ID B0C9D4_ACAM1 Unreviewed; 556 AA.
AC B0C9D4;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN OrderedLocusNames=AM1_2816 {ECO:0000313|EMBL:ABW27815.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW27815.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW27815.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW27815.1; -; Genomic_DNA.
DR AlphaFoldDB; B0C9D4; -.
DR STRING; 329726.AM1_2816; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR KEGG; amr:AM1_2816; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_006010_2_1_3; -.
DR Proteomes; UP000000268; Chromosome.
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.
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:UP000000268}.
FT DOMAIN 15..97
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 108..549
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT ACT_SITE 527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 556 AA; 62651 MW; 0F28662ECC8E55AE CRC64;
MAKWVCSQQL AEDFAPKIVL NQVGYRANWD KVAFLLNAED NAPITTNVID RQSGKTVATI
QPGPAELDEQ SRDRIQTLDF SNFKRSGEYY LQAGDLKSVP FQIGQDIYQD TFTKLLRTYY
LQRCGVAIFD PITGIYHPPC HLKDAVIAHD DAFHKAGDTV QSQGGWHDAG DYGKYVATTT
VTIGSLFSLY EQYPQNFTDD QLDIPESGNQ LPDLLDEMKV GLDWLLSTQR QDGGVYRKLS
GKEWPIGKAP DEDKQTRYLY GVSTPETGKF AAVMAMAGRI YKDPQQAKTY LDAAQLAWDY
LQTQDQMQEG WIDGDDSGSG KYLLSEIDIE DSLKTDIDDR YWAAAELFLT TGDSKFEQYL
VDHFDQMPFN LYEWKDASTL GMVDYLFYAK ADPNQLKPQI QQKLLDRADQ IMGRVEGSGY
RLANHRFIWG SNKMTVEEGI TLVHAYHLTQ EQKYKEAALD QLHYMMGRNH FDQTFVTGVG
THPVAKVNHL FARAKQINIP GLVVGGPNDG AQDNIAPKGL GIRSYLDSEK SYATNEYAID
YNAPLITLLG MLLETS
//
