ID A0A420F1S3_9ACTN Unreviewed; 868 AA.
AC A0A420F1S3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=D7I43_13365 {ECO:0000313|EMBL:RKF26932.1};
OS Micromonospora globbae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1894969 {ECO:0000313|EMBL:RKF26932.1, ECO:0000313|Proteomes:UP000285744};
RN [1] {ECO:0000313|EMBL:RKF26932.1, ECO:0000313|Proteomes:UP000285744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WPS1-2 {ECO:0000313|EMBL:RKF26932.1,
RC ECO:0000313|Proteomes:UP000285744};
RX PubMed=29458491; DOI=.1099/ijsem.0.002625;
RA Kuncharoen N., Pittayakhajonwut P., Tanasupawat S.;
RT "Micromonospora globbae sp. nov., an endophytic actinomycete isolated from
RT roots of Globba winitii C. H. Wright.";
RL Int. J. Syst. Evol. Microbiol. 68:1073-1077(2018).
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:PRU10060, 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:RKF26932.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RAQQ01000008; RKF26932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420F1S3; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000285744; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-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; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000285744};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 30..868
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5018810045"
FT DOMAIN 757..868
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 725
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 868 AA; 90396 MW; 73FD9662687ABFCE CRC64;
MTPPRRRRAL LAAAAALALA TVGAAPAHAE PPPDAPEQID NGDFSAGVAP WFSYGTGPLG
VTDGRLCATV PGGLANPWDA GIGQDGVPLV AGAEYTLGFD VSATPGTPVT AVLQLGAPPY
TGYASVTVTA GGTAQRVERT FTATDGNPSA QLIFQVGGSA DEQTVCLDNV SLRGGEPPEP
YEPDTGPRVR VNQVGYLPGG PKNATVVTEA TEPLPWRLRS ADGDVLAEGT TTPRGVDPAS
GQNVQTADFS AYRTPGTGLR LEIDGEASHP FDISGGLYER LRADSLQFFY AQRSGIAIDG
ALLGEAYARP AGHLGVAPNQ GDTDVPCQPG VCDYRLDVRG GWYDAGDHGK YVVNGGIATY
QLLSAFERTK TAATAGGGAA LGDGTLRVPE HGNGVPDILD EARWELEFLL RMQVPAGQPL
AGMAHHKIHD RNWTGLPLAP HDDPQPRELH PPSTAATLNL AAVAAQCARL YAPYDAAFAG
RCRTAATTAY AAAKAHPDRY ASPADSTGGG AYDDTRVTDE FYWAAVELWL TTGAPAYLAD
LTASPHHTQD VFEPRGFGWQ GVAALGRLDL ATVPNALPAA ELARVRASVT DAADGYLAEL
RRQAYGLPMP GDAGSYFWGG NSNVLNNTVV LATAFDLTGD ARYRDGAVQA VDYLFGRNAL
NISYVTGWGE HAARNQHSRI FAHQLDPSLP HPPAGSLAGG PNAALQDPFA AQLLAGCAPM
FCYVDDINSY STNEVAINWN SALAWVASFL ADQGAADPVA APTCAATYTL HGSWPGGFTS
QVTIRNTGTA PVDGWTARFA FTGDQAVDRA WLARVSQSGA TVTARNEPHN ARINPGATVT
FGFTATTGGG ANPPPGLVTL NGVPCTSA
//
