CAZyme Information: MGYG000004698_00691

Basic Information

• Species: Prevotella sp000436695
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436695
• CAZyme ID: MGYG000004698_00691
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1281		144137.16	8.1953

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004698	3424026	MAG	Denmark	Europe

• Gene Location: Start: 26483; End: 30328 Strand: +

Full Sequence      

MIRKAFITALAVALCMPVMAARKQNAKKSQFPVAVTELKTERMVNPMSIDTSTPRLGWII
TSDENDLMQTACHIIVASTPEKAEKLEGDLWDATLLGDRSQWVRYEGKELRSNTPCYWRV
KVTTNKGESDWSNTAMWNVGLLNEADWSGQWIGLEKAMPWDVEDVHSRLSSRYLRTEFSL
DKPVKRATLYISGLGMYEAYINGKKVGDQVLAPAPTDYRKTVLYNAFDVTQMLTEKNAIG
VTLGNGRFYTMQQKKKPYKITNFGYPKLRLNLVIEFTDGKKKVISSNNKWKLNPDGAIRS
NNEYDGEIYDARKELGAWTSVGYDDSKWMAAERVGIPTGTLRGAMSPNMKVVKTMKPVSI
TKHGEGYIIDMGQNMAGWIKLRISGVNAGDSVKIQYAEKLNEDGSLFTKNLRNAFTTDYY
VAAGNEDGRWWAPTFVYHGFRYAEITGLDNVTADGIVGEVVSDEMEMTGTFECADTILNK
VYHNAMWGILGNYKGMPVDCPQRDERQPWLGDRVRGCFGEAFIFNNNALYAKWARDITEA
QREDGCIPDVAPAYWNYYSDNITWPSALPFSLEMMYNQYGDAEPMSRYYGNVKRWLEHMK
YQYGKDGLMPRDKYGDWCVPPEDIKLIHSRDPKRVTDGTLIATAYYYKLNKMMERFAKIL
EKPNDASEFGAEAARVKEAFNKKFLTINRNTAKVPGLMLYPDSTFYGNNTVTANLLPLAF
GMIDDNYVRGEVEKNIIHNIITLNKGAISCGVIGVQWLMHGLTDMGRGDMAWLLATNKKY
PSWGYMAEHGATTIWELWNGDTANPWMNSGNHVMLLGDLVSWIYEDVAGINSDENKPGFK
HIVMKPAFNVDEIDDINASYKSIYGTIVSRWHKKAGKLIWHVEIPANTTAELHMPDGSIR
NIGSGKYDLTADMPMTDKAVVSDEFLYKSASFPECHSATIAETSKGDLVATYFGGTKERN
PDVCIWVSRKPKGSDEWLAPQLVADGVFKTGSEEAKLAGLSGLDSTNAPAAKGPILDKKI
RKNPEGYQRKACWNPVIYQIPGGDLVIYFKIGNKVADWTGWMVRSKDGGKTWSKREPLQE
GYLGPIKNKPIINKGRIIAPTSIEEGGWRLYFEYSDDMGKTWKRTDFVKADEGVKAIQPS
IMVLNDGRLAAVARTRSEHIGITYSSDNGLTWSKLQLIDTPNNNSGLDAVTLKDGSHVLI
CNDRPIPKGIKNGKGARTPLSVMKSDNGTDWKHWITLEESPVSQYSYPSIIQTSDGKIHC
IYTWRRQRIKHVVIDPNRTAE

Enzyme Prediction     

No EC number prediction in MGYG000004698_00691.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	363	893	2.8e-152	0.9861111111111112
GH33	924	1262	3.7e-35	0.9210526315789473
CBM67	159	338	6.8e-35	0.9147727272727273

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	3.58e-120	466	827	1	340	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam13088	BNR_2	4.61e-88	946	1260	1	280	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam08531	Bac_rhamnosid_N	6.57e-66	182	353	1	172	Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd15482	Sialidase_non-viral	1.07e-46	925	1275	4	339	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam05592	Bac_rhamnosid	1.17e-31	367	462	8	102	Bacterial alpha-L-rhamnosidase concanavalin-like domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIU95828.1	0.0	33	1276	24	1285
QDH55645.1	0.0	33	1278	22	1285
QNL37629.1	0.0	33	1278	24	1287
QUT29077.1	0.0	33	1278	22	1285
QUR43127.1	0.0	33	1278	22	1285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6I60_A	1.36e-166	37	895	34	899	Structureof alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
3W5M_A	2.34e-110	157	895	289	995	CrystalStructure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6GSZ_A	4.12e-104	33	908	2	862	Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
4X6K_A	7.29e-13	1062	1269	237	466	Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C]
4X47_A	7.37e-13	1062	1269	240	469	Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en [[Ruminococcus] gnavus ATCC 29149],4X49_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with oseltamivir carboxylate [[Ruminococcus] gnavus ATCC 29149],4X4A_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac [[Ruminococcus] gnavus ATCC 29149]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
T2KPL4	2.40e-129	45	902	42	914	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1
T2KNB2	1.66e-121	40	895	41	879	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22090 PE=1 SV=2
P9WF03	1.03e-110	36	895	32	879	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
Q82PP4	9.97e-110	157	895	289	995	Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 PE=1 SV=1
T2KM26	7.76e-20	440	896	700	1138	Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 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
0.008608	0.735109	0.254326	0.001159	0.000410	0.000332

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004698_00691.