CAZyme Information: MGYG000001059_00301

Basic Information

• Species: Porphyromonas_A somerae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A somerae
• CAZyme ID: MGYG000001059_00301
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
763	MGYG000001059_16|CGC1	87105.18	4.677

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001059	2193999	MAG	Spain	Europe

• Gene Location: Start: 27901; End: 30192 Strand: -

Full Sequence      

MNAPFRFLYLGLLISLLSLTACNQATTHELEEQPALIPLPNQIEWLSNKAYTFGNHNTLS
IPKEVENRDLLAEQLNATLQEHGLPTLALTINDEGASVAISIDNQLEGNTYHLESNFTYG
VTITAGSPEAVGYAIQTLRQLVTDEGIAEVEIQDAPRLDYRGVMLDVSRHYMSIDFIKQL
LDEMQYYKFNRFHWHLVDAGGWRIEIKNYPELTEKTAYRTESDWQKWWIEKDRRYCSKDT
PGAYGGYYTQEEAREIVAYAAERGITVIPEIEIPGHSEEVLAAFPQLSCSGKALPYESDF
CIGNEESYTFLEVVLSEIMDIFPSEYIHIGGDEAGKQAWGTCSRCKKLMREMGYKHIDQL
QSHMIHAMEEYLNDNGRQIIGWDEILEGGLAPNATVMSWRGEAGGIEAAKAKHKVIMTPN
SHLYLDYYQEDPTQSEKKQIGGYLPLEKVYSYDPLPKELTPEEQSYIYGVQANLWTEYVM
DENHAAYMLFPRILALSEVAWTNPEYKSWDSFRKRVNTQVPQLIKRGINSYPLSTYLNIS
HTIDYDKRAFEVQMTTELYPYEIHYRTDGQVPTTEDPTYTEGETITLRDSATLVAGVFRD
GKLLGKPTTQRFDYHKGIGHTVKWLTPLGGGYPAGGVETALLDGLRGSITYMDGRWLGNV
ASQSTIGVIDLGEPTEINSVSTKCMHDIDPWVHMPEWVELSTSMDGKQYEVVDRVMSQTD
PKDTRLRFETFRFTPNTTARYLKIEYHLPIKDKFLFTDEIVIW

Enzyme Prediction     

No EC number prediction in MGYG000001059_00301.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	159	503	1.4e-117	0.9554896142433235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	0.0	160	516	3	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	6.96e-159	160	503	3	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	2.38e-118	35	605	135	709	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	1.07e-92	159	516	2	329	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
cd06570	GH20_chitobiase-like_1	7.29e-79	160	515	3	310	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCY55921.1	9.99e-234	61	763	26	725
QJE28072.1	2.00e-233	92	763	59	725
QRO17366.1	2.00e-233	92	763	59	725
QUT53805.1	2.00e-233	92	763	59	725
ABR42441.1	2.00e-233	92	763	59	725

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q63_A	2.75e-161	16	762	4	773	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
7CBN_A	1.97e-98	34	529	11	509	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]
6EZR_A	2.09e-88	36	529	142	636	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]
7DUP_A	4.17e-88	32	529	2	519	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	2.22e-87	32	529	2	519	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
P49008	4.86e-125	16	580	13	582	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	1.38e-98	22	529	18	528	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
P96155	9.80e-81	35	497	140	601	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	3.91e-61	106	526	55	472	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1
Q7WUL4	1.05e-53	121	521	93	468	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000032	1.000003	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001059_00301.