CAZyme Information: MGYG000003769_01513

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium
• CAZyme ID: MGYG000003769_01513
• CAZy Family: GH5
• CAZyme Description: Endoglucanase E1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
468	MGYG000003769_12|CGC3	53476.17	4.8154

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003769	4856301	MAG	Canada	North America

• Gene Location: Start: 42756; End: 44162 Strand: -

Full Sequence      

MKKIKRMISTLMILIIFFSSGYFKSEQKVIAADTNNDDWLHCVGNKIYDMYGNEVWLTGA
NWFGFNCSENVFHGAWYDVKETLTNIANRGIGFLRVPISTELLYSWMIGKPNKVSSVTAV
NNPPYYVCNPDFYDTVNNKVKNSMEIFDIIMGYCKELGIKVMVDVHSPDANNSGHNYPLW
YGLTTTTAGEITTEKWIDTLAWLADKYKNDDTILAFDIKNEPHGKRGYSPSTPSDMAMWD
NTTDENNWKYAAERCARAILSKNPKVLIMIEGVEQYPKTELGYSYDTPDIWGASGDASPW
NGAWWGGNLRGVKDYPVDIGTLNSQIVYSPHDYGPSVYSQSWFDKDFTTQTLLDDYWYDT
WAYINDQGIAPLFIGEWGGFMDGAKNQKWMTLLRDYMVNNRIHHTFWCINPNSGDTGGLL
SYDWRTWDEEKYALLKPALWQANGKFIGLDHKIPLGENGISLGEYYGN

Enzyme Prediction     

No EC number prediction in MGYG000003769_01513.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	49	418	8.6e-117	0.9967741935483871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	7.78e-43	48	413	1	272	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.58e-34	44	446	34	398	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX41541.1	0.0	1	467	1	467
BAI52933.1	5.26e-306	5	468	3	467
BCJ94038.1	1.64e-303	2	468	5	472
ACL75118.1	5.84e-303	5	468	3	467
AAG45162.1	5.84e-303	5	468	3	467

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ECE_A	3.23e-69	39	437	5	349	AcidothermusCellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus],1ECE_B Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus]
1VRX_A	2.50e-68	39	437	5	349	ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
3VVG_A	2.10e-53	55	436	28	373	TheCrystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
3W6M_A	2.10e-53	55	436	28	373	Contributionof disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
2ZUM_A	3.59e-53	13	436	10	406	FunctionalAnalysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q05332	6.68e-297	1	467	1	473	Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1
P10474	1.36e-161	33	468	623	1029	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
P04956	1.10e-137	36	464	38	469	Endoglucanase B OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celB PE=3 SV=1
P50400	1.33e-134	31	463	37	438	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P23548	3.76e-72	21	435	19	378	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001032	0.979702	0.018436	0.000335	0.000247	0.000207

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003769_01513.