ID A4BCU5_9GAMM Unreviewed; 933 AA.
AC A4BCU5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 03-MAY-2023, entry version 62.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=MED297_08061 {ECO:0000313|EMBL:EAR10027.1};
OS Reinekea blandensis MED297.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR10027.1, ECO:0000313|Proteomes:UP000005953};
RN [1] {ECO:0000313|EMBL:EAR10027.1, ECO:0000313|Proteomes:UP000005953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED297 {ECO:0000313|EMBL:EAR10027.1,
RC ECO:0000313|Proteomes:UP000005953};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (FEB-2006) 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:EAR10027.1}.
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DR EMBL; AAOE01000006; EAR10027.1; -; Genomic_DNA.
DR RefSeq; WP_008045668.1; NZ_CH724152.1.
DR AlphaFoldDB; A4BCU5; -.
DR STRING; 314283.MED297_08061; -.
DR HOGENOM; CLU_008926_0_1_6; -.
DR Proteomes; UP000005953; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.2810; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-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; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF17963; Big_9; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS00592; GH9_2; 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:UP000005953};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 22..933
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5018381058"
FT DOMAIN 481..638
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 830..933
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ SEQUENCE 933 AA; 101201 MW; C8BE8A7A1371E29A CRC64;
MNYKPTLALA IAIASTSYAY AENYGEALQK SIYFYEAQQS GELPDWNRVE WRGDSALTDG
ADNNVDLTGG WYDAGDHVKF GFPMAATATM LAWGVIENPD AYEQTGQLPH IKNNLRFVAD
YFVKAHTGPN EFYGQVGKGS VDHAWWGSAE VMPMARPSYK IDAANPGTDL AGETAAALAA
IAMVFETTDP AYAQNLLTHA EQLYQFADTY RGKYSDSITD AQAFYNSWSG YQDELVWGAA
WLYQATGNPD YLTKAINEYD NLNTEPQSTI KSYKWGQAWD DKGYGSYVLL AKLTGDAQYE
ADAERWLDYW TTGYNGERIR YTPGGLAFLD TWGAARYTSN TSFLALVYSD YLKNANKKPV
KADTYYDFAR SQIEYLLGDN PMNMSYLIGY GDVYPTAPHH RTAHGAWADS LSVPTDNRHT
LVGALVGGPG LDDSFENDRG DYVKNEVATD YNAGFTGALA RLWKDFGGQP IDDAQFPMPE
PRDNEFFVEA KVNASGPRHI EIATLTHNRS AWPSRNTDQL KFRYWVDLTE EMAAGYEATD
VSVSTAYNQA SSVTGLTHWR DNLYYAEVSF AGVDIYPGGQ SESKKEVQFR LSLPTNTNAA
EWDNTSDPSW DNYSNSFVLA DKIALYDGNT LVWGEEPSPG CGADSGINCA PTANAIQVDT
AFESAVTLTL SGQDSDGTVT DVRLTSQPSN GSVSLSGSSA TYQPDSGFFG TDQFQYVVTD
NDGADSAPAE VTINVDEPMV PAVVITSPAD NSTVAVDSTV TLMLDIRYAA GVNVYVNNQL
TSSRVGDGPV TLDTPSQPTT WVVDVVATDE QGQEIGATDT LTLQIEDVVV PDQDIQCEVP
GADVWNTGFV ISAATVTNAG DEPVDGWTVT LQFDQPITVV NSWGANTSLS SDGLTLTASN
VSYNGTLSSG GSTTFGLQGG HGGNFTIPSC LGQ
//
