ID K4KM49_SIMAS Unreviewed; 565 AA.
AC K4KM49;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 2.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN OrderedLocusNames=M5M_14917 {ECO:0000313|EMBL:AFV00107.2};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00107.2, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFV00107.2, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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DR EMBL; CP003746; AFV00107.2; -; Genomic_DNA.
DR AlphaFoldDB; K4KM49; -.
DR STRING; 1117647.M5M_14917; -.
DR KEGG; saga:M5M_14917; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_026903_0_0_6; -.
DR OrthoDB; 1153097at2; -.
DR Proteomes; UP000000466; Chromosome.
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; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..565
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003878420"
FT DOMAIN 14..122
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 115..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 61823 MW; 1BC4892C71A11E0B CRC64;
MKRKILGMAM AGLFATFAEA AQVSMSASGD WGSAFQGDTK ITNDEAGAVN GWTITFGASF
TIDQIWNARI ISKTGNTYVI GNLDYNGAIN PGESVNFGFI GSPGNAMMPV DIVFNGGAAP
TPTPTPTPTP TPTPTPTPTP TPTPTPTPTP GNGLPGDDWL SVSGNTIVNK SGQPVWLTGA
NWFGFNTTER VFHGLWSVNL DATVKAMADR GINLVRVPFS TELVKEWMAG QFKAININTH
ANPELTGMNS LQVFDAFLAA CKKYGVKVLL DAHSAEADNS GHVQPLWTKG NITEADFINT
WVWLAERYKN DDTIVAFDLE NEPHGKAHSD TVFAKWDGST DANNWKHVSE KTAKAVLAAN
PEILIMIEGI EVYPIDGLSW DSKNEKSYHF NWWGGNLRGV ADHPVLVPGH QNKIMYSPHD
YGPLVFAQDW FYPGFSKETL INDVWQDNWL YIHTQGISPL LMGEWGGFLD GGDNEKWMLA
LRELMNDYKI HHTFWCLNPN SGDTGGLLTG DWTNWDEAKY KVLEPVLWQN AAGAYIGLDH
EVPLGANGIT VKQHYLNGGA RPIGL
//
