CAZyme Information: MGYG000004402_01357

Basic Information

• Species: RC9 sp000432515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp000432515
• CAZyme ID: MGYG000004402_01357
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2018	MGYG000004402_18|CGC2	228481.18	5.6776

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004402	3046184	MAG	Israel	Asia

• Gene Location: Start: 47925; End: 53981 Strand: +

Full Sequence      

MKRSVFTVFLFVFLSIFSQAKDVQGQWIAPAEISSPNVWMAFRKDVNLGKAPSQAVASIA
VDSKYWLWINGDIVIREGGLKRGPDPHNTYYDEVDLSGYLKQGKNEIAILVWYFGKEGFS
HKSSGKAGLLFEMSASGKRIVSDGTWWCRIHPAYGNTEAPHPNFRLPESNIRFDARSDIK
GWQTVDSPETMGFHKAVTVAKKGEAPYNELVLRPIPQWKDFGVKDIDKTEIKVGEQADTI
AAYFPYNLQMTPVLDITDTVGGNLVSIYTDNTYAAGDINLRAEYITAPGQQTYESKGWLN
GHILYIVAPKGVTVNKISYRETGYATCLTGSFSCSDDFINRYWQKSLRTLYVNMRDTFFD
CPERERAQWWGDETLLMGECFYTTDMATRALMKKGMHELIAWQRADSSLFSPIPAGNYSE
ELPGQMLASIGWYGFWNYYMNTGDKQTIADVYPGVRKYLGIWTLDSTGLTNFRSGGWTWG
DWGDNKDVRLIFAGWHYLALKAAHQMALLLGQEADAEEYAATMARVKDAYNKCWNGKEYR
HPDYKDCTDDRVQALAVISGIADEDKYPQILDVLKHCFHASPYMEKYVTEALFMMGEGNY
AIRRMKERYAPMVNHPFYTTLFEGWDIGEKGFGGGTVNHAWSGGELITIAQYVCGITPQT
PGWKTFNIKPNCNILKHTDITVPTSFGNIHSSVISESDRVLMDVTVPEGTTANVTVPGEG
RSLVYINDVPQPKADFYTLTSGTYRIEKIFEPEFAIGNGEFILNGRPFIVKAAELHYPRI
PREYWEHRIRMCKALGMNTICMYVFWNYHEQKEGEFSFEGNADIAEFCRLAQKHGMYVIV
RPGPYVCAEWEMGGLPWWLLKKKDVKLRTLDPYYMDHVRLFLNRVGKELAPLQISEGGNI
IMVQVENEYGAYGTDKQYITQVKNTLLESGFTGVPLFQCDWNTNFTNNGLDDLLWTMNFG
TGADIRKQFARLKQLRPDTPLMCSEFWSGWFDHWGRKHETRPAGVMVDGIRDMLEDKISF
SLYMTHGGTTFGHWGGANNPPFSAMCSSYDYDAPISESGRATEKYMLLRNLLSKYSDSSS
MPQIPDPLPVIGIPEFRFREVSPLFDNLPRAKKSREIRPMEEFDQGWGTILYRTKVNEDI
PSGATLAITELHDWGQIYIDGKLIARLDRRKGEFTAELPAVSKGSRLDILVEAMGRVNFD
KSIHDRKGITEKVEIISGSQAVSLHDWKVYNFPVDYEFTSSRKFREAKGQCTAPAYWKAE
FEVDKTGDTFLDMRSWGKGLVWVNGHEIGRFWQIGPQQTLFVPGCWLREGKNEIYVLDLL
GCKEPVIKGLETPILDDLRSGDIKAGAKKVIDLKSETAVHEGSFAHEGGWQEVRFDKPAE
GRYFCLEMLSLQNEGEKAAIAELDILGSDGKPVSRENWKISFVDSEDSEDGNHSGEKVFD
LQESTFWSAAAGEKCPHQLVIEMESNIPVTGFRYLPRAESGCPGMIKDYKVYLRQYDFTY
VVADETAVNEGLAILPYPQKVDVTGGNLILSSGRLSIGAVPQFKNEVGLFIDQVAADKGI
DLKKTGVKKAAIRILKDDSLQNEEAYALSVSEDGVVVRSRGAAGAFYALQTLSQIMTANG
DGVSIPECNIEDAPQLGWRSFMLDEGRSFKGMAVVKQLLDDMARLKMNVFHWHLTDDQGW
RIEIRKYPLLTEVGARRDSTQVGWYEYNTYDGKPHEGFYTQAQIKEIIEYAAARHITVVP
EIEMPGHSAAAVAAYPWLSAAGKQIRVPCKFGVQYNVFNPADERVLGFLEDVLDEVMELF
PSKVIHIGGDEVRYDEWKNSRQVMGFIAENNLGSPAGLQVWFTNKIASYIESKGRRMMGW
NDITGDQLHHFQNEEAETTVGLSPDAVVQFWSGKPELMLKSARHGNDIVNSFNEYTYLDY
STEYDPVQATYNWKPISLEKAYSFSPVPDNFPKELKCKVIGAGCQMWGEWIPTVEKMNRQ
VYPRIAAYAEAFWSAPSQKDFSRFQRSLLPFLTRWSSR

Enzyme Prediction     

No EC number prediction in MGYG000004402_01357.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH35	761	1072	9.6e-116	0.990228013029316
GH20	1636	1995	6.8e-108	0.9584569732937686
GH78	278	715	3.3e-84	0.8888888888888888
CBM67	26	189	3.3e-32	0.8920454545454546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	2.88e-165	1637	2008	2	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	7.60e-149	760	1073	1	316	Glycosyl hydrolases family 35.
pfam00728	Glyco_hydro_20	1.05e-118	1637	1995	2	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	9.44e-100	1579	2000	201	620	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06570	GH20_chitobiase-like_1	1.60e-80	1638	2000	3	303	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
ANU56223.1	0.0	753	1500	28	778
QQR18938.1	0.0	753	1500	28	778
QRM98976.1	0.0	753	1500	28	778
ALJ48378.1	0.0	753	1500	28	778
QRQ55220.1	0.0	753	1500	28	778

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EON_A	0.0	751	1498	25	777	GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482]
3D3A_A	6.83e-274	751	1348	5	602	Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
4MAD_A	6.31e-138	761	1335	24	593	ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans]
4E8C_A	2.27e-112	760	1343	9	595	Crystalstructure of streptococcal beta-galactosidase in complex with galactose [Streptococcus pneumoniae TIGR4],4E8C_B Crystal structure of streptococcal beta-galactosidase in complex with galactose [Streptococcus pneumoniae TIGR4],4E8D_A Crystal structure of streptococcal beta-galactosidase [Streptococcus pneumoniae TIGR4],4E8D_B Crystal structure of streptococcal beta-galactosidase [Streptococcus pneumoniae TIGR4]
3WF3_A	9.35e-108	740	1319	23	622	Crystalstructure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_B Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_C Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_D Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF4_A Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_B Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_C Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_D Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48982	6.94e-116	752	1302	28	573	Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1
P16278	1.25e-106	747	1319	29	621	Beta-galactosidase OS=Homo sapiens OX=9606 GN=GLB1 PE=1 SV=2
Q60HF6	6.59e-106	753	1319	33	621	Beta-galactosidase OS=Macaca fascicularis OX=9541 GN=GLB1 PE=2 SV=1
Q95LV1	6.58e-105	761	1336	39	625	Beta-galactosidase-1-like protein OS=Macaca fascicularis OX=9541 GN=GLB1L PE=2 SV=1
Q5R7P4	6.65e-105	747	1319	29	621	Beta-galactosidase OS=Pongo abelii OX=9601 GN=GLB1 PE=2 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
0.000270	0.999033	0.000182	0.000182	0.000162	0.000145

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004402_01357.