ID A0A1G6UZB4_9ACTN Unreviewed; 1285 AA.
AC A0A1G6UZB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SAMN04489747_0990 {ECO:0000313|EMBL:SDD45976.1};
OS Auraticoccus monumenti.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Auraticoccus.
OX NCBI_TaxID=675864 {ECO:0000313|EMBL:SDD45976.1, ECO:0000313|Proteomes:UP000198546};
RN [1] {ECO:0000313|EMBL:SDD45976.1, ECO:0000313|Proteomes:UP000198546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MON 2.2 {ECO:0000313|EMBL:SDD45976.1,
RC ECO:0000313|Proteomes:UP000198546};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; LT629688; SDD45976.1; -; Genomic_DNA.
DR STRING; 675864.SAMN04489747_0990; -.
DR OrthoDB; 9758662at2; -.
DR Proteomes; UP000198546; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_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; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF02018; CBM_4_9; 3.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000198546};
KW Signal {ECO:0000256|RuleBase:RU361166};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 30..1285
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5009029010"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..149
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 193..289
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 333..440
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 492..559
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 588..1086
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 833..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1012
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 1065
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 1074
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 1285 AA; 134726 MW; A9236AD6F5F8A852 CRC64;
MVSPRHRLHR TAAALVGGLL VTTTLLAPAA ASPLDIPHDF SAGPDGWFSY GPGATTEVTD
GELCTSLPAH SGNPWDVAVA HNAVGLEAGT TYDVAFTASS TAEIAIRAQV GINAEPYPGV
HAEDLTITAT PEEHSFSFSF TSDVDAEAAE TGGQLSFQIG NQGEPFTFCL DDFSLTEAGA
TEEQLPALDV PPFFTTGNLT PSTTVEEGVL CTTVPAGTTN TYDAIVGVNG IPVQEGGSYT
LSFLASADVA SDITVVVGEN GGDYRQAFSQ AVALDSAEPT RYSYEFTSDL AFPASTGDGA
PEGQVAFQLG GGAEAFELCL SEPSLALEVA AGGNLVPNGD FGSGALDPFT APEGVAVDLS
SGAACLTVPD TLGQYDGLVL NGLAVEEGQT YTLTFDASAD PGKTVRALIG ENGGSYGTVL
DEDVALTAET TGHELTFVAS AGYPAATVDP GDGPFEGQLA FQVGGRGAFD FCIDDISLVE
SDTPPPPYEP ETGPRIRVNQ VGYLPDGPKQ ATLVTDATEP LEYEVLADGI VVHTGQTVPA
GLDETAGTDV HELDFSDYRP DVVDADAVHE IAVDGEVSFE FAVRDDLYQQ LRADALNYFY
PARSGIAIDG GIMDGQPDAG EYTRDAGHVE DPDSSLVADS PNRGDVDVRC LSPETEGDYW
KYGDWSCDYT LDVVGGWYDA GDHGKYVVNG GISVGQVLST YERTLYSPTG TGSALGDGSL
NIPESDNGVP DPLDEARWEL EWMLSMQAPD GAQHAGMVHH KIADVDWTGL PLLPSEDPQE
RYLHRPSTAA TLNLAAVAAQ GARLWAPYDQ AFADELLAAA RVAWDAAVAT PDLFEPAPNA
DPSPGSGPYD DDEVGDEFYW AAAELFLTTG EEAFEEHVLG SPFHTADIWS PSGFSWGSTA
ALGRMDLATV ESDLPGRDDV RASVVEGADR YLGWQQAQPF GTAYPGNEGV YEWGSNSAVL
NNQVVIATAF DLTSDQVYAD AVLEAMDYLL GRNALNNSYI TGYGDVFSDD QHSRWFAHSI
DPDLPNPPRG SVAGGPNSDV GTWDPVISGL YDEERMCAPQ RCYLDDIQSW STNEITVNWN
SALSWVASFV ADQQAGDESG AGQVVDVVDH PEDMTVEEGE DAVFTASASG DPVPDVQWQR
LVDGVWTDVD GAEEETFTFE AALEDDGALV RAYFSNGFGG FFTDPATLSV TDAEPRPTPG
PSDEPDDGTP DDGGAPDDGA SPGAGGLPED GGTPSEPGAG GGPTQNLSDT GPSDLVLPAL
LTAVLLLAVG SVVVARGRRQ QDELG
//
