ID A0A085EQK0_9BURK Unreviewed; 587 AA.
AC A0A085EQK0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN Name=celD {ECO:0000313|EMBL:KFC61495.1};
GN ORFNames=FG94_05136 {ECO:0000313|EMBL:KFC61495.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC61495.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC61495.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC61495.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) 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}.
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:KFC61495.1}.
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DR EMBL; JNNN01000083; KFC61495.1; -; Genomic_DNA.
DR RefSeq; WP_051997113.1; NZ_JNNN01000083.1.
DR AlphaFoldDB; A0A085EQK0; -.
DR STRING; 1502852.FG94_05136; -.
DR PATRIC; fig|1502852.3.peg.5050; -.
DR eggNOG; COG3291; Bacteria.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000028601; 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; 2.60.40.10; 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; 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; 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; 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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 35..587
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005105947"
FT DOMAIN 38..114
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 128..578
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT ACT_SITE 511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 557
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 566
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 587 AA; 62705 MW; 638594E5461CABC6 CRC64;
MHHPAPQTGT PLSLPPLRLA AACAALLLAG GAHAAGPASV KLNQVGYLPA AQKLAVVPAD
AQARFAVVEA GSGKQVFEGS LASAATWDAS GERVRLADFT ALRTPGSYRL RVAGLPDSAP
FAIQPGVYRE LDIAAIRNFT LNRTGIALTP AIAGPYARPL AHPDTRVLVH ASAASKARPA
GTVISSPKGW YDAGDYNKYI VNSGISTYTL LAAYEHFPEW FAKLPLNLPE AGNGLPDILN
ETLWNLDWML TMQDPNDGGV YHKLTNKVFD GIVMPEKATA PRYVVQKTTT ATLDFAAVMA
VASRVLKPFD SQQPGRSARY LAAAEQAWRW AEANPKVLYE QPADIQTGAY GDKSAEDELA
WAAAELLIAT GNSDYRSRAF AHAGDAAKGT EPGWADVGML GWISLAQHAG RLPAGADAAP
VRKQLLEVGD RLVERWRASP YRVTMGAKDF VWGSSSTILN QAMMLVAAYR VEPRPDYLNA
AQSALDYVLG RNGPGMSFVT GFGERSPMHP HHRPSEADGV KAPVPGMLVG GPNPGQQDAK
DCPVPYPSKL PALSYIDHVC SYASNEIAIN WNAPLVYVAA AMESLQR
//
