ID L8K1J5_9BACT Unreviewed; 1585 AA.
AC L8K1J5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=C900_01404 {ECO:0000313|EMBL:ELR73794.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR73794.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR73794.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR73794.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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:ELR73794.1}.
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DR EMBL; AMZN01000002; ELR73794.1; -; Genomic_DNA.
DR RefSeq; WP_009577604.1; NZ_AMZN01000002.1.
DR STRING; 1237149.C900_01404; -.
DR PATRIC; fig|1237149.3.peg.167; -.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG2730; Bacteria.
DR eggNOG; COG3469; Bacteria.
DR eggNOG; COG5498; Bacteria.
DR OrthoDB; 976933at2; -.
DR Proteomes; UP000011135; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:UniProtKB-EC.
DR GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04080; CBM6_cellulase-like; 2.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
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; PF17957; Big_7; 1.
DR Pfam; PF03422; CBM_6; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00606; CBD_IV; 2.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51175; CBM6; 2.
DR PROSITE; PS50853; FN3; 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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000011135}.
FT DOMAIN 913..1034
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1049..1134
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1257..1376
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 1115..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1585 AA; 171236 MW; A3361EBCC69ABBA4 CRC64;
MKPIITIGWN SFGNLVRTLA GLLRQTFAKT TPLKTYLTSL FITVLSFQLS AQIVPVGSGS
YTTAFPGTDE AGRNEFPSGT PKVSGVAATK PVPTNDWWSN LVKNDHGGQA FNYPLSFRSE
TEGLVVNYTI PLSSSANEYR EPMSAVDAIK VGVSGLSASQ STISDFSDWT VTANWASGSN
NFSATMGMGM PFVYFTKGSG NTARVEVNFN APGVSVSGNK LLIQNNMNNS NYVVFGPAGS
TWSGSGGAFT SSLAGKNYWS MALVPPGMDI NAFIANYEKY AYVFPAETSV DWSYNENTST
VTTTFTVTPD VKEGSYNEAL LGLLPHQWAH LGAGSPQPSL ATYPSVRGEL KMLGGNSFTV
ENKFSGVLPT LPDLAKYSNG FDITSLYNKV DGIKGEGLPG WTDSYNEGQN MNRLIQAARI
ADQIGHIEAR DKLLDTVQER LEDWLTAEGG EVAFLFYYND TWNALLGYPA GHRQDVNLND
HHFHWGYFIH AASALEQFRP GWANNWGEMI NMLVRDAGNP SKTDSMFPFL RNFSPYSGHA
WANGFATEPF GNDQESTSES MQFNASLIHW GTITNNTGIR DLGIYLYTTE ITAIQEYWFD
IHDRTFQPEY AHEMIARIWN AGYDNGTWWT SDIAASYGIQ LYPIHGGALY MGYDLDYVQE
VWNGMTSKTQ VLNNVANPNL WYDTYWSFLA FVDPEQAISL YDSYPNREVK VGISDAQTYH
WLHTMNALGH VANEITADYP IAAVFDKNGE KTYVAHNYGN SAITVHFSDG ASLYVPAGEM
ATSKDTGASI SISAPGVIAE PCTSGVNNNF TLEANVTGSG VSYVEFFRNG VSIATDNSAP
YELPQSFSAD GVYTYIAKAY VGSGFEISNI YRVIVGLGSQ EPYSSAHVVP GTFESGWYDK
GGNGISYYDV DPNVYEANFR PEDEVDAATS TSQGTSIGWI AAGEWVEYSL NATSGKYDIA
LNIASNQAQG GTSGSVSLDL DCNTVGLVNS TPLTGSWDNY EAVTISDVNV PSGSHILRIT
FNSGVYNLGR ITFTRTGDYN GGGNTPPTTP TGLQVTNTTT SSLSISWNAS TDAENNLSGY
NVYLNNTLAD NTTGTSYTFT GLSPNTSYDM QVEAVDSQNA TSPQASVAGT TNQSSDDDDD
DDDNGDNCSA TVNADFSVDI TGDATNPSMT FVPERSGVAS TTCILYYSTS PDGAYPGYLV
SANTPYQINA SAGQTIYYYY TYNVPEGGEN NTFNNKQNFV VGECGNGDTN TGVPIPALIQ
AEDYTEMSGI QVEETSDTDG GQNVGWIDTG DWMEYEISVP ASGTYYVNYR VASETAGGAI
TIAQNGTALE TTSFSATGGW QEWTTVNTTV ALSAGDQTIR LTATAGGWNF NWFEFTTDAS
DTTSNGNGCN VTVNADFSVV VSNDASNPSL TFIPVRSGVG APTCILYYGT SPTGSYPGYL
VSANAPYQIN ASAGQTIYYY YTYSLPEGGE NNTLNNKKSF VVGNCSGGSG ARTGTLETEA
LRKGGPQFEH LVLFPNPAND RLTIAGLPED VTEIAVYDAT GRDQLISRPA SVKEVSLDIR
HLTEGLHFIR IQTKTDIVTR SFIKR
//
