ID A0A1Q4YSE5_9PSEU Unreviewed; 966 AA.
AC A0A1Q4YSE5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=A6A25_18130 {ECO:0000313|EMBL:OKI37498.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI37498.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI37498.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI37498.1,
RC ECO:0000313|Proteomes:UP000186828};
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 -!- 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}.
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:OKI37498.1}.
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DR EMBL; LWLC01000003; OKI37498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4YSE5; -.
DR STRING; 1835005.A6A25_18130; -.
DR Proteomes; UP000186828; 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; 2.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR008965; CBM2/CBM3_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; PF00942; CBM_3; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 2.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51172; CBM3; 2.
DR PROSITE; PS50853; FN3; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000186828}.
FT DOMAIN 478..625
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 636..722
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 729..815
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 816..966
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT ACT_SITE 396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 966 AA; 103271 MW; 1728A37EC4DD0E42 CRC64;
MLVSALTLTP FQPSATAAPA FNYGEALQKS IWFYDAQRSG DLPADNRVNW RGDSALRDGS
DVGLDLTGGF YDAGDHVKFG LPFAATMSML AWGAVENRAA YESSGQLRHL MANLKWGTDW
IIKAHPSPNV VYGQVGKGDD DHKWWGAAEV MQMARPAYKV DASCPGSDLA GEYAAAMASA
SMVFKQTDPT YAATLLTHAK QLYTFADTYR GKYSACITDS ANFYNSWSGY QDELVWGAIW
LYRATGDASY LAKAKAEYPK LSTEPQTTTR SYRWTIAWDD KSYGAYALMA KLTGEAEYVA
DANRWLDYWT TGYNGNRVRY SPGGQAHLDT WGSLRYAANT AFVALVYSDW LRERDAARAT
TYHDFGVRQI NYALGDNPRS SSYVVGFGAN PPKNPHHRTA HGAWADTMQE PVTSRHVLYG
ALVGGPGTNN DSYKDDRTDF VANEVALDYN AGFTGALARL YQEYGGTPLA NFPVAEATDG
PELTVQASVN QSAAGFTEIK SFVLNKTAWP ARMFNGSLRY YFTLDGATTP DQITVTTNYN
QCGTPSGPEQ HSGSVYYVDV PCPGVYPGGQ SAHKHEVQFR ITSAGTWDPS NDWSYTGLGT
GNAVALTDRL VLVQDGVVQW GKEPGPAVED REAPTVPIGL RASGVAATSA TLSWTASTDN
VGVTGYEVLR ADGTVVGAPV TPTFQLTGLT PGEHSFSVRA RDAAGNRSAA STPISITIVA
GDDDEPPTAP NRPVVGSITS TGATLTWPAS SDNVAVAGYE ILRPDATVAA TTTATTYTFT
GLTADTSYTF TVRAKDTSGN LSPPSTGVTF RTTPGGVTGT LAVQQRGNGS ASANQIGATL
ALVNRGTAAV DRSTVTLRYW FTGDTANANY QVFCDWAVVG CANVRATVVK LPDARPGADS
YLQVSFAAGT LAAGAGTGDI QLRVAKSDWS AFNQADDHSY RVSSTLADFD RVTAYTGGTL
AWGTEP
//
