CAZyme Information: MGYG000000043_00073

Basic Information

• Species: Phocaeicola sp900066455
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900066455
• CAZyme ID: MGYG000000043_00073
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
836		93878.37	7.9508

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000043	4183533	Isolate	United Kingdom	Europe

• Gene Location: Start: 92906; End: 95416 Strand: -

Full Sequence      

MFQAKFLPVRDFLNNLQLLIFFIHTYTMKSIFIRKWKGVAVMACTISLHTFSLSAQNRLV
LHYDRPAEYFEEALVIGNGTMGAILYGGTDKDVLSLNDLTLWTGEPDRKITTPDAHKAIP
EIRALLDKEDYRGADLAQRKVQGHYSENYQPLGQLSLTYLDEPAQVTGYQRSLDIRQALA
RTSYQRNGKAFSCDYFASAPDSVIVLRLQTESEKGIQALLSFTSLLPHATTASGNEISAE
GYAAYHSYPVYFDDVKNKHLYDPERGTHFRTLIRVIAPESQVKSFPSGELKIAGGKEALI
LVANVTSFNGFDKDPMKEGRDYRNLVAQRMNRAARKSFETLEKAHVADYQSFFNRVELNL
GSTDKAIANLPTDIQLLQYTDQSQKNPELEALYFQYGRYLLISSSRTPGVPANLQGLWNE
RLLPPWSCNYTSNINLEENYWAAETANLSEMHRPLMEFIANLQHTGEATAKAYYGVQKGW
CLGQNTDIWAMTCPVGLNVGDPSWACWTMGGAWLSTHIWERYAFTQDKAFLQQYYPALKG
AAEFCLNWLIEKDGKQLTSPGTSPENKFVTPDGYVGATSYGCTADLAMTRECLIDAAKAA
EVLGTDKDFRKQIDKTLARLLPYRIGKNGNLQEWFHDWSDEDPQHRHQSHLFGLYPGRHL
SVENTPDLAKACARTLEIKGDNTTGWSTGWRVNLYARLKDGKNAYHIYRRLLRYVSPDGY
KGKDARRGGGTYPNLLDAHSPFQIDGNFGGCAGVIEMLMQSSENSITLLPALPDEWKDGS
VKGICARGGFVIDMEWKDGKVTSLHIQARKGGKTKVSFNGKTKTVNLKANKGIQLL

Enzyme Prediction     

EC	3.2.1.63

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	56	824	1e-267	0.9903047091412742

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	9.61e-71	61	310	1	233	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.
pfam04685	DUF608	0.001	518	619	108	201	Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.
COG3669	AfuC	0.004	379	519	135	259	Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJR97976.1	0.0	59	836	1	778
QCD34846.1	0.0	37	835	5	804
QCP71443.1	0.0	39	835	6	802
QCD40341.1	0.0	39	835	6	802
QCD41177.1	0.0	43	836	9	802

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2RDY_A	1.56e-183	59	810	3	746	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
7KMQ_A	3.40e-164	53	822	35	763	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]
4UFC_A	1.09e-151	52	816	15	741	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
2EAB_A	2.34e-91	71	818	49	851	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	3.24e-91	71	818	49	851	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	8.86e-164	59	820	52	816	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797	1.15e-87	64	801	26	761	Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81	1.29e-79	50	821	11	801	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	2.82e-52	42	796	1	694	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.985687	0.013960	0.000196	0.000045	0.000043	0.000061

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000043_00073.