CAZyme Information: MGYG000002624_00754

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; Borkfalkia
• CAZyme ID: MGYG000002624_00754
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
660	MGYG000002624_7|CGC2	75020.55	7.497

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002624	1428680	MAG	China	Asia

• Gene Location: Start: 56103; End: 58085 Strand: -

Full Sequence      

MRAEFICHPEFAELRPADVFRRGQAPLSAAEEDIRDRHILFRRKVFLPAAKRAFLRITAD
DYFKLYINGEYVAQGPPPSYPQHYYYMEIDVSSRLRAGENVFAVHTYYQGLINRVWVSGD
LRACFWCELFADGKQVLVSDGLWRCSLHSGYSARGKIGYDTAFAVSYDSSAPEVGFEKPG
FDDSAWSRAAVRKYADYRLARSPVPPLSVYTVPPAVLSRRGGVLFADFGAERAGQLRVEA
KGRKGDRLYIRCGEELNPDGSVRFDMRCNCRYEEEWVLSGGTDVFDPYDYKGFRYAEIAV
PEGAHVARVEMTVRHYPFEKRAVYETRSERLRQILKLCEDTVHYGTQEVFIDCPTREKGQ
YLGDLCISGRAQCVLTQDARLLKKSILDFCRSSSVSRGVMAVAPASFMQEIADYSLLFPA
LVLWAYKQDGDIGFLRQAWPCLRAEHEYFLRFCNAEGLLENVNEQWNMVDWPENLRDGYD
FPLTIPVGGGVHNVINALWVGFLQAQDEIRRILGKPETGRTARAKEAFVSAFYSKEKGLF
CDTPRKTHSAVHSNIFPLLFGIGTENEQIRQNLVGFICERGLSRMGVYMAYFALAALVKC
GERERAERLAVDPRAWPRMLAEGATTAFEAWGKEEKWNTSLFHPWACAPLIVFAKGAIPY

Enzyme Prediction     

No EC number prediction in MGYG000002624_00754.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	219	655	4.7e-79	0.8611111111111112
CBM67	34	192	3.9e-35	0.8863636363636364

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	1.11e-16	324	645	6	328	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	7.44e-16	51	192	4	153	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	9.01e-10	220	305	4	88	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.
pfam04685	DUF608	0.008	426	540	112	206	Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBH20286.1	1.69e-186	2	658	6	672
QQQ94267.1	2.03e-184	4	652	7	657
ANU76688.1	2.03e-184	4	652	7	657
ASU29495.1	2.03e-184	4	652	7	657
AYQ75662.1	6.89e-183	32	658	18	648

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W5M_A	1.68e-22	25	631	296	897	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]
4XHC_A	4.11e-17	293	649	173	534	ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]
2OKX_A	3.13e-14	31	189	16	176	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
Q82PP4	9.11e-22	25	631	296	897	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

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
1.000078	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002624_00754.