dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002530_02370

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Basic Information help

Species

Ruminiclostridium_E siraeum

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminiclostridium_E; Ruminiclostridium_E siraeum

CAZyme ID

MGYG000002530_02370

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1080		119761.64	4.5312

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002530	2864211	Isolate	not provided	not provided

Gene Location

Start: 2652362; End: 2655604 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.151	3.2.1.78

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	73	399	2.3e-88	0.9896193771626297
CBM23	633	790	1.9e-45	0.9876543209876543

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3934	COG3934	3.12e-38	50	431	4	315	Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism].
pfam03425	CBM_11	1.95e-12	633	790	7	173	Carbohydrate binding domain (family 11).
pfam03442	CBM_X2	4.91e-12	454	528	7	83	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.
pfam03442	CBM_X2	1.45e-09	545	617	6	78	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.
pfam03442	CBM_X2	8.67e-09	805	879	5	81	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK97477.1	0.0	1	1080	1	1080
CBL33682.1	0.0	1	1080	1	1173
CCO04515.1	5.36e-317	1	885	1	889
QEH70547.1	1.15e-168	22	632	19	633
ADZ85047.1	1.15e-168	22	632	19	633

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PZ9_A	8.25e-79	51	430	21	378	Nativestructure of endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZG_A I222 crystal form of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZI_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with beta-D-glucose [Thermotoga petrophila RKU-1],3PZM_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with three glycerol molecules [Thermotoga petrophila RKU-1],3PZN_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with citrate and glycerol [Thermotoga petrophila RKU-1],3PZO_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with three maltose molecules [Thermotoga petrophila RKU-1],3PZQ_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with maltose and glycerol [Thermotoga petrophila RKU-1]
6TN6_A	7.18e-76	51	430	7	364	X-raystructure of the endo-beta-1,4-mannanase from Thermotoga petrophila [Thermotoga petrophila RKU-1]
4QP0_A	1.63e-74	40	401	2	327	CrystalStructure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei]
3WH9_A	1.35e-59	42	367	2	281	Theligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger],3WH9_B The ligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger]
1QNO_A	6.25e-59	40	364	2	278	ChainA, ENDO-1,4-B-D-MANNANASE [Trichoderma reesei],1QNP_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei],1QNQ_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei],1QNR_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei],1QNS_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8NVK8	8.50e-71	8	443	8	386	Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=manA PE=3 SV=2
Q2U2I3	6.52e-69	42	372	119	405	Probable mannan endo-1,4-beta-mannosidase F OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=manF PE=3 SV=2
Q2TXJ2	2.58e-68	8	442	8	385	Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=manA PE=3 SV=1
B8NIV9	4.33e-68	42	372	119	405	Probable mannan endo-1,4-beta-mannosidase F OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=manF PE=3 SV=1
A1C8U0	2.17e-65	9	424	57	423	Mannan endo-1,4-beta-mannosidase F OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=manF PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.140292	0.834924	0.004422	0.018830	0.000899	0.000608

TMHMM Annotations download full data without filtering help

start	end
13	35