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Database: UniProt
Entry: A0A1G5AJC2_9FIRM
LinkDB: A0A1G5AJC2_9FIRM
Original site: A0A1G5AJC2_9FIRM 
ID   A0A1G5AJC2_9FIRM        Unreviewed;       808 AA.
AC   A0A1G5AJC2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=SAMN02910370_00084 {ECO:0000313|EMBL:SCX77981.1};
OS   Lachnospiraceae bacterium XPB1003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520825 {ECO:0000313|EMBL:SCX77981.1, ECO:0000313|Proteomes:UP000199543};
RN   [1] {ECO:0000313|EMBL:SCX77981.1, ECO:0000313|Proteomes:UP000199543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XPB1003 {ECO:0000313|EMBL:SCX77981.1,
RC   ECO:0000313|Proteomes:UP000199543};
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; FMVK01000001; SCX77981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5AJC2; -.
DR   STRING; 1520825.SAMN02910370_00084; -.
DR   Proteomes; UP000199543; Unassembled WGS sequence.
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; 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; 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; 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; 1.
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; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000199543};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           24..808
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5039747306"
FT   DOMAIN          88..213
FT                   /note="CBM-cenC"
FT                   /evidence="ECO:0000259|Pfam:PF02018"
FT   DOMAIN          255..330
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          344..803
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   REGION          28..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        738
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        781
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        790
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   808 AA;  87460 MW;  2A016DFCEFF1F801 CRC64;
     MKKKKMRGIA LVTAIALTSA GCAADKNPAT PVNSASEGNA ATQTVSSENG TGFNGPMVGQ
     TAPRGAATTD DNIPVPEEGS APAPKTGDTL INIDFEDGNT GDFMTFTNGG DLELTNTARQ
     LDCSINKCGS VDYGNQAYLD GFELVQGCEY TYSFDICSDI ERTVEYRLQL NGGDYHAYQG
     DYISISPEVL HFSVDFTMEE ASDPAPRLVF NMGKMKDMSA DPGDHHVFID NIRLTVKNAD
     NASLAGAGSL PAYLNVNTNQ VGFRPDDTKT VFVKTENDGE DFFVCRTSDS SIIWQGKLSE
     AADDPASRAK TARGDFSEVS EPGSYYIYTA SGVSYPFTIG EDVYNGLYKD VVSMLYRQRC
     GMALEGASAG AYAHEACHTA PAVIYGTNTT KDVSGGWHDA GDYGRYVVPG AKTVADLFAA
     YEDYSLTSDD MGIPESGNGF PDLLDEAKYE LDWMLKMQDE KTGGVYHKVT CSNFPAMDAA
     PEEETEELII SPISVTATGD FAAVMAKASV IYKDRDPEFA KTAYGAAVKA WDYIADKEDT
     IGFLNPDGVE TGEYPDAVTA DERYWATAEL YLACLASAPG SENDDPAKYS SRLEELARQY
     DEEKATQNSQ AGSDNASPDN RLGWADIISY AWYDLAKSDT EFSSAAKTNL TNEADKMLEA
     SQKDRYFMCL GTDYYWGSNM GIASDAELLY MAANISDDAK AAEYRSLASR ALDYLLGANA
     LGYSFITGYG TFFPKDIHHR PSLAAGNVMP GLLAGGADNR MEDPYAESVL SEAAPSMCYV
     DNSQSYSTNE IAIYWNSPFI YILSAEMK
//
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