CAZyme Information: MGYG000003018_01603

Basic Information

• Species: Alistipes_A sp900549685
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900549685
• CAZyme ID: MGYG000003018_01603
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
929		104529.76	4.9738

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003018	2600623	MAG	China	Asia

• Gene Location: Start: 2915; End: 5704 Strand: +

Full Sequence      

MLAAALLHFSGNARVKQTEPVSLAGKWRFSLDEKDAGVREKWFSRALPQATELPGSCEQF
GFGTPAGEPTVGRLTRVVRYEGKAWYQRDIDIPQAWRGKRVELMLERCHWESNVWVDDKP
FGMQNSLSAPHVYDLGELSPGRHVLTICIDNTYKIPVGTWVHALTEDTQGNWNGIIGRIE
LRATDPVWIRDVQIFGDRMTVEVGNATGRSVRATVDGTSFTVPDGGATVELPMAPEKEKW
NEFAPVLHEKTVSLKASSYRDSRTVRYGVRKLAVENEQFTIDGVPFLMRGPVDECVYPLT
GYPPMDKEEWARILSICKSYGFNYMRFHSWCPPEAAFAAADEAGFFFQIEIPLWTMDAPH
FGQHPERDRFIENELDLILKTYGNHPSFALMAMGNESSGSLDRLVAEGRKKDSRHLYRCE
NGETSEAGDFFETGQRGVAGPRTDWDRWTVGAWIAGSEDGQDDRPKGGPVPTLSHEVGQW
AMYPDFDEIAKYTGTLRAYNYEGYRRSLEKNGMLAQNKDFARASGLFSVLLYKDEIEASM
RSWPHGGFQILEARDYPGQGTAIVGWLDAFWDSKGLIEPEDFRRFCGSTVVLARMPKRVY
TEDETFRVQAELANYGPRDLKEQTLWQLKDEKGNTLAEGTLPAAEAPVGRVTSLGEISVP
LAGAASPCRLIFSLVSGDAANDWNIWVYPARQSEAPQDVRIAYRYDKQTREALARGEKVL
LFSDPTKGLYKIDRVMLGPDEVRLFEVKRGQNALAGSFLPAFWNLRLFNQVGTLGLLCDP
DHPALAGFPTECHSDWQWADLLGRYSASDSFRTAGAPADYCDEMERRWGDVSDRSKAIVL
NDTPEDFRPIVQVIDNYERNYKLGMIFETRVGNGKLLVCAMDLDTDAAERPAARQLKSSL
LNYMAGESFAPKHELSADLLERILTFDEE

Enzyme Prediction     

No EC number prediction in MGYG000003018_01603.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	17	429	6.5e-59	0.48936170212765956

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10150	PRK10150	1.55e-21	22	290	14	296	beta-D-glucuronidase; Provisional
pfam02837	Glyco_hydro_2_N	4.28e-13	22	151	3	135	Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
COG3250	LacZ	4.46e-13	22	398	14	408	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA23712.1	0.0	1	929	8	936
AQT69276.1	1.25e-227	1	929	13	923
QOY86859.1	3.12e-226	53	924	37	864
ASV75422.1	6.10e-222	12	911	23	941
AQT69150.1	9.00e-216	21	929	25	944

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JHZ_A	1.04e-18	23	290	17	294	Structureof E. coli beta-Glucuronidase bound with a novel, potent inhibitor 2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-N-[(1S,2S,5S)-2,5-dimethoxycyclohexyl]acetamide [Escherichia coli K-12],4JHZ_B Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-N-[(1S,2S,5S)-2,5-dimethoxycyclohexyl]acetamide [Escherichia coli K-12]
3LPF_A	1.04e-18	23	290	17	294	Structureof E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea [Escherichia coli K-12],3LPF_B Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea [Escherichia coli K-12],3LPG_A Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea [Escherichia coli K-12],3LPG_B Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea [Escherichia coli K-12],5CZK_A Structure of E. coli beta-glucuronidase bound with a novel, potent inhibitor 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)thiourea [Escherichia coli K-12],5CZK_B Structure of E. coli beta-glucuronidase bound with a novel, potent inhibitor 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)thiourea [Escherichia coli K-12]
3K4A_A	1.38e-18	23	290	17	294	Crystalstructure of selenomethionine substituted E. coli beta-glucuronidase [Escherichia coli K-12],3K4A_B Crystal structure of selenomethionine substituted E. coli beta-glucuronidase [Escherichia coli K-12]
6LEM_B	2.38e-18	23	290	13	290	ChainB, Beta-D-glucuronidase [Escherichia coli]
6LEJ_B	2.39e-18	23	290	15	292	ChainB, Beta-D-glucuronidase [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05804	1.31e-17	23	290	15	292	Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2
Q56307	7.39e-13	9	420	29	467	Beta-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=lacZ PE=1 SV=2
P08236	1.11e-11	23	402	41	457	Beta-glucuronidase OS=Homo sapiens OX=9606 GN=GUSB PE=1 SV=2
Q5R5N6	5.77e-11	16	402	34	457	Beta-glucuronidase OS=Pongo abelii OX=9601 GN=GUSB PE=2 SV=2
Q48727	9.65e-11	19	428	36	465	Beta-galactosidase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=lacZ PE=3 SV=3

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
0.998568	0.001442	0.000007	0.000003	0.000001	0.000003

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003018_01603.