ID A0A0V7ZV20_9CYAN Unreviewed; 639 AA.
AC A0A0V7ZV20;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=BC008_01165 {ECO:0000313|EMBL:KST68508.1}, BC008_12535
GN {ECO:0000313|EMBL:KST63127.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST68508.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST68508.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST68508.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(2015).
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:KST68508.1}.
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DR EMBL; LMTZ01000143; KST63127.1; -; Genomic_DNA.
DR EMBL; LMTZ01000060; KST68508.1; -; Genomic_DNA.
DR RefSeq; WP_058183504.1; NZ_LMTZ01000143.1.
DR AlphaFoldDB; A0A0V7ZV20; -.
DR Proteomes; UP000053372; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 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; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 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 Reference proteome {ECO:0000313|Proteomes:UP000053372}.
FT DOMAIN 511..625
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 376..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 639 AA; 68034 MW; 6ECB8869B16A23A8 CRC64;
MDKLQTQPKY NYGEVLQKSN IFYMAQRSGK LPEDNPIPWR GDSALNDGAD VGRDLTGGYY
DAGDHVKFGF PMAYSMTTLA WGVEQYRKGY EKVGQLDEAL DNIKWGTDFI LKAYDDKGTA
TTKDDVFWGQ VGDGFVDHAY WGAPEKMTMD RPSFKVDAAN PGSDLTGESA AALASASIIF
RGTNDAYADK LLDKAKQLYD FADTYKGKYS DAITNASTFY NSWSGYQDEL AWGAAWLHKA
VEAAGGKDTK YLDKAESYYN GIGTGWTQNW DDKSYGTGVL LAQETGKEKY QGDVEAWLDN
WADPNGGIEK TEGGLPYIAP WGSLRYSSST ALLAGIYGDT VNDKGGKYTG FAEDQINYIL
GDNPRNSSYV VGFGENSPQN PHHRAASGAS DAHNQDVEPT KHVLYGALVG GPKEANDFSY
KDDRGDFIAN EVALDYNAGF QGAVARMTQV FGGEALTEIP GLDLDGTGSS GGGGNPGGGD
GNPGGGDGNP GGGDGNPGGG DGNPGGGGNP GGGGTDPDPI TGDVDFSIRS EWDTGFTGNV
EITNNGSQDI NGWKLEFNAP FEVNDIWGGE ITSHEGNAYV IENVDWDANI GAGESIQFGF
NGSNSDNMNL VLNNVELNDV LLGTENPTNA SGAAMVYMV
//