CAZyme Information: MGYG000003035_00062

Basic Information

• Species: CAG-485 sp900542185
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900542185
• CAZyme ID: MGYG000003035_00062
• CAZy Family: GH26
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
460	MGYG000003035_1|CGC1	51980.87	4.3515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003035	3548444	MAG	Netherlands	Europe

• Gene Location: Start: 89570; End: 90952 Strand: -

Full Sequence      

MIRTKTINRICTCMAICLVNISATSCSDARADRASGLTVTAEGTPIDYVRFGSRASARIF
GVETDIPWHIGVTDSDTAWIKVSPHSGNGWNFSADDAINRESFFRVEVSSNDADEERSTV
LTVEAGGLTRDLTVTQSAAGTEYDVAESPVMADATPQTVNVYDFLRDNYGKKVISGVVSY
GTLDIRNAEYLHDKTGKYPVINYFDFMHHVHSAPLNPTDWAENYTDMSVPQKWWNDGGIV
LFDWHWSVPKNESVKDSFDDCAFYSENNSFSPSRALLEGTWEHDILIRDLDVISGYLLDL
QSKNVPVLWRPLHEAAGRWFWWGKEGPDTYKDLWKFMFEYFTQKGLRNLIWVWTGEEPEW
YPGDTYVDVLGVDIGVKDHQSVPEKMDLLRSVTSHKICAITECGSIPSIEDMQANGDIWS
WITPWVGGSDPDSGDNTLEFYISQYNSEMIITRDEVPDLK

Enzyme Prediction     

EC	3.2.1.78

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH26	151	455	7.4e-89	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02156	Glyco_hydro_26	8.06e-46	150	455	1	311	Glycosyl hydrolase family 26.
COG4124	ManB2	4.54e-13	302	373	177	254	Beta-mannanase [Carbohydrate transport and metabolism].
cd14948	BACON	6.54e-11	47	137	7	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam13004	BACON	1.33e-04	72	137	4	61	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
pfam19190	BACON_2	1.53e-04	51	139	11	91	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CEA16910.1	5.79e-81	141	460	243	558
QGY44077.1	1.54e-79	144	460	131	461
SCD21902.1	2.56e-79	141	460	288	603
QIK58757.1	6.87e-76	49	460	52	456
ARK08557.1	3.78e-75	114	460	100	456

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HF2_A	2.00e-75	154	425	50	314	Thestructure of BoMan26B, a GH26 beta-mannanase from Bacteroides ovatus [Bacteroides ovatus ATCC 8483],6HF4_A The structure of BoMan26B, a GH26 beta-mannanase from Bacteroides ovatus, complexed with G1M4 [Bacteroides ovatus ATCC 8483]
6D2X_A	1.56e-64	152	456	7	334	Crystalstructure of the GH26 domain from PbGH26-GH5A endo-beta-mannanase/endo-beta-glucanase from Prevotella bryantii [Prevotella bryantii B14]
6D2W_A	1.13e-60	152	456	98	425	Crystalstructure of Prevotella bryantii endo-beta-mannanase/endo-beta-glucanase PbGH26A-GH5A [Prevotella bryantii B14],6D2W_B Crystal structure of Prevotella bryantii endo-beta-mannanase/endo-beta-glucanase PbGH26A-GH5A [Prevotella bryantii B14]
3WDQ_A	3.25e-56	142	457	27	353	Crystalstructure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus [Symbiotic protist of Reticulitermes speratus],3WDR_A Crystal structure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus complexed with gluco-manno-oligosaccharide [Symbiotic protist of Reticulitermes speratus]
6HPF_A	1.62e-54	148	456	5	310	Structureof Inactive E165Q mutant of fungal non-CBM carrying GH26 endo-b-mannanase from Yunnania penicillata in complex with alpha-62-61-di-galactosyl-mannotriose [Yunnania penicillata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49425	4.10e-56	152	458	149	459	Mannan endo-1,4-beta-mannosidase OS=Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OX=518766 GN=manA PE=1 SV=3
G2Q4H7	1.47e-46	128	456	153	476	Mannan endo-1,4-beta-mannosidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=Man26A PE=1 SV=1
Q5AWB7	1.02e-45	175	456	50	350	Probable mannan endo-1,4-beta-mannosidase E OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=manE PE=3 SV=1
P55296	7.00e-45	154	457	162	461	Mannan endo-1,4-beta-mannosidase A OS=Piromyces sp. OX=45796 GN=MANA PE=2 SV=1
P55298	8.16e-45	154	457	161	460	Mannan endo-1,4-beta-mannosidase C OS=Piromyces sp. OX=45796 GN=MANC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000390	0.090068	0.909267	0.000117	0.000087	0.000070

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003035_00062.