CAZyme Information: MGYG000003145_01527

Basic Information

• Species: UMGS822 sp900545825
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; UMGS822; UMGS822 sp900545825
• CAZyme ID: MGYG000003145_01527
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2533	MGYG000003145_13|CGC1	271503.83	5.8703

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003145	2320952	MAG	United States	North America

• Gene Location: Start: 30146; End: 37747 Strand: +

Full Sequence      

MTRKCSALFALISAIALVITGLCHAAPQAQAAPSADTDSGKNVALAANGAKVTASGVESG
TNTTPDAVIDGNPDTRWSSDYNDNAWLRVELKDATQIDHVKIRWEAACAPSYKIQVSNDD
KDWKDATDVRALAECGQTETIKLNSSVANQKWKYVKLQALERKPINGVKYGVSLFEFEVW
DGAEPTPAKVPNLVPLPKSVKDQSKDGTVVFSLTSESKIVATGDATAPANILAAELRAAT
GYDLPVVDKASGANNITFTKGAVTGEAGAEAYMLKTAADGATLTANSAHGFFNATRTLLQ
LLPIQASSKIQVAGPWDAPATEILDSPRYEYRSVMIDPARSFLTVAEVKSIIDQISNLKM
SYLHIHLADDQGWRIQITNDGRVDGDDIDYNLLTEVSGKTAMNVHERQGSHQVGYSGFYT
QADYKDIVKYAKSRYVTVVPEIDVPGHVNAALHAIPQLNTAGSSHNGGGKTTAPANGTGN
VGYSYLDPDSQATWHFIGHVFKQLSEMTPGARVHIGGDEPHSFTGRYGEAKYNEVLTKVL
KIVRDDCKKTPVGWNEIAATELKENDGIQYWAGGTDKLVSAAKNKHAKIVMSRGSSAYLD
QKYNSKTPLGLTWAGCGTGGCSVQNYYNWNPTTDVVSGLSESDVLGPEMALWSETIRGGS
EAEFMIWPRMAAGAEIGWTPQNARSFEGFSKRLASVGDRWTLQGQNFYDTDQVNWDYALA
APVKTTGATGKDVAYPLGRLVAPGTVLNDTSSVSPDTKDDADGVSKSQIPANTKVMVNWG
DGTPATEATIQTDRERSAYNAPHPYYLTANHKYATDGDHTVTLTAGERTATTVIHTEGGA
ADPAVFTPWNPDATAPSAKVNPTEFSIKDRIEVQASGFKPYSLITMKVGDVELGQLRADS
QGNVAPQWVFVDPEVLPGPQKMTFTSGTRVATVDVVVKNGKIVLKNPLKHDQLSVVDVDS
QETVGEKAPATNAIDGDKTTFWHTQWQGTQKPFPHYITLALPADQTCTVTGFEYTPRQDN
SNTRAKDYSIQVSNDNENWTTVHEGSLEEGAATQAVNFDQEHQLQAKYVKMVQKNSQNGD
NFGGAAEIRVGAICKTADEPSTGGDDDDAQCDAQKTATTSYPTSTVVFPGNDKKSHKVTY
DKNSFMVDGKRLTVWSGELHYWRLPDPNGWRDVLQKMRADGFNAVSLYFDWGVHQAEKDG
KFEFTKDTYRDLDQLLTIAQQEGLYVIARPGPYVNAETSMGGLPAYMTNEAANLRSTNPE
VLKASKAWLHAFNEVAAKHQVTDGGGSILLYQVENEMPNSDDAHQAFMKALVKQVKDDGI
TVPLFHNDWGLNGIFKDAKGAGLDLYAYDKYPMGFNCAAGRGQVPDTENTFRGIAPNTPH
FIAESQGGAFTPWGANFQPAKCREYTDANFIRQWGAATIGNGVTAHNYYMEYGGTNWGWT
GAPASGFTSYDYGAPLTEDRTITPKFGVQKELGYFFAGVPAFASMNPIAAPTPKVESGAS
LNVKARLAGDTEGSATGNGTRVLAIRHSDSNDTSTTKFTLPLALGKSGTLQTKEFSTDDT
DSAITYNGSWKAVNDQTAWKSTLHRSTTSGDKATFTFDGTEVSLIVGTGTKNGTFTVSLD
NGTPETITKGMVDTDQNKPSQVVAYKKTGLAKGKHTLVVTNTGTDGKTTLDIDAFDAVDG
ADSGAKVVNDNDRSFFTYSNAWTHDTNWWAAGDIEKDETSTDKKGETAEFTFTGVGFDLI
GPFSENHGSATVTVDGKDVGKTKEEVTSSAQAQKVLFSWRDESGQAKKHTVKITVDGEAF
SGSKGTFVAIDAVRYYPTADALPSDGSPKPGEIGWKQIPQQEGTSLTLHGRDALLITADT
VIDGKQLYYTTSQIFGQPLPVNGHTTQYLVGYAGDAGETVFHFEKEPQVTLPEGATKVWD
EKTGQLRLNYTHKATPQEITITEGGKALTLRIITRDLAQTTWIIQGANGSQQTQVAVEGV
ELARTATFDGGKLALTGSNSKAADITVLVPTGVKAVTWNGTELKVADGVATGKEAAPNTV
KPITLQFVKHTDNAYAAKAFDDSKWKTASDTTAANPKQQGPQGNQKVVLDSNHYGFYEGS
VWYRAHYKATSDQAITLNGNGGSDDNHNGPAFMQVWANGHYVGAYPANGTDQQVTLPEGA
VQAGKDVVLAVLVNNIGQNLDWSDNGLSKQNRGLKGATIASDGDVTWKIEGATTADAAKH
NPSGSIYNNGGLAGEKAGWHMPGFDDKSWEKAETLHSAAGVTWYRSTFDLNVTAGKDVAF
HLDLESERAPKGDKAQATIFVNGWNTGVYIGDAGPQTSFTVPKAFLHLNGKNTVAIAIAA
KSDTMGPEAVTLRAVHTTTLPKVACPETPKPDDPNKPVNPDNPTAKTALTVTPDVVKAGE
ATTLKATGFTPDKLVVFTVNGVKVGEAKADGNGQATVKYTVPASSALGKFAVVASQPDTG
LSATSSLTVVASDQAKVQPNPKHDGKATDGKAKTGPSHGKLARTGVALRGVLVAMLLSAA
AGFALTRRRRRDA

Enzyme Prediction     

No EC number prediction in MGYG000003145_01527.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH35	1145	1472	1.8e-86	0.9869706840390879
GH20	325	681	5.3e-85	0.973293768545994
CBM32	54	178	9.6e-22	0.9274193548387096
CBM32	963	1088	1.3e-20	0.8870967741935484

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06568	GH20_SpHex_like	2.71e-127	329	693	1	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.
cd06563	GH20_chitobiase-like	2.33e-90	329	693	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.
pfam01301	Glyco_hydro_35	1.63e-83	1144	1473	1	315	Glycosyl hydrolases family 35.
pfam00728	Glyco_hydro_20	3.57e-82	329	680	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	7.20e-59	331	678	1	302	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
VEG55570.1	0.0	1117	2371	58	1341
QQM67568.1	0.0	1117	2371	57	1341
QWW19060.1	0.0	1113	2531	31	1492
AOZ72117.1	0.0	1122	2473	54	1414
QQO77161.1	0.0	3	1100	9	1119

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4C7D_A	2.43e-88	183	715	1	493	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
4C7G_A	6.10e-88	183	715	1	493	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
6YXZ_JJJ	5.63e-87	28	770	6	772	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
6Z14_JJJ	1.36e-86	28	770	6	772	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
1HP4_A	5.44e-86	185	715	21	511	ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7WUL4	1.04e-72	190	722	1	492	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
B8N2I5	1.27e-64	1134	1475	28	376	Probable beta-galactosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=lacC PE=3 SV=1
Q2UMD5	1.27e-64	1134	1475	28	376	Probable beta-galactosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=lacC PE=3 SV=1
A1D1Z9	2.12e-64	1138	1546	46	453	Probable beta-galactosidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=lacA PE=3 SV=1
Q4WS33	2.12e-64	1138	1546	46	453	Probable beta-galactosidase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=lacA 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
0.000509	0.974992	0.023746	0.000304	0.000218	0.000181

TMHMM  Annotations     

start	end
7	29
2506	2525