dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003431_00574

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; HUN007;

CAZyme ID

MGYG000003431_00574

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
625	MGYG000003431_263\|CGC1	70398.11	4.071

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003431	2512610	MAG	Fiji	Oceania

Gene Location

Start: 26; End: 1903 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.4	3.2.1.91	3.2.1.73

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	237	575	3.8e-121	0.9967741935483871

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	2.04e-42	236	570	1	272	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	5.02e-33	232	600	34	395	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
smart00637	CBD_II	9.90e-10	88	168	1	77	CBD_II domain.
pfam00553	CBM_2	1.79e-05	89	180	9	95	Cellulose binding domain. Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
smart01063	CBM49	3.53e-05	89	163	8	78	Carbohydrate binding domain CBM49. This domain is found at the C terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT53501.1	1.19e-234	216	623	97	504
QNL98527.1	2.39e-234	216	623	97	504
ADD61853.1	5.54e-233	216	623	97	504
CUH91791.1	2.38e-230	70	623	28	578
ADU23246.1	3.85e-221	75	621	91	641

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ECE_A	2.22e-63	234	588	12	343	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	3.11e-63	234	588	12	343	ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
3VVG_A	2.24e-56	235	596	20	376	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	3.12e-56	235	596	20	376	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	1.59e-55	235	596	53	409	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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P10474	1.53e-171	219	624	621	1025	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
Q05332	2.43e-149	221	623	38	471	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
P04956	4.48e-134	218	625	33	472	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	4.94e-128	225	617	43	434	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P23548	1.03e-74	227	596	38	382	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000002	1.000047	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
7	24