CAZyme Information: MGYG000002001_00595

Basic Information

• Species: CAG-177 sp000431775
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-177; CAG-177 sp000431775
• CAZyme ID: MGYG000002001_00595
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761	MGYG000002001_2|CGC5	85705.41	4.5092

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002001	2259768	MAG	Spain	Europe

• Gene Location: Start: 222173; End: 224458 Strand: +

Full Sequence      

MLSKKFVCAGYDYSTYTDFVPAPYFRKSFYVECLPTDCRVTVCGLGFYDIFINGTKITKG
LLAPYISNPDDIIYYDEYDLSEYLAEGENVLGFQLGNGMQNSPGGQIWDFDIAAFRGAPR
LAFALELDGETIEADDSVKTAASPIVFDDLRCGCFYDARNESDGWAEPGFDDSAWKSALR
AETPRGEARICEAEPILPRETLKPVSVRRCTLAHYEARGDVVKDSKPFCSKEKEGWLYDF
GVNTAGIETLRIKGERGQQIDLQFAEYINPDGELDYGNLGFYPDGFVQRDVYILKGEGEE
VFEPQFTYHGARYCLVLGLTDEQATEELLTFDICASAIGDRGDFRCSDDTVNKLQVMTRN
SDLSNFYYFPTDCPHREKNGWTGDAAVSCEQLSLNFAPEKSYKEWLRNIRKTQKETGELP
GIIPTGGWGYEWGNGPAWDQVATVLPYMTYLLRGDREILEENSPTIMRYAEYISRNRTAR
GTVELGLGDWCPVTKFKSPLEFTDSVVCMDILDKAAYIFSVLGQPLQEKFCVKLRREIRS
AVREHLIDLSTCTSIGCCQTSQAMAIYYNVFDPGEKAQAFKVLLKIISDSDDHMDCGILG
ARCLFRVLADHGKAELAYELITRPDYPSYGNFVTRGLTALPEDFLREGQRPNSLNHHFFG
DISAWFIEYIAGIRVNPAGNDCREVRVTPNFIARLDFAEGHYDTVGGRVAVRWERDGSDI
ALTVECADGVHGEIRLPNGCRFKQSQLSFAELESGRYEIVY

Enzyme Prediction     

No EC number prediction in MGYG000002001_00595.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	232	736	3e-124	0.9900793650793651
CBM67	22	182	1.3e-25	0.8693181818181818

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	1.99e-71	342	670	4	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.
pfam08531	Bac_rhamnosid_N	1.37e-35	35	196	3	168	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	4.27e-24	236	328	8	96	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.
pfam17390	Bac_rhamnosid_C	3.61e-06	683	737	10	64	Bacterial alpha-L-rhamnosidase C-terminal 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
APO32478.1	2.99e-182	215	577	2	364
QGQ94103.1	2.76e-149	20	737	141	841
QMW03094.1	1.15e-136	1	753	136	875
AVM44981.1	1.40e-135	21	739	49	744
ASU33388.1	2.61e-135	21	739	160	865

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6I60_A	3.76e-101	22	737	176	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	8.95e-74	39	755	320	1015	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	1.86e-54	25	719	134	822	Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
2OKX_A	1.06e-07	48	208	50	209	Crystalstructure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1],2OKX_B Crystal structure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
T2KPL4	5.42e-86	22	761	184	949	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
Q82PP4	4.33e-73	39	755	320	1015	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
T2KNB2	6.97e-67	24	737	176	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	5.19e-65	24	724	172	868	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000001	0.000039	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002001_00595.