CAZyme Information: MGYG000000289_02100

Basic Information

• Species: Prevotella buccae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella buccae
• CAZyme ID: MGYG000000289_02100
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1338		151285.23	8.1188

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000289	3001000	MAG	Sweden	Europe

• Gene Location: Start: 15005; End: 19021 Strand: +

Full Sequence      

MKRLRLLFMLCAALTGIASFAANVAVNHLTTENMTNPLGLGTTVPRFSWQLSSEKRQVVQ
TAYHIMVASTPRLLERGEADLWNSGEVKSDAQLWIDYRGRALQSGDEAYWRVRVTTNRGK
TEWSAVQRFTIGLLGENRWNGRWIGLEELQPGERKGMYTRLAARYLRKEFKLKGRVKRAM
AYVAGLGVHEFFVNGIRMGGHHVLQPVPSDYRKTVYYNTYDVTEPLNASHTACLAIMLGN
GRLFPMRQEKPYKTPFFGYPKCRINVRIDYEDGSHAVWATDPSWKLTVDGPIRANNEYDG
EEYDARKEMPGWNRVGFDDSRWQEARRCAVPDGTLRPQPTEGMVETPYPHRPRIVSPLGN
HKNTSLPPTTHHPTPLILDFGQNMAGWIGVKVRGNRGDTIRVRYAEKLNADGTLYRDNLR
NARSEDIYVCNGREGGRLWKPAFSYHGFRYVEVSGPVNATPDDFTAFTVSDEMATTGHFE
CSDTTLNAVVRNAWWGIYGNYKGMPVDCPQRNERQPWLGDRTVGCLGESFLFNNERLYSK
WMGDLAEGVRSDGALSNVTPAFWNYYEDNVTWPAVFPFACDMLYQQYGNIRPITECYPYI
KKWFTHILDEYRHEDIITKDKYGDWCVPPEKPELIHSQDPARKTDGALISTAYGIRVFQL
LEKFARLQGMECEADCWKEQRSRMTAAFNRKFLTLKRGTSPRPGHVLYPDSVFYGNNTAT
ANLLPLAFGIVPDSLKDEVVKNVVTNIITTGDGHVTCGVIGISWLLRGLSDNGFADVAYL
LATNNTYPSWGYMAKNGATTIWELWNGDKADPAMNSGNHVMLLGDLLTWCYQYLAGIRQA
PGSTAYKHIVLQPSFDIEDCFHVDASYMTPYGRVVSKWKKTLERVEWQVEVPVNTTATVY
LPNGKTEEIGSGSYTFESDITPKNPAIVEDEFLYESAGFPQAHASTITQLKNGDLVAAYF
GGTWERNPNVCIWVSRKPKGSDRWEAPVLAGDGVYELGTPDAELAGIDEKTTPASAGPIK
QRRGEQLKDYRQQIAHWHYTYPQTKEEAAATKPKNMPFNARLKRKACWNPVLFTMPDGEL
WLFYKVGATVADWTGWLVKSRDGGRTWSDREPLPKGFIGPVKNKPELVDGRLVCGSSTEN
DGWRFHVEILDLKTGRWKYVGPVEAESRARTDDVEPGCDMIAPVYKQGEGPRPIYSIQPS
ILRLKDGRLQVLMRTHNAKLATSFSADGGDTWSPVTLTEVPNNQSGTDAVTLRDGRHVLI
YNDFETLPGTKKGPRTPISIALSDDGTHWHHALTLEDSPINQYSYPAIIEGRDGKLHCVY
TWRRQRIAYKKIDLNKLK

Enzyme Prediction     

No EC number prediction in MGYG000000289_02100.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	374	901	5.9e-152	0.9861111111111112
CBM67	143	331	2e-33	0.9545454545454546
GH33	936	1321	1.5e-28	0.9093567251461988

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	1.36e-119	476	834	3	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	2.70e-80	953	1318	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	2.13e-53	174	347	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.
pfam05592	Bac_rhamnosid	4.17e-34	366	466	3	98	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.
cd15482	Sialidase_non-viral	4.57e-34	932	1333	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS84864.1	0.0	21	1338	3	1271
QNT66960.1	0.0	19	1338	22	1328
QDH55645.1	0.0	19	1336	17	1285
QRQ56894.1	0.0	19	1336	17	1285
ALJ45265.1	0.0	19	1336	17	1285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6I60_A	1.62e-150	29	916	35	939	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	7.13e-103	26	916	6	1009	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	6.18e-94	25	916	3	863	Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
4X6K_A	1.83e-06	1198	1332	322	471	Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C]
4X47_A	1.84e-06	1198	1332	325	474	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
T2KNB2	1.63e-123	28	931	37	905	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
T2KPL4	2.46e-117	36	918	42	923	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
P9WF03	4.01e-115	32	924	38	916	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
Q82PP4	3.09e-102	26	916	6	1009	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	8.51e-10	448	806	700	1047	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
0.000695	0.998462	0.000217	0.000225	0.000191	0.000175

TMHMM  Annotations     

start	end
7	29