CAZyme Information: MGYG000004281_00854

Basic Information

• Species: Parabacteroides sp900552465
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900552465
• CAZyme ID: MGYG000004281_00854
• CAZy Family: GH20
• CAZyme Description: N-acetylneuraminate epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1699	MGYG000004281_7|CGC3	191843.04	6.6784

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004281	4813571	MAG	China	Asia

• Gene Location: Start: 67494; End: 72593 Strand: +

Full Sequence      

MKRILFILVSLGLGILAAQAAGIPHLLPWPQKVIWTGEEFHTDETKVSPGGNKSSIGMKL
LADYGVATAPSSPLRLSINLVEDLPEIPLNRDEAYKLRVTASGIEIEATTETGIYRAIQT
LRQLTEKKSNGIAITGCEIIDWPAFRIRGFMQDVGRTYISMDELKREIAALARYKINVFH
WHLTENQAWRLQSKRFPMLNDSTNMTRMPGKFYTLEEAHELVDFCKQHHVMLIPEIDMPG
HSAAFVRAFGHDMQSPEGMRILKILLDEVCETFDVPYLHIGTDEVQFTNPDFVPEMVAYV
RSKGKKVISWNPGWHYKPGEIDMTHLWSYRGKAQKGIPAIDSRFHYLNHFDTFADLFALY
NSRIYNEPQGSDDLAGTILAVWNDRMIQPEADIIKQNNFYPNMLAIAERAWRGGGNEYFD
KQGTALPPEESEEFKAFADFENRLLWHKEHCFQGYPFAYVRQTNAKWRITDAFPNQGDLT
RSFPPEKALHTQYAYNGKTYRTHEARGAGIYLRHVWGTLVPGVFKQPEENHTAYAWTWVY
SPEAQDAGAWIEFQNYSRSEMDLPPMPGKWDYRESRVWLNDREILPPVWTATHREKSNET
LLGNENCVVRPPIPVHLKKGWNKVFLKLPVGRFTQPEIRLQKWMFTFVFVTPDGEKAVDS
LIYSPDKTFPVAEAKKIKVACVGNSVTYGYGIENRETNSYPAQLQRMLGDRYEVANFGKS
GATLLRRGHRPYNEQEECRAALDFAADRVVIHLGLNDTDPRDWPDYRDDFVKDYLRLIQA
FRRANPECRIWICRLTPISHRHPRFKSGTRDWYWQIQQTIEEIASLANTGLIDLQAGLYD
RPDLLPDALHPTAEGAGIIARTVSQALTGNYGGLQMPVTYSDNMVLQREKPLVIAGIANA
GEEVTVRIAGQQGQTVTGANGRWSVTLPPMQAGGPYTLSISAGSKRLDYTNVLIGEVWLC
SGQSNMAFQVSGAIDSQRKELLEFAAGKPQIRLFDMKPRWETYAVEWDASVLDSLNRLQY
YHNTRWQECDPATADRFSAVAFAFGQMLSDSLQVPVGLILNAVGGSPTEAWIDRKTLEFD
FPDILYDWRENDFIQDWVRGRASLNIKKSANKQQRHPYEPCYLYESGIQPLGKFPIRGII
WYQGESNAHNVEAHERLFRLLTESWRENWQEELPFYYVQLSGIDRPSWPRFRDSQRKLMQ
SIPNSGMAVSSDRGDSLDVHPRYKREIGERLAHWALHETYGHDCLPSGPLYRSVSFKADT
AYITFDYGAGMHSADGGELRTFEIAEHDGLFVPAEARIVDGKTIKVWSSPIKHPGFVRYG
WQPFTRANLVNGEGLPASTFRSEASSIDWSGLPDLPNAGQTSASGVSAPFAGVSNGQLLV
AGGCNFPGKPAAEGGAKRYYNEIYAWDLTGQAAAEWRMIGQLPKPVAYGASVTTPQGIVW
IGGNNEKRASKEVLLVNWLTAEGKLSISKLPELPVAMDNFAATYADGQIYVTGGNQQQKP
SNALYALRLTESGDGEWTRLPDFPGPARIQPVLTAQQSQDGTRLYLAGGFQPVSGRRQAV
VSTDMLSYHPEKKEWRQESILPFSAEGSPNTLTGGCAVSSGNNSILLMGGVNYSRFRDAL
NTPSPDYLLHPVEWYRFNTFLLQYDTFTRKWEIIGEDERLARAGAGIALDGDEIILINGE
LKPGIRTPEVNRFRLKGSK

Enzyme Prediction     

No EC number prediction in MGYG000004281_00854.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	142	412	5.7e-61	0.9643916913946587

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR03548	mutarot_permut	3.60e-113	1365	1691	3	331	cyclically-permuted mutarotase family protein. Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family (TIGR03547) and this cyclically-permuted family have multiple repeats of the beta-propeller-forming Kelch repeat.
cd02742	GH20_hexosaminidase	3.49e-93	147	412	1	303	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
cd01827	sialate_O-acetylesterase_like1	3.84e-76	677	868	1	188	sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
cd06563	GH20_chitobiase-like	4.34e-50	145	444	1	357	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
pfam00728	Glyco_hydro_20	2.34e-45	145	411	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT50180.1	0.0	1	667	1	667
QIX64921.1	0.0	1	667	1	669
QUT52022.1	0.0	1	667	1	669
QUR48261.1	0.0	1	667	1	669
QUT21124.1	0.0	24	667	24	669

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KMM_A	2.81e-55	876	1343	25	634	ChainA, Sialic acid-specific 9-O-acetylesterase [Xanthomonas citri pv. citri str. 306],7KMM_B Chain B, Sialic acid-specific 9-O-acetylesterase [Xanthomonas citri pv. citri str. 306]
4PYS_A	1.22e-36	93	467	78	505	Thecrystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343],4PYS_B The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343]
6YHH_A	1.60e-36	25	411	8	476	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7DUP_A	8.06e-36	67	284	59	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
7DVB_A	3.50e-35	67	284	59	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P82450	6.01e-37	879	1321	30	509	Sialate O-acetylesterase OS=Rattus norvegicus OX=10116 GN=Siae PE=1 SV=2
P70665	5.07e-34	879	1285	30	468	Sialate O-acetylesterase OS=Mus musculus OX=10090 GN=Siae PE=1 SV=3
Q9HAT2	5.32e-34	873	1304	25	464	Sialate O-acetylesterase OS=Homo sapiens OX=9606 GN=SIAE PE=1 SV=1
Q5RFU0	2.31e-33	873	1267	25	425	Sialate O-acetylesterase OS=Pongo abelii OX=9601 GN=SIAE PE=2 SV=1
P49008	4.70e-32	25	284	36	335	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA 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
0.000238	0.999087	0.000182	0.000160	0.000159	0.000149

TMHMM  Annotations     

start	end
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