CAZyme Information: MGYG000004596_01374

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-617
• CAZyme ID: MGYG000004596_01374
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1033	MGYG000004596_64|CGC1	113554.48	5.1779

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004596	2214446	MAG	France	Europe

• Gene Location: Start: 80; End: 3181 Strand: +

Full Sequence      

MGKRFYFLLGALFCLVFRTYAQLPSFSTDTDEEWYVLQFTTGEAVLQDQGEGRNLQTATL
SNDDSQRWKLLGSPESLHLVGKSGRYVGFSGSRFVATAAADEASDFALVQNGTSWELKYL
GAADGDYAYLNQFGGTGAGRELGTWTAGDKNNLLRFVQPKEVVVPYNVRPVVGYEPEHKN
TLWYTLPTTRATVENPWMEFALPIGNGQFGAMVYGGIAQEQIQFNDKTLWTGASTTAERG
AYQNFGNVYVEDLSGVFGSTSGQTVQDYYRQLDLHTATASVHYKSPDKSVSYSREYIASY
PDQVVAMRLAASEGGQISVRVSMDDAAGRSLPAYADGGGHFSGKLTTVSYDARLRVVPTG
GTMTTAADGVTVSGADEVLIVLAGATDYDPTSLTYVSQTAQLADKVRARVDDAAAKGWAE
LYATHEADYRSLFDRVVLDFPTSENTMTTDRLVTRYNQQPVSSTQPYVLMLEQLYFNYGR
YLMIASSRGVDLPSNLQGIWNNSSTPPWESDIHSNINVQMNYWPAEPTNLSELHLPFLNY
LYNMAEVQPQWKAYARQSGQTTGWTCFTQNNIFGQSNWGENSVVANAWYSSHIWQHYRYT
LDKDYLREKGFPVMLSAAKFWLERLIKDRRVNDGTWVCPDEYSPEQNNAAIIKQDATAYA
QQLVADLLHNTLEAIRVLGQEEAGVDDAFVAELTEKYTHLDRGLHAEEYTGAWGATLNGV
RTGDPLLREWKYSGYENGENGHRHLSHLMCLYPLGQINQSDSLFEAAVNSLKLRGDESTG
WSMGWKINLWARALDGNHARRILRNALKHSTSYATNQYAGGIYYNLFDSHAPFQIDGNFG
ACSGVAEMLLQSYTDTLHLLPALPAQWRAGTIKGLKGVGDFTVDQTWANVRLTQAVITSG
AGQECAVRYAGVAGAKVTDETGAEVPVTVVNDDVVKFATRKGGVYTLTFGGGEVGIRPDA
TAASGCPLTVSGRTLTAPDAVTRMSVADAEGRSWGATSGRSLTVKRAAGPVVLVRLTWND
GSAGTYKVALHDE

Enzyme Prediction     

No EC number prediction in MGYG000004596_01374.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	178	912	6e-210	0.9847645429362881

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	1.65e-49	182	389	1	232	Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.
pfam03632	Glyco_hydro_65m	4.16e-07	593	691	125	220	Glycosyl hydrolase family 65 central catalytic domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.
COG1554	ATH1	7.44e-05	545	691	409	539	Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
PRK13807	PRK13807	0.007	593	624	434	465	maltose phosphorylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ13809.1	2.52e-303	23	1030	114	1131
QFQ12384.1	1.62e-245	22	937	192	1113
ASE18155.1	7.19e-243	23	947	186	1104
ADK97265.1	7.19e-243	23	947	186	1104
QUB64500.1	4.01e-242	23	947	186	1104

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2RDY_A	4.50e-114	197	947	14	789	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
4UFC_A	7.85e-112	182	908	24	742	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
7KMQ_A	3.25e-104	182	911	43	761	ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]
2EAB_A	5.20e-101	182	948	20	895	Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]
2EAD_A	3.65e-100	182	948	20	895	ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	1.54e-96	197	915	63	820	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797	1.55e-79	181	887	22	756	Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81	2.05e-64	204	887	46	775	Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1
Q2USL3	1.33e-51	180	914	16	719	Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000261	0.999133	0.000164	0.000148	0.000140	0.000128

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004596_01374.