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Database: UniProt
Entry: A0A3S9PA10_9BACT
LinkDB: A0A3S9PA10_9BACT
Original site: A0A3S9PA10_9BACT 
ID   A0A3S9PA10_9BACT        Unreviewed;       587 AA.
AC   A0A3S9PA10;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=EI427_22100 {ECO:0000313|EMBL:AZQ64922.1};
OS   Flammeovirga pectinis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ64922.1, ECO:0000313|Proteomes:UP000267268};
RN   [1] {ECO:0000313|EMBL:AZQ64922.1, ECO:0000313|Proteomes:UP000267268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L12M1 {ECO:0000313|EMBL:AZQ64922.1,
RC   ECO:0000313|Proteomes:UP000267268};
RA   Bae J.-W., Jeong Y.-S., Kang W.;
RT   "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT   scallop, Patinopecten yessoensis.";
RL   Submitted (DEC-2018) 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:PRU10060, ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; CP034563; AZQ64922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9PA10; -.
DR   KEGG; fll:EI427_22100; -.
DR   OrthoDB; 9808897at2; -.
DR   Proteomes; UP000267268; Chromosome 2.
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; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; 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   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 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: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:UP000267268}.
FT   DOMAIN          23..101
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          118..569
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        548
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        557
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   587 AA;  66029 MW;  25CE99DCDD73E9A6 CRC64;
     MKLSPIVLSI ICLLFLSCSN SKEENRILIN QEGYYRTATK IITVKTDKPA KFLLLSADKS
     KDILKGDVTN ISPWKFSGET YGKIDLSSFK EAGAYVVWIE DIGYSDIINI KDNLGEQSLA
     TSVEAYYLQR CSSPIEKEYA GIYAREGGHP DDKVLIHSSA LNPGQDPKTT ISSPKGWYDA
     GDYNKYIVNS GITTYTLLLV YKNYADILKP IELKIPVNNK NLPLYLDNIK WNLDWMFTMQ
     DPLDGGVYHK LTNASFDGMV MPAKAQKKSR YVVQKSTAAA LNFAAVFFHA SRVFSEFDKT
     LAEDYKLAAI KALDWAEKNP SIIYDQVEMN KKYSPKITTG AYDDKNLSDE FIWAYTEAFL
     TTLDDTYYTK VEWSKGDYNK VPSWSNVEYL AIYSLLTMKY DIPKIAQKDF LLLKKMMTKK
     ADVLASTYKS SAMSTSMGAT NNDFVWGSNA VAANHAMFLL QAYAINFNKE YIDTAIGAFD
     FVMGRNPLDM CFLTGSGKQH PMHIHHRLSD ADKIKEPLPG LLVGGPQNEN NSDNCGYNNE
     FPATTYKDVV CSFTTNEIAI NWNAPFVYMM AGLESHYGNK IDPLAQN
//
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