CAZyme Information: MGYG000001850_00923

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; QALW01; UMGS1322
• CAZyme ID: MGYG000001850_00923
• CAZy Family: GH78
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
826		93619.78	5.1148

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001850	2350438	MAG	Denmark	Europe

• Gene Location: Start: 44139; End: 46619 Strand: -

Full Sequence      

MNKAQFQHYVMAPQSRECYPQAVKDIYGNVTDAENLLSGGAETVVLRYDSETAPKIILDL
GEASTGGYPVFKVKSFGGNPVLRLAYSDWYDYIVDKDFGEIGDFRRGCCKYLGVELPVLP
GDPNRFNLFTITHNGLYISPLIQGQQRWLMLKLDTPDSFVELEFVYIHYTANMSPYDGFF
ECSDQDLTKLWYASAWTCQIATLENSQSWDTLCGRLLLRALTKGNDAGVYKAGINLTDYK
MSFEGAIAYNPHMGSGIGLLLRAGDITGGYAVFFNLDGTVQAYKRKNNVYKLLKEAAVDF
QVVDNRFYAIEAIAQGKEFTIKIDGKIALTFSDDEYSRGTFGFCQTTEKWALAKNLTVSD
LNGTVLWQDDFRHGLDAYDFTRSAPFVSDGAKRDRLPWIGDLDWAGRNIYYAFKDYIAMP
ESLRMFAFNQTPEGFIWGTCYPENTKKPDIGEYGYYESDIFSAWIIPTLADYLLFTGNTS
FAEEIYPNIKADADYLWRFVEADGLFNQRYATSKGLWDHVLNDIGKFAYNNLIVSDAFSE
AAFIAEKLGKQEDAAEFTRRKERMHKAIRKAFWDEEKGWLTKSTVDRDMCEMANSLALSI
AFFEDKKDAKRALDALLARTPGHGKITALMIRGAYMYDFDREAIGTLIQPGYQYVKDQGD
FIVYDALENPNFDFSSHQMHPANWIKALKDWRGPHTTWECMTYPPQKHSYGGAWGDRSHP
DTAVAHILSGYVLGVLPDEIGFRSFTVKPHTSGLSCARGIVPTAYGDIELEWQKENEFLT
LNLTFTGSNTLTDIRLNKKDAHEFVVTCNKKRLFACGETDGYIIFK

Enzyme Prediction     

No EC number prediction in MGYG000001850_00923.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	387	784	8.3e-48	0.7043650793650794

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	2.66e-12	389	624	34	259	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.
pfam17390	Bac_rhamnosid_C	4.51e-06	734	784	1	52	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.
TIGR01577	oligosac_amyl	8.30e-06	472	583	365	468	oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.
pfam06202	GDE_C	1.19e-05	462	614	86	257	Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
PLN02567	PLN02567	4.91e-05	542	584	342	389	alpha,alpha-trehalase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTH42040.1	5.12e-251	1	814	1	781
QJD86808.1	8.61e-242	9	814	15	790
ACU72642.1	2.90e-51	52	787	101	816
ABK06922.1	1.76e-46	13	790	67	828
AMU18509.1	2.00e-41	20	773	81	823

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1V7V_A	6.74e-06	464	579	430	553	Crystalstructure of Vibrio proteolyticus chitobiose phosphorylase [Vibrio proteolyticus],1V7W_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc [Vibrio proteolyticus],1V7X_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc and sulfate [Vibrio proteolyticus]

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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001850_00923.