CAZyme Information: MGYG000000658_00963

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia
• CAZyme ID: MGYG000000658_00963
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
951		105833.07	6.471

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000658	1755704	MAG	Germany	Europe

• Gene Location: Start: 117691; End: 120546 Strand: -

Full Sequence      

MRKHLCYLLGVLYSLVCVAQAQPLKFSNGAEEQWYVIQFTAGEAVLQDEGNGQNLKTAAL
AGTDVQLWKLTGSPERMQLIGKSGRYVEFNGKRFQTTETATRAADFELVKNGSSWELKCI
TAKWGGTSFLNQFGGAGAGQELGVWTAGDNNNLLRFVVPKEIVQPFPVVGVKKYEPEHIN
TLWYDRPVTLASVKNPWMEYALPVGNGQLGAMVYGGIAQEQIQFNEKTVWTGDSTTARRG
AYQSFGNVYIRDISGVFGPSAVTAVREYYRQLDLSTGVASVHYQSPDKSVTYTREYIASY
PDQVVAMRLSASAPGKISVRITMDDEAGRTSPSYADGEARFAGKLTTVSYDCRMKVVPAG
GTMSTGEDGITVTGADEVLLVLAGGTDYAPSELSYVSGTAQLGEKMQARVDGAAAKGWAA
LYARHEGDYQRLWNRVELRFPLAANTMPTDQLVDRYNELDFNSPQPPAFMLEQLYFHYGR
YLMIASSRGVDLPSNLQGIWNNSAAPPWESDIHSNINVQMNYWPAESANLSELHLPFLHY
LYNMAEVQPQWRAYARQSGQSVGWTCFTQNNIFGQSNWGENYVVANAWYATHIWQHYRYT
LDRDFLKDKGFPVMLSATKFWLERLVQDRVVNDGTWVCPDEYSPEQNNQTILKQDATAHS
QQLVWDLFHNTLQAIEVLGLADAGVDRDFVEKLTERFNRLDRGLHTEIYTGVWGDTLNGV
VKGDTLLREWKYSGFENGENGHRHLSHLMCLYPLGQVYPGSPLFRAAVNSLKLRGDASTG
WSMGWKINLWARALDGDHARRILKTALKHSTSYNVDQYSGGVYYNLFDSHAPFQIDGNFG
SCAGIVEMLLQSHTDTLQLLPALPSLWRDGVVSGLKAVGDFTVDQTWHDGRLTEAVITSG
AGRTCAVRYKGIAQASVTDMNGTAVKIVAKGDDLITFNTRSGGVYRLTVRR

Enzyme Prediction     

No EC number prediction in MGYG000000658_00963.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	180	913	1.5e-211	0.9833795013850416

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	4.82e-54	182	388	1	231	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	3.55e-06	580	692	114	221	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	5.19e-04	580	648	432	501	Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03636	Glyco_hydro_65N	0.006	247	392	75	209	Glycosyl hydrolase family 65, N-terminal 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. This domain is believed to be essential for catalytic activity although its precise function remains unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ13809.1	1.57e-284	19	942	110	1044
QFQ12384.1	2.90e-253	26	939	196	1115
BBA29879.1	2.68e-237	27	947	190	1104
QUB76594.1	2.12e-236	27	945	190	1102
QUB64500.1	8.39e-236	27	945	190	1102

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2RDY_A	6.63e-120	197	907	14	752	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
4UFC_A	5.52e-111	182	922	24	757	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
2EAB_A	3.00e-106	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	2.16e-105	182	948	20	895	ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]
2EAE_A	4.08e-105	182	948	19	894	ChainA, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	4.94e-104	185	916	49	821	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797	3.64e-87	181	895	22	764	Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81	2.50e-69	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	4.49e-53	180	900	16	707	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
0.000262	0.999115	0.000158	0.000163	0.000147	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000658_00963.