CAZyme Information: MGYG000001489_00666

Basic Information

• Species: Parabacteroides goldsteinii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii
• CAZyme ID: MGYG000001489_00666
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
812		92888.91	6.2465

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001489	6453137	Isolate	not provided	not provided

• Gene Location: Start: 787126; End: 789564 Strand: -

Full Sequence      

MCLVRFFSLIISLSLAVSAYGNDDLFIGSKTDKPASIWQEGMLTGNGIMGAIMFGNPICE
EIVFTHNELYLPLGTKEIVPDLRTCFDELKKKALDSGNMAPSVFHAEILKKTGKTISWTD
PFHPGFSLQIKDSLRGREYTDYEMSENFSTGELAVSWTDKYGEKWNRRLFISRKDSVGVM
EINGPKGKVGGTFSLSLGHDLVSVKKSAFNNELRAHVVYDKGKGGYENVVRIIPLGGRLE
VKGNDIEVHNSDKILLFIQIRPWKSPLSKELSEAWAYNPSNPDFSSNTNSDKLTDIHNCM
DRLQTDYKELLKAHSLLHSELFGRVELSLGNDDKGRSEINTLKLLQMCRNDRQASPEFIS
YLYDACRYLIVCSTNNKPANLQGLWTGTWNPEWSGDYTLDSNIQLEIQSLMSCNMPELME
GYFKLIESWVEDCRTNALKMYNCRGIVSNPRASNTPLYLHWGNWPGELAIGTMGWMLHFF
YDYYLFTGDKSFLRDRVVPLLKESALFYEDLLAGTEDENGKYRFFISYSPEQDDLLYMNS
TFDVAVAKNVLTNLIKSSRILGIESDNIPKWEMMLKKMPEYKINASGVFSEWTVEGVREN
PNHRHHSHLLPLYQFCEFDRSDTIMWNASCKAFEEKVLHWLNNNDNPDSNHITHGLMNQL
QCAARLGRGDIIQYVFDLLVSGNYIYPNFMISYWPGLRGFGFDPVGTIPDVINNSLIFSW
NDKIDILPALPKTWRRGSLSNILLRGVVKVDKFSWDLDKGEIFLVLYSDTDKDVEFILPD
KYFVFSVDSNQSGNKIKLFKGKNQFRFKQIKS

Enzyme Prediction     

No EC number prediction in MGYG000001489_00666.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	31	773	5.2e-132	0.9653739612188366

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	1.35e-18	32	258	4	225	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	2.03e-07	461	620	106	275	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	7.12e-05	455	578	418	548	Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQT00436.1	5.52e-165	28	802	6	758
QFK72468.1	1.01e-151	31	809	16	775
QUE51752.1	4.56e-149	28	780	35	793
BAM46900.1	1.97e-133	32	779	16	725
QGH33961.1	1.43e-131	28	779	9	724

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KMQ_A	1.62e-35	33	756	47	738	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	8.32e-32	33	751	28	718	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
2RDY_A	2.22e-29	32	751	8	729	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
2EAE_A	7.66e-25	28	746	36	820	ChainA, Alpha-fucosidase [Bifidobacterium bifidum]
2EAB_A	1.01e-24	28	746	37	821	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	8.95e-24	34	750	59	788	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
Q2USL3	2.25e-06	29	756	17	695	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
0.000277	0.999071	0.000171	0.000151	0.000143	0.000139

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001489_00666.