CAZyme Information: MGYG000001876_01626

Basic Information

• Species: Acetatifactor sp900760705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900760705
• CAZyme ID: MGYG000001876_01626
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
541	MGYG000001876_40|CGC1	61731.67	4.8888

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001876	3172346	MAG	Denmark	Europe

• Gene Location: Start: 6593; End: 8218 Strand: +

Full Sequence      

MENTTSFKRFGIMLDCSRNAVATVDSLKKWIDITTDLGYNTLMLYTEDTYEVPDNPYFGY
MRGRYSCEELKEVDAYAKEKGMELIPCIQTLAHLNAIVRWPEYQPHFDIDDILLAEDDRV
YELIDSMFKTLSSCFTTRIAHIGMDEAHNLGRGRYLDQHGMQNRFEIMTNHLKKVCDIGA
KYGFRFLMWSDMFFRLATGGKYSSDAKISDEIKKQIPENVDLVYWDYYSTDKSHYDQMFV
SHEQLKSGTWFAGGLWSWAGLAPHNGYSMRSTEAALTSSKDHRIENVILTMWGDNGGECS
RYALLPSLFYASELAKGNTDLASIKALFEEKYGIPYDTFMLLDLPGTPDNDNSGVSNPEK
YLLYTDCFLGLFDRNLNGHEKEQFDNATSLLTEVLDTGAAKEWSYLFASMRDLSAVLAVK
ADLGVRTHKAYKSGDKEAVKALLPVYDELSKKLEAFYHSYKKQWLTDNKPFGLEVQDARL
GALMNRVHSCHDRLEDYCEGRIAKIEELEAVQLDYCGGGDIDGQDKLRVNNWCSNISTSI
V

Enzyme Prediction     

No EC number prediction in MGYG000001876_01626.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	5	314	2.2e-39	0.9525222551928784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	3.78e-112	11	315	3	299	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.
pfam18088	Glyco_H_20C_C	1.55e-58	337	524	1	191	Glycoside Hydrolase 20C C-terminal domain. This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature.
cd02742	GH20_hexosaminidase	8.21e-50	11	315	3	301	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	6.41e-14	11	208	5	238	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	8.57e-14	11	193	5	223	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
QCJ40720.1	7.73e-143	7	541	87	626
ANU74916.1	2.38e-141	2	541	77	628
QQQ92469.1	2.38e-141	2	541	77	628
ASU27725.1	2.38e-141	2	541	77	628
QEH70468.1	4.67e-141	1	541	79	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2EPL_X	1.90e-135	1	532	78	615	N-acetyl-B-D-glucosaminidase(GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPM_X N-acetyl-B-D-glucoasminidase (GCNA) from Stretococcus gordonii [Streptococcus gordonii],2EPN_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPN_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii]
5A6B_D	2.47e-132	1	515	100	619	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5A6B_A	7.98e-131	1	515	100	620	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5A69_A	7.98e-131	1	515	100	620	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-PUGNAc [Streptococcus pneumoniae TIGR4],5A6A_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6A_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6J_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_D GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6K_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5A6K_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5AC5_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4],5AC5_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4]
5AC4_A	2.24e-130	1	515	100	620	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4],5AC4_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P43077	1.37e-09	6	225	165	388	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
A6QNR0	6.95e-07	37	262	28	246	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q3U4H6	9.91e-07	1	292	1	298	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
B2UP57	1.75e-06	11	147	115	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

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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001876_01626.