CAZyme Information: MGYG000004468_01392

Basic Information

• Species: Alistipes_A sp900539755
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900539755
• CAZyme ID: MGYG000004468_01392
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
913	MGYG000004468_5|CGC1	102983.71	5.766

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004468	2418771	MAG	Israel	Asia

• Gene Location: Start: 74806; End: 77547 Strand: -

Full Sequence      

MKRVLFMAVCAAWLGFSCTSSKIEVDELRVELRENPVGVGTDHPRFMWQIESEKPDVMQE
AYRIQVAASKDDLEKGKNLLWDSGFVDSDTSLFITYNGSQLQSATEYFWRVRVKTTGGNT
AWSETQSFATALLDSTAWKAQWIGIAGMTNPGETMGKDGAKQALPTRLAARYLRKEFPVR
SDLKRAVLYISVGGSAKSYLNGEEITEDVFESMPTHAPATMYYNSYDVTKLLGSGDNTIG
VVLGNGRFFPMRNPGTRGFGVPRLLAQLELEYRDGTKELVVTDTTWQATARGPIIANNEF
DGEEYKAYNEMPGWNRTGYKTNNKWMAAQVLPAPGGKLVAQPNENIRVMEELKPVSITKM
ANGNLLLDMGQNMVGWLHVKLEGKINKPISFRFAERLKPDGSLMTENLRTAKATDTYIPA
WNAEFEWEPSFVYHGFRYVEISGLDYMPPLHVFTGKVIYDKMETIGEFETSNPVINQIYK
NAYWGIRGNYRGMPTDCPQRDERLGWLGDRTTGALGESFIFENALLYKKWLQDIYDSRDT
LGRISDVSPRTWSVYNDDVTWPAAYFYVADMLYRQFGDKSGITTHYQAMRQWMQYMEKNA
MRDGLIYKDTYGDWCMPPEKQQLIHSEDPARKTAGEILGSSMYYSLLQMMSNFAVLSGNA
ADTTHYQQVAAQLKEAYNKKYFNYETAQYDNGTVTANLLSLRLGLVPEGYEAKVFQNIVN
KTVNESKSHVSVGVMGIQHLMRGLTEYGNPQLAYTIATNETYPSWGYMAKQGATTIWELW
NGDTAEMRMNSGNHVMLLGDLVIWLYENLAGIRNDPQSAGFKKILMQPVFIDGLDYVKAS
YNSVSGKIKSHWERKDGQIEWEITIPANTTATVNLKDVQSVEVAEGKAANVKVDSGNATI
DLPSGEYKLVVKM

Enzyme Prediction     

EC	3.2.1.40	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	357	875	2.1e-156	0.998015873015873
CBM67	166	336	4.8e-34	0.9147727272727273

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	1.82e-119	463	809	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.
pfam08531	Bac_rhamnosid_N	2.69e-48	182	350	2	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	1.84e-32	358	459	1	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.
pfam17390	Bac_rhamnosid_C	5.51e-21	811	887	1	75	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.
cd17643	A_NRPS_Cytc1-like	0.004	188	236	299	347	similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCG54613.1	0.0	1	912	1	933
QUT49169.1	0.0	4	907	7	907
SCD21045.1	0.0	4	909	13	904
CEA16358.1	0.0	18	909	24	909
SCM59085.1	0.0	4	912	5	908

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6I60_A	3.31e-163	27	912	34	942	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	1.45e-124	21	913	2	1032	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	1.43e-102	23	886	2	859	Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
T2KNB2	7.18e-141	17	899	25	894	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
Q82PP4	6.18e-123	21	911	2	1030	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
P9WF03	4.16e-122	3	908	5	907	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KPL4	3.37e-120	3	910	5	948	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

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
0.000482	0.230097	0.769113	0.000090	0.000112	0.000099

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004468_01392.