CAZyme Information: MGYG000000123_04101

Basic Information

• Species: Blautia sp001304935
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp001304935
• CAZyme ID: MGYG000000123_04101
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
626	MGYG000000123_14|CGC3	71139.35	4.7098

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000123	5803260	Isolate	Canada	North America

• Gene Location: Start: 146919; End: 148799 Strand: -

Full Sequence      

MEKPCLIPKPQVYLQRAGYFVKKAAVSKERMPGGLEAPLAVIWPEVTGTEDTIQFTEKKE
MQKEQYVLEITEEGIEISWGSPAGAFYAVMTLHQLVLFSEGKIACCRIEDFPGLRDRAVM
IDISRGKVPKVESLKAMIDLLAGLKINQFQLYVEGFSFAYPSFSEVWEKRAKDYLTPAEI
RELDAYCAERFIELVPNQNCLGHMNAWLETEAFGHLAENPGGLQIKGTTLPPATMDPTNP
ESLKLIEQMLDDLLPCFHSRMFHADLDETFDLGYGKNKDKAEKEGVVSIYLDYVKKLSEK
VKARGHNMMMWGDVLSKEEDAAAQLPKDIIVLDWGYEKEHPVRRRAERLQRAGVEFYLCP
GTNSWCSFTGITDNMMQCTENAVSAAYDFHARGLMVTDWGDFGHLQYSLFSLPGILYGAA
GAWNRELVTEEELAEALNRYVFRDETGIFGRLCLEAGRYSRKEEFLFPCRTLAFMTLQTG
CVSRDRFEASIKNMVDSMRFFVEPCVYLPCEEAYAGRSGMEEEAILEYLDELAVQARKAD
PACPDGTLLKEEMINGLAMVRAATRTRALCYGLEDGSGLEKEIEDLCERHRNLWQKRNKT
KGQEDSLLGFTTLLEQLRERKQEEEE

Enzyme Prediction     

No EC number prediction in MGYG000000123_04101.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	117	425	2.3e-49	0.9495548961424333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	3.71e-92	117	424	2	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.
cd02742	GH20_hexosaminidase	6.14e-32	116	412	1	293	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.
pfam00728	Glyco_hydro_20	6.56e-29	117	362	4	263	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06564	GH20_DspB_LnbB-like	4.27e-24	116	336	2	223	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.
cd06570	GH20_chitobiase-like_1	1.33e-22	117	334	4	223	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
QJD87484.1	5.16e-128	2	618	4	624
AIQ67154.1	2.19e-120	61	607	82	620
QUL55869.1	2.19e-120	66	607	87	620
AYQ72904.1	2.78e-119	47	619	71	630
BCG57589.1	1.67e-118	55	607	77	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YHH_A	1.61e-17	62	334	90	383	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
4H04_A	1.33e-15	52	334	98	375	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
6EZR_A	1.25e-14	53	369	198	534	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]
4PYS_A	8.75e-14	64	336	78	363	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]
6EZT_A	1.15e-13	53	369	195	531	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	8.94e-12	117	413	2	304	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q8WVB3	3.06e-11	117	413	10	312	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
B2UP57	1.67e-10	49	269	40	280	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
Q3U4H6	5.04e-10	117	336	10	225	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
P96155	8.20e-10	66	361	210	523	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1

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
1.000045	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000123_04101.