY
TDSRPAGTSG PTTNTGAPVT PKVTAAAKDK PVPTNDWWSS LAFQRYGDNP YSTPMYGHPL
TYQATSGGLE VGYPTTPAIV GDGRQYEYAH KADLTVGLSG LNSPDTKADD WSDWTVTPYW
ADGSRTFRAT IGHGMPFVYA KGSGGDARVT TASAPTVFSD QGNVLGITVA GHHYALFAPT
GSDWNISGST ITAGLGGKDY FSLAVLPSTD ALATYRKYAF SFVTGSRVAW QSTGGDVRAT
YTLTTEAEEG TERGTLQALY RHQWLHTTDA LTPYTYVSPR GTMKVRESAS FTTSQRSSGV
VPALPATSGV DKARLTGYLN EVANASDPFS GATDTYWTGK ALGRLAQLVP VADQIGETAT
RDKLLGLMKG RLQEWFTAGG ASEFSYDKDW KTLTGYPASY GSDTELNDHH FHYSYYVYAA
AIVAQYDQAW AADSAWGTMI KHLIRDTANP SRTDSAYPFL RGFDVYAGHS WASGHQGFAA
GNNQESSSES INLSAGLVLW GAATGDTALR DLGSYLLTTE SEAITQYWFD ASQEVFPASF
GHDTVGMVWG SGGAYATWWT ANPEEIHGIN VLPVTGGSLH LAREKAAIKR NIAEMERNNG
GPAQEWRDLL WEFEALSDPA AAKAKWDAAN GNYAPEAGES KAHTYHWINT LNTVGAPDMT
VSGDLPTSAV FSKDGTRTYT AHNHSSSART VSFSDGKTLS VPARSTATST GPGGGDPDPG
EPGPSTGNTF RLKTGGILTT ATTDPAGTDT LASADGVNRD GTPYRATAYE IKNVDGELAA
GAATSFRLRV DAGTTVGLAP QVRVSYDLTG DGTFDRVETF RYFATDPVAG WEEYTQAVGT
QAVTGSLGDL RGGTVRLEIW NALGNDTSQV QTGTEAAVLR IPYE
//
