CAZyme Information: MGYG000000273_02446

Basic Information

• Species: Phocaeicola coprophilus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprophilus
• CAZyme ID: MGYG000000273_02446
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
606		69675.88	6.099

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000273	3492533	Isolate	China	Asia

• Gene Location: Start: 5155; End: 6975 Strand: +

Full Sequence      

MFSIRFTVITLFLLQLAVHAYGGMEHFRILPEPQSVEIMKGKGLHYNDLSFIVNRSGEDY
PVLGTMLGSLPHKERNGKGVYLSLSEKEVPQSPEGYVLQVSEKGVFITSSGQAGLFYGCQ
TLEQLMEDSRDFGLQIPALKITDYPDIAYRAVHLDTKHHLDRMEYYYRMVDKLARYKVNA
IIWELEDKFEYSSHPEIASPNAISKQEMQAFCRYARERNIEISPLVQGLGHASFILKHHW
ELRENPESDWEFCPSNPKTYEFLYDLYQDAIEAMPYGKYLHIGGGEITAIGIDKRCKETG
KTAFELQMHWLKQVCDYAKSHGRTPIFWDDMPLKFAGLWPQILGDETESELDKSWNTEKL
DQAIELFPKECIYMRWNYGDATKPAHKRLLKWYKEKGLPVMAATAASAGDSPFMPREYTK
ANYIKGFSQLVVENDLQGILATAWDDGSPHLETVFRGYIAQGEFGWNPDGRTVEEFAEAH
GQREFGLEAGKGKTDFIQELEKAFFFFDGALVESGRRNPAWGTTHFKLIELPDKTHPGQW
TQKYQKRIEQAEKEQLRFEQIRRELTEARQEALRNRYTLFSLPYSSSETGSSHSLEVFSP
GTSKAR

Enzyme Prediction     

No EC number prediction in MGYG000000273_02446.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	147	468	4.4e-44	0.9584569732937686

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	1.53e-81	149	467	1	301	Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.
COG3525	Chb	4.19e-23	84	330	196	488	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	3.04e-22	148	366	2	250	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	5.20e-21	148	330	2	226	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.
cd02742	GH20_hexosaminidase	6.03e-21	149	331	1	193	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO25975.1	0.0	1	579	1	579
QUT49641.1	3.51e-297	3	579	2	578
QQY42843.1	6.69e-283	27	579	26	578
QQY39583.1	6.69e-283	27	579	26	578
ABR38110.1	6.69e-283	27	579	26	578

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YHH_A	6.27e-23	65	390	66	408	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
6Q63_A	7.49e-23	77	381	90	436	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
4PYS_A	1.03e-20	86	334	70	347	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]
1M04_A	1.42e-20	28	468	26	476	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
1M03_A	1.42e-20	28	468	26	476	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7WUL4	4.79e-15	24	303	1	315	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
A6QNR0	3.37e-14	150	444	2	290	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q3U4H6	7.10e-12	150	444	10	298	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
Q8WVB3	2.18e-11	150	444	10	298	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
Q04786	9.31e-10	77	237	247	438	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1

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
0.000225	0.999215	0.000150	0.000141	0.000132	0.000127

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000273_02446.