ID A0A1N7H1W1_9ACTN Unreviewed; 910 AA.
AC A0A1N7H1W1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SAMN05421833_13563 {ECO:0000313|EMBL:SIS18668.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIS18668.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIS18668.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIS18668.1,
RC ECO:0000313|Proteomes:UP000186096};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10059, ECO:0000256|RuleBase:RU361166}.
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DR EMBL; FTNI01000035; SIS18668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7H1W1; -.
DR STRING; 58117.SAMN05421833_13563; -.
DR Proteomes; UP000186096; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 27..910
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5011809697"
FT DOMAIN 510..653
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 686..779
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 802..910
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 645..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 468
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 910 AA; 96344 MW; C24E0E5D627EC84F CRC64;
MRLLSLGGVA AILAALLVPG PAPAQAASSY NYTEALQKSI YFYEAQQSGK KPAWSRVEWR
GDRTLNDGKA AGVDLSGGWY DAGDHVKFGF PMAFTTTMLA WGLVENRTGY GTQLTPMLNN
LKWATDYLIA AHPEPETLYV QVGDGSVDHA YWGPPEVIDI KGMARPVYKI TPTCKGTDVV
AETAAAMAAS SMAFRPADPS YADTLLTHAK QLFTFADTTK GSNGQDTAYT SCVPGISGYY
NSTWEGGSDH PGATKMYWDE LAWAAVWLYQ ATGTGSYLDK AREFYPKMGS EPDVGQGAGG
TAVPAYTFGL GWNDKEYGVY ALMATLTGEQ QYKDDVQRYL DYWTVGYKGK KGPVTPGGLA
YIFNWASLRM ALNTAWVALV YADHLGPDDP LYARYHDFAK RQVDYALGDN PRHSSYMVGF
GTNPPTHVHH RAASGQYLGY MSDTSGPNLH VLYGALAGGP DQTDAYTDSR TDYVRNEVAI
DYNSGITNVL ARFAKEYGGT PAAGFPAPEN KYDEIHAETG NVYTGVDGTS LSVTITNTSN
WPPRVLQSGK ARYYFTLDGS ISVSQVKVTG GDSNGCAVTG PTLAQDRTYY AEVDCTGKPI
YPGDAQLYRR STQLRISVPN GATWDPSNDW SASAASHVPV YDGNTLVWGT PPGGTPSPSP
SPSPSPSPSP SPSPSPSPSA SVDTTPPSAP TGLWVCGADF VNAVPMCWTA STDDTGVTGY
DVYMKQGTSF TKIGSSTSAL YVADKLVAGT SYTFYVVARD AAGNTSQPSA TLTATAQSGL
PTPSPSPSPS RSPSPSPSPS PSPSAGGGCK VTYGTSDWGG GFTATVTLAN TGTTAINGWT
LKFAFPGNQT ITPPGWSATW AQTGANVTAT SLDWNKAINP GQSIQIGFNG AYTGSNPKPT
AFTLNGTTCS
//
