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
//