CAZyme Information: MGYG000000201_02429

Basic Information

• Species: Blautia_A sp900066145
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900066145
• CAZyme ID: MGYG000000201_02429
• CAZy Family: GH78
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
522	MGYG000000201_9|CGC2	59375.9	4.6179

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000201	4593677	Isolate	China	Asia

• Gene Location: Start: 55842; End: 57410 Strand: +

Full Sequence      

MPEVSIDLNMVRVTNDDFVKKAEACAPKLQETVVKPVSIVDVVKTENIYPDVVVKDSIEN
LSSYHLAKGDKLCLDFGDHQVGYVTLKLASVGSPQDSPAFFRLKFGEIAKEMTEDSADYD
GWISRGWIQEEFIHIDVLPAELKLPRRYAFRYLEIEAIDTSLKWQMVVEDVTCVSVSSVN
MDQVKPIKSDDEMIRTLDKVSLRTLMNCMQSVFEDGPKRDRRLWLGDLRLQALANYDTFK
NYDLVKRCLYLFAGQTRDDGMVSACLFTEPKFIVDDTFLLDYSMFYGAALLDYYKASGDM
ETLRDLSKCAYRQMELAGKQFDEKDLLICGEGFWAFIDWTDGLDKQAAMQGVYIYCAKKV
REIAEILGDTEKAAELAKEEKAKTEAAKKYLLDSEAGLFVSGPDRQINYASQVWMVLAGA
VDKEDGAQILEKVTDMKPEKGMVSPYMNHHYVEALLLCGKKEQALDYMKYYWGGMISHGA
DTFWELYNPENPAESPYGSSIVNSYCHAWSCTPTYLLRKYFA

Enzyme Prediction     

EC	3.2.1.40

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	68	521	1.3e-83	0.8611111111111112

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	4.83e-22	182	520	1	339	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.
COG3459	COG3459	6.45e-08	289	505	677	942	Cellobiose phosphorylase [Carbohydrate transport and metabolism].
pfam17167	Glyco_hydro_36	0.001	276	446	122	307	Glycosyl hydrolase 36 superfamily, catalytic domain. This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region.
cd01967	Nitrogenase_MoFe_alpha_like	0.004	355	405	244	298	Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Three genetically distinct types of nitrogenase systems are known to exist: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). This group contains the alpha subunit of component 1 of all three different forms. The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. The role of the delta subunit is unknown. For MoFe, each alphabeta pair of subunits contains one P-cluster (located at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein is a homodimer which contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo- nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL22278.1	0.0	1	521	1	521
QCU02819.1	0.0	1	521	1	521
AGF55542.1	2.78e-188	15	521	15	520
AWH77632.1	2.88e-188	15	521	16	521
AXU46522.1	2.88e-188	15	521	16	521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4XHC_A	1.39e-148	17	520	38	541	ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]
3CIH_A	1.25e-27	75	521	197	636	Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000201_02429.