CAZyme Information: MGYG000002449_00864

Basic Information

• Species: Parabacteroides acidifaciens
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides acidifaciens
• CAZyme ID: MGYG000002449_00864
• CAZy Family: GH20
• CAZyme Description: N-acetylneuraminate epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1539	MGYG000002449_6|CGC3	173348.99	6.6093

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002449	5100482	Isolate	not provided	not provided

• Gene Location: Start: 81155; End: 85774 Strand: +

Full Sequence      

MKRILFILVSLGLGILAAQAAGIPHLLPWPQKVTWTGEKFHAREISVSCAWNKNSPGMEW
LSDCGISVVESPGNRRLTVNLVNSIPGIPVNPDEAYKLRVTSNEILIEATTETGVYRAVQ
TLRQLTEKTGKGISVAGCEIVDWPAFRVRGFMQDVGRSYISLEELKREIAALSRYKINVF
HWHLTENQAWRLQSKRFPMLSDSTNTTRMPGKFYTLKEARELVDFCKRHYVTLIPEIDMP
GHSAAFVRAFGHDMQSPEGMKILKLLLDEVCETFDVPYLHIGTDEVKFTNPNFVPEMVAY
VRSKGKKVISWNPGWHYKPGEIDMTHLWSYRGKAQKGIPAIDSRFHYLNHFDTFADLFAL
YNSRIYNEPQGSDDLAGTILAVWNDRMIQPEADIIKQNNFYPNMLAIAERAWRGGGTEYF
DKHGTVLPPESSEEFKAFADFENRLLWHKEHYFQGYPFAYVRQTNVKWRITDAFPNQGNL
HESFPPEKTLDTQYTYNGKTYGTCEARGAGIYLRHVWGTLVPGIYEQPEENHTAYAWTWV
YSPEAQDAGAWIEFQNYSRSEMDLPPLPGKWDYRESRVWLNDREILPPVWTATHREKSNE
TLLGNENCVVRPPIPVHLEKGWNKVFLKLPVGAFTQPEIRLQKWMFTFVFVTPDGEKAVD
GLVYSPDKKLPAVHAQKAKVACTGNSVTHGYGGLQMPVTYSDNMVLQREKPLVIAGIANA
GEEVTVRIAGQQGQAVTGANGKWSVTLPPMKAGGPYTLSISTGSERLDYTNVLIGEVWLC
SGQSNMAFQVNSAIDNQRKAFLEFAAGKPQIRLFDMKPRWATNAVEWGVSVLDSLNRLQY
YQDTEWKECNEETANRFSAVAFAFGQMLSDSLQVPVGLILNAIGGSPTEAWVDRQTLEAE
FPDILYDWRQNDLIQEWARERASLNIKKSTNKQQRHPYEPCYLYESGIQPLEKFPIRGII
WYQGESNAHNIEAHEKLFRLLTTSWRENWREELPFYYVQLSSIDRPSWPRFRDSQRKLMQ
SIPNNGMAVSSDKGDSLDVHPRHKREIGERLAHWALNKTYGHDCLPSGPLYRSVSFKADT
AYITFDYGEGMHSSDGGELRTFEIAEHDGLFVPAEALITDGKMIKAWSSQIKHPKFVRYG
WQPFTRANLVNREGLPASTFCSEASKVDWSGLPDLSDDGKSALGVSAPFAGISNGQLLVA
GGCNFPGKPAAEGGTKQYYSEIYALDITGQTQAEWRVAGQLSKPLAYGASIATPQGIVWI
GGNNDKGASKEVFQVNWQTTEGKPSISKLPELPVTMDNFAAAYADGQIFVTGGNQQQRPS
NALYSLRLTESGNGEWTRLPDFPGPARIQPVLAAQQSQDGTRLYLTGGFQPVSGRQRAIV
STDMLSYHPEKKEWRQESILPFSAEGSPNTLTGGCAVSSGNSSILLMGGVNYTRFRDALN
RPLEIEQATAAGNTLLQDSLQNEARNYLLHPVEWYKFNTTLLQYNTFTRQWNVLEENEKL
ARAGAGIAINGDEIILINGELKPGIRTPEINMFIYDPDK

Enzyme Prediction     

No EC number prediction in MGYG000002449_00864.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	142	413	2.1e-61	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR03548	mutarot_permut	4.03e-113	1182	1531	1	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	1.54e-93	149	413	2	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.
cd06563	GH20_chitobiase-like	5.64e-50	146	445	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	6.37e-46	146	412	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	2.58e-42	89	501	201	702	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT50180.1	0.0	1	669	1	668
QIX64921.1	0.0	1	670	1	671
QUT52022.1	0.0	1	670	1	671
QUT21124.1	0.0	24	670	24	671
QRO15216.1	0.0	24	670	24	671

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KMM_A	9.18e-53	696	1160	25	631	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	1.81e-37	92	468	76	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]
7DUP_A	5.25e-36	89	285	74	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	2.28e-35	89	285	74	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]
6EZR_A	6.26e-34	89	286	204	439	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P82450	1.62e-37	699	1141	30	509	Sialate O-acetylesterase OS=Rattus norvegicus OX=10116 GN=Siae PE=1 SV=2
P70665	1.76e-35	699	1105	30	468	Sialate O-acetylesterase OS=Mus musculus OX=10090 GN=Siae PE=1 SV=3
Q9HAT2	4.43e-35	693	1114	25	454	Sialate O-acetylesterase OS=Homo sapiens OX=9606 GN=SIAE PE=1 SV=1
Q5RFU0	1.44e-34	693	1087	25	425	Sialate O-acetylesterase OS=Pongo abelii OX=9601 GN=SIAE PE=2 SV=1
P49008	1.24e-31	25	285	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
0.000278	0.999001	0.000166	0.000183	0.000171	0.000157

TMHMM  Annotations     

start	end
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